Author: claimsbot

1. A method for making a cardboard pack of the box type, of a variable volume adapted in each case to the height of the packed products, the method involving cutting the box along its vertical edges, beginning at its top and continuing for part of its height; forming fold lines at a suitable height around the sides of the box to define top flaps; and then folding these flaps onto the contents of the prefilled box; in which at least one inflated or inflatable void-filling bag is inserted into the box, around andor above the packed products, after the fold lines defining the top flaps have been formed, and before these flaps are folded onto the contents of the box.
2. The method as claimed in claim 1, in which, after the box has been filled, the height of the packed products and the unoccupied volume around and above these products are detected automatically, and the result of this detection is used to determine, in a combined manner, the height to which the corners of the box are to be cut, the position of the fold lines on the sides of the box, and the volume or quantity of inflated or inflatable bags to be inserted in order to prevent the products moving about inside the box.
3. The method as claimed in claim 1, in which the volume of the void-filling bag deposited in the box is such that the top of the bag coincides approximately with the height marked on the sides for the purpose of their folding, while nonetheless allowing an initially slightly greater height to the top of the bag, so that when the box is closed the bag is slightly compressed and holds the packed products securely in position.
4. The method as claimed in claim 1, in which the or each void-filling bag is inserted into the box in the uninflated state, and this bag is inflated inside the box.
5. The method as claimed in claim 4, in which the void-filling bag has a variable length that is a function of the difference in height between the top of the box and the tallest product, bag inflation being done at a constant level above the box.
6. The method as claimed in claim 4, in which the void-filling bag has a constant length adapted to the dimensions of the box, bag inflation being done at a variable level inside the box.
7. The method as claimed in claim 1, in which the or each void-filling bag is inflated before being inserted into the box, the degree of inflation of the void-filling bag andor the number of void-filling bags introduced being determined for each box as a function of the calculation of the volume to be filled.
8. The method as claimed in claim 1, in which each void-filling bag is first inflated to a predefined maximum degree of inflation independently of the volume to be filled, inserted into the box, partially deflated, and finally sealed, so as to adapt to the volume to be filled in each case.
9. The method as claimed in claim 8, in which each void-filling bag, pre-inflated to the maximum extent is pierced once inside the box, to evacuate the excess air, after which the void-filling bag is sealed in order definitively to enclose the quantity of air held in this bag.
10. A combined machine for carrying out the method as claimed in claim 1, in which the prefilled boxes advance along a conveyor, the machine comprising the following items encountered successively along the conveyor: a station for detecting the height of the products in each box, a station for cutting the boxes along their vertical edges to a certain height, a station for marking the sides of the boxes to form the fold lines, a station for folding the flaps down onto the contents of the box, and a station for placing the closing lids on top of the boxes, which machine also comprises, between the side marking station and the flap folding station, a station for preparing inflated or inflatable void-filling bags and inserting them into the boxes.
11. The combined machine as claimed in claim 10, characterized in that the void-filling bag preparing and inserting station comprises means for unwinding a continuous film or sheath material, in which the void-filling bags are formed and separated by sealing and cutting them, means for inflating and closing each bag, and means for placing each bag in a box.
12. The combined machine as claimed in claim 11, in which the placing means comprise a rigid plate designed to be lowered into each box, approximately level with the fold lines formed in each case, so that the bags are inflated to a volume corresponding to the volume to be filled and in which the flaps will be once folded.
13. The combined machine as claimed in claim 11, in which the void-filling bag inflating means and the means for closing the void-filling bags, notably by sealing them, are maintained at a constant height above the tops of the boxes.
14. The combined machine as claimed in claim 11, in which the void-filling bag inflating means and the means for closing the inflated void-filling bags are situated at a variable height and can be introduced into the boxes, which means may be connected to the bag placing means.
The claims below are in addition to those above.
All refrences to claim(s) which appear below refer to the numbering after this setence.

1-22. (canceled)
23. A method of degrading or modifying a plant cell wall which method comprises contacting said plant cell wall with a polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
24. A method according to claim 23 wherein said polypeptide is derived from a family 11 xylanase.
25. A method according to claim 23 wherein said amino acid modification is of one or more surface amino acid residues.
26. A method according to claim 23 wherein said amino acid modification is of one or more solvent accessible residues.
27. A method according to claim 23 wherein there are at least two of said amino acid modifications.
28. A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,

of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or itstheir equivalent positions in other homologous xylanase polypeptides.
29. A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
30. A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
31. A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
32. A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
33. A method according to claim 23 wherein the inhibitor is an inhibitor found naturally in plant tissues.
34. A method according to claim 23 wherein the sensitivity to the inhibitor is reduced.
35. A method of processing a plant material which method comprises contacting said plant material with a polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
36. A method according to claim 35 wherein said polypeptide is derived from a family 11 xylanase.
37. A method according to claim 35 wherein said amino acid modification is of one or more surface amino acid residues.
38. A method according to claim 35 wherein said amino acid modification is of one or more solvent accessible residues.
39. A method according to claim 35 wherein there are at least two of said amino acid modifications.
40. A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,

of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or itstheir equivalent positions in other homologous xylanase polypeptides.
41. A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
42. A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
43. A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
44. A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
45. A method according to claim 35 wherein the inhibitor is an inhibitor found naturally in plant tissues.
46. A method according to claim 35 wherein the sensitivity to the inhibitor is reduced.
47. A method of baking or processing cereals or starch production or processing wood or enhancing the bleaching of wood pulp which method comprises the use of a polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
48. A method according to claim 47 wherein said polypeptide is derived from a family 11 xylanase.
49. A method according to claim 47 wherein said amino acid modification is of one or more surface amino acid residues.
50. A method according to claim 47 wherein said amino acid modification is of one or more solvent accessible residues.
51. A method according to claim 47 wherein there are at least two of said amino acid modifications.
52. A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,

of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or itstheir equivalent positions in other homologous xylanase polypeptides.
53. A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
54. A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
55. A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
56. A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
57. A method according to claim 47 wherein the inhibitor is an inhibitor found naturally in plant tissues.
58. A method according to claim 47 wherein the sensitivity to the inhibitor is reduced.
59. A nucleotide sequence encoding a variant polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
60. A nucleotide sequence according to claim 59 wherein said polypeptide is derived from a family 11 xylanase.
61. A nucleotide sequence according to claim 59 wherein said amino acid modification is of one or more surface amino acid residues.
62. A nucleotide sequence according to claim 59 wherein said amino acid modification is of one or more solvent accessible residues.
63. A nucleotide sequence according to claim 59 wherein there are at least two of said amino acid modifications.
64. A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,

of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or itstheir equivalent positions in other homologous xylanase polypeptides.
65. A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
66. A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
67. A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
68. A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
69. A nucleotide sequence according to claim 59 wherein the inhibitor is an inhibitor found naturally in plant tissues.
70. A nucleotide sequence according to claim 59 wherein the sensitivity to the inhibitor is reduced.
71. A method according to claim 23 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
72. A method according to claim 23 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
73. A method according to claim 23 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
74. A method according to claim 23 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
75. A method according to claim 35 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
76. A method according to claim 35 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
77. A method according to claim 35 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
78. A method according to claim 35 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
79. A method according to claim 47 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
80. A method according to claim 47 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
81. A method according to claim 47 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
82. A method according to claim 47 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
83. A nucleotide sequence according to claim 59 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
84. A nucleotide sequence according to claim 59 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
85. A nucleotide sequence according to claim 59 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
86. A nucleotide sequence according to claim 59 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
87. A method according to claim 23 wherein said polypeptide is derivable from SEQ ID NO: 9.
88. A method according to claim 35 wherein said polypeptide is derivable from SEQ ID NO: 9.
89. A method according to claim 47 wherein said polypeptide is derivable from SEQ ID NO: 9.
90. A nucleotide sequence according to claim 59 wherein said polypeptide is derivable from SEQ ID NO: 9.
91. An isolated variant polypeptide or fragment thereof having at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package, and having xylanase activity, comprising two or more amino acid modifications, wherein said amino acid modifications are at two or more of positions 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ ID NO: 1, or their equivalent positions in other family 11 xylanases, such that the polypeptide or fragment thereof has altered sensitivity to a xylanase inhibitor as compared with the parent xylanase, wherein one of said modifications is at position 11, wherein the variant polypeptide is a family 11 xylanase.
92. An isolated variant polypeptide or fragment thereof having at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package, and having xylanase activity, comprising two or more amino acid modifications, wherein said amino acid modifications are at two or more of positions 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ ID NO: 1, or their equivalent positions in other family 11 xylanases, such that the polypeptide or fragment thereof has altered sensitivity to a xylanase inhibitor as compared with the parent xylanase, wherein one of said modifications is at position 11, wherein the variant polypeptide is a family 11 xylanase.
93. An isolated variant polypeptide or fragment thereof having at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package, and having xylanase activity, comprising two or more amino acid modifications, wherein said amino acid modifications are at two or more of positions 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ ID NO: 1, or their equivalent positions in other family 11 xylanases, such that the polypeptide or fragment thereof has altered sensitivity to a xylanase inhibitor as compared with the parent xylanase, wherein one of said modifications is at position 11, wherein the variant polypeptide is a family 11 xylanase.
94. A variant xylanase polypeptide, or fragment thereof having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
95. A variant xylanase polypeptide, or fragment thereof having at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
96. A variant xylanase polypeptide, or fragment thereof having at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues;
wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
97. A variant xylanase polypeptide, or fragment thereof having at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues;
wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
98. A variant xylanase polypeptide, or fragment thereof having at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
99. A method according to claim 23 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
100. A method according to claim 35 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
101. A method according to claim 47 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
102. A nucleotide sequence according to claim 59 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
103. A variant xylanase polypeptide, or fragment thereof having at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues;
wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
104. A variant xylanase polypeptide, or fragment thereof having at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
105. A variant xylanase polypeptide, or fragment thereof having at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
106. A variant xylanase polypeptide, or fragment thereof having at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
107. A variant xylanase polypeptide, or fragment thereof having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn

1. A flow control device for use with a pulse detonation chamber, said device comprising:
an inlet coupled in flow communication with a source of compressed air, said inlet extending at least partially into the chamber to facilitate controlling air flow into the chamber; and
a body portion extending downstream from and circumferentially around said inlet, said body portion positioned in flow communication with said inlet.
2. A device in accordance with claim 1 wherein said inlet is coupled within the chamber such that a pre-determined circumferential gap is defined between said inlet and said body portion for fixedly controlling air flow into the chamber.
3. A device in accordance with claim 2 wherein said inlet portion comprises a converging nozzle coupled to a chamber inlet portion, said nozzle includes an outlet formed for fixedly controlling air flow into the chamber.
4. A device in accordance with claim 1 wherein said inlet is variably adjustable within the chamber to facilitate changing a circumferential gap defined between said inlet and said body portion.
5. A device in accordance with claim 1 wherein said body portion comprises a substantially convergent diameter for at least a portion thereof.
6. A device in accordance with claim 1 wherein said body portion comprises a first portion comprising a substantially convergent diameter and a second portion comprising a substantially divergent diameter.
7. A device in accordance with claim 1 wherein said body portion comprises a first portion comprising a substantially convergent diameter and a second portion comprising a partially divergent diameter.
8. A pulse detonation engine comprising:
a compressor configured to compress air therein;
a pulse detonation combustor coupled to an axial turbine including at least one pulse detonation chamber comprising an inlet portion, an outlet portion, and a body portion extending therebetween, said inlet portion coupled in flow communication with said compressor for receiving compressed air therethrough, said chamber comprising:
a fuel injector for supplying fuel to said chamber;
a detonation device coupled to said chamber for initiating a detonation wave within said chamber; and
a flow control device comprising an inlet for controlling air flow into said at least one pulse detonation chamber and a body portion coupled in flow communication with said inlet.
9. An engine in accordance with claim 8 wherein said air inlet portion is fixedly secured within said chamber such that a pre-determined gap is defined circumferentially between said air inlet portion and said body portion, said gap facilitates controlling air flow into said chamber.
10. An engine in accordance with claim 9 wherein said inlet comprises a converging nozzle coupled to said chamber inlet portion and comprising a port formed for fixedly controlling air flow into said chamber.
11. An engine in accordance with claim 8 wherein said inlet portion is adjustably coupled within said chamber such that said circumferential gap is variable to facilitate selectively controlling air flow into said chamber.
12. An engine in accordance with claim 8 wherein said body portion comprises a substantially convergent diameter for at least a portion thereof.
13. An engine in accordance with claim 8 wherein said body portion comprises a first portion comprising a substantially convergent diameter and a second portion comprising a substantially divergent diameter.
14. An engine in accordance with claim 8 wherein said body portion comprises a first portion comprising a substantially convergent diameter and a second portion comprising a partially divergent diameter.
15. A method for adjusting air flow through a pulse detonation combustor, said method comprising:
providing at least one pulse detonation chamber including an inlet portion, an outlet portion, and a body portion extending therebetween;
coupling an inlet within the chamber inlet portion and in flow communication with a source of compressed air for controlling air flow into the at least one pulse detonation chamber; and
coupling a body portion downstream from and circumferentially around the chamber inlet portion and in flow communication with the inlet.
16. A method in accordance with claim 15 wherein coupling an inlet within the chamber inlet portion further comprises coupling the inlet within the chamber such that a pre-determined circumferential gap is defined between the inlet and the body portion to facilitate controlling air flow into the chamber.
17. A method in accordance with claim 15 wherein coupling an inlet within the chamber inlet portion further comprises variably coupling the inlet within the chamber to facilitate changing a circumferential gap defined between the inlet and the body portion.
18. A method in accordance with claim 15 wherein coupling a body portion downstream from and circumferentially around the chamber inlet portion further comprises coupling the body portion comprising a substantially convergent diameter for at least a portion thereof.
19. A method in accordance with claim 15 wherein coupling a body portion downstream from and circumferentially around the chamber inlet portion further comprises coupling the body portion comprising a first portion comprising a substantially convergent diameter and a second portion comprising a substantially divergent diameter.
20. A method in accordance with claim 15 wherein coupling a body portion downstream from and circumferentially around the chamber inlet portion further comprises coupling the body portion comprising a first portion comprising a substantially convergent diameter and a second portion comprising a partially divergent diameter.
The claims below are in addition to those above.
All refrences to claim(s) which appear below refer to the numbering after this setence.

1. A drum brake apparatus comprising:
a first and a second brake shoes disposed in a drum to oppose each other; and
a cam mechanism for generating a braking force by opening the first and second brake shoes outward according to a shoe operating force generated by an operating force generator, and for controlling the braking force by utilizing a reaction force exerted from the brake shoes during a braking period,
wherein the cam mechanism includes:
a cam supporting plate, having a central circular aperture portion is continuous with two opposed circular aperture portions, loosely and rotatably fitted on an anchor pin projecting upright on a backing plate, and having an input power receiving portion for receiving the shoe operating force at a position radially inwardly of the drum with respect to the anchor pin;
a first cam plate, rotatably connected to the cam supporting plate at an outer cam supporting position which is located radially outwardly of the drum with respect to the anchor pin, and having a first shoe receiving arcuate portion which comes into abutment with an end of one of the brake shoes; and
a second cam plate, rotatably connected to the cam supporting plate at an inner cam supporting position along a point between the anchor pin and the input power receiving portion, and having a second shoe receiving arcuate portion which comes into abutment with the end of the other brake shoe.
2. The drum brake apparatus according to claim 1, wherein the first cam plate and the second cam plate respectively comprise an anchor abutting arcuate portion rotatably slidable against the outer periphery of the anchor pin, further comprising:
a damper spring for alleviating an impact applied when each anchor abutting arcuate portion comes into abutment with the outer periphery of the anchor pin when controlling a torque.
3. The drum brake apparatus according to claim 1, further comprising a strut, for opening one of the brake shoes by being displaced toward the one of the brake shoes when the operating force is fed from a parking lever, provided in a vacant space between the second cam plate and the input power receiving portion.
4. The drum brake apparatus according to claim 3, wherein the strut includes a guide groove extending in the direction of displacement caused by braking, and is supported by the cam supporting plate so as to be capable of moving along the direction of displacement caused by braking, by inserting a guide pin provided upright on the cam supporting plate into the guide groove.
5. The drum brake apparatus according to claim 3, further comprising a resilient member for maintaining abutment between the strut for the parking brake and the parking lever.
6. The drum brake apparatus according to claim 1, further comprising a resilient clip for retaining the first cam plate, the second cam plate, and the cam supporting plate in the assembled state.
7. The drum brake apparatus according to claim 1, wherein the input power receiving portion of the cam supporting plate includes a supporting shaft, which comes into abutment with the output end of the operating force generator, engaged and supported by a notch formed on the cam supporting plate.
8. The drum brake apparatus according to claim 1,
wherein the first cam plate is rotatably connected to the cam supporting plate by a first cam pin fitted to the cam supporting plate at the outer cam supporting position,
the second cam plate is rotatably connected to the cam supporting plate by a second cam pin fitted to the cam supporting plate at the inner cam supporting position,
each cam pin is provided with a positioning shaft passing through the cam supporting plate and projecting toward the root side of the anchor pin, and
the cam supporting plate loosely fitted to the anchor pin is located in the direction of the axis of the anchor pin by abutting the extremity of the positioning shaft of each cam pin against a flange projecting on the root side of the anchor pin.
9. The drum brake apparatus according to claim 8, wherein the extremity of the positioning shaft of the cam pin is formed into a substantially semi-spherical surface.
10. A drum brake apparatus comprising:
a first and a second brake shoes disposed in a drum to oppose each other; and
a cam mechanism for generating a braking force by opening the first and second brake shoes outward according to a shoe operating force generated by an operating force generator, and for controlling the braking force by utilizing a reaction force exerted from the brake shoes during a braking period,
wherein the cam mechanism includes:
a cam supporting plate, loosely and rotatably fitted on an anchor pin projecting upright on a backing plate, and having an input power receiving portion for receiving the shoe operating force at a position radially inwardly of the drum with respect to the anchor pin;
a first cam plate, rotatable connected to the cam supporting plate at an outer cam supporting position which is located radially outwardly of the drum with respect to the anchor pin, and having a first shoe receiving arcuate portion which comes into abutment with an end of one of the brake shoes; and
a second cam plate, rotatable connected to the cam supporting plate at an inner cam supporting position along a point between the anchor pin and the input power receiving portion, an having a second shoe receiving arcuate portion which comes into abutment with the end of the other brake shoe,
wherein, until a shoe clearance is eliminated, the cam supporting plate rotates about one of cam supporting positions of one of the cam plates which receives the brake power, to open the brake shoe being in abutment with the other of cam plates, and
after the shoe clearance is eliminated, the cam supporting plate rotates about the anchor pin to press the first and the second brake shoes against the drum.
11. A drum brake apparatus comprising:
a first and a second brake shoes disposed in a drum to oppose each other; and
a cam mechanism for generating a braking force by opening the first and second brake shoes outward according to a shoe operating force generated by an operating force generator, and for controlling the braking force by utilizing a reaction force exerted from the brake shoes during a braking period,
wherein the cam mechanism includes:
a cam supporting plate, loosely and rotatable fitted on an anchor pin projecting upright on a backing plate, and having an input power receiving portion for receiving the shoe operating force at a position radially inwardly of the drum with respect to the anchor pin;
a first cam plate, rotatable connected to the cam supporting plate at an outer cam supporting position which is located radially outwardly of the drum with respect to the anchor pin, and having a first shoe receiving arcuate portion which comes into abutment with an end of one of the brake shoes; and
a second cam plate, rotatably connected to the cam supporting plate at an inner cam supporting position along a point between the anchor pin and the input power receiving portion, and having a second shoe receiving arcuate portion which comes into abutment with the end of the other brake shoe, wherein the drum brake apparatus, further comprising a swinging movement limiter,
wherein distances L1 and L2 are set to L1\u2260L2, where L1 is a distance between the center of curvature of the first shoe receiving arcuate portion and the center of the anchor pin and L2 is a distance between the center of curvature of the second shoe receiving arcuate portion and the center of the anchor pin, and
wherein the swinging movement limiter limits the range of swinging movement of the respective cam plates, so that only one of the cam plates being smaller in distance between the center of the anchor pin and the center of curvature of the shoe receiving arcuate portion swings integrally with the cam supporting plate, and opens the brake shoes outward until the shoe clearance is eliminated.