C - Chemistry – Metallurgy – 12 – N
Patent
C - Chemistry, Metallurgy
12
N
C12N 15/56 (2006.01) C12N 9/24 (2006.01) C12S 3/08 (2006.01) D21C 5/00 (2006.01) D21C 9/10 (2006.01)
Patent
CA 2210247
Producing a xylanase enzyme of superior performance in the bleaching of pulp. More specifically, a modified xylanase of Family 11 that shows improved thermophilicity, alkalophilicity, and thermostability as compared to the naturalxylanase. The modified xylanases contain any of three types of modifications: (1) changing amino acids 10, 27, and 29 of Trichoderma reesei xylanase II or the corresponding amino acids of another Family 11 xylanase, where these amino acidsare changed to histidine, methionine, and leucine, respectively; (2) substitution of amino acids in the N-terminal region with amino acids from another xylanase enzyme. In a preferred embodiment, substitution of the natural Bacillus circulans or Trichoderma reesei xylanase with a short sequence of amino acids from Thermomonospora fusca xylanase yielded chimeric xylanases with higher thermophilicity and alkalophilicity; (3) an extension upstream of the N-terminus of up to 10 amino acids. In a preferred embodiment, extension of the N-terminus of the xylanase with the tripeptide glycine-arginine-arginine improved its performance.
Production d'une enzyme xylanase, améliorant le rendement dans le blanchiment de la pâte. Plus précisément, une xylanase modifiée de la family 11, offrant de meilleures propriétés thermophiles, alcaliphiles et une thermostabilité améliorée, comparativement à la xylanase naturelle. Les xylanases modifiées comportent n'importe laquelle des trois modifications suivantes : 1) changement des amino- acides 10, 27 et 29 de la xylanase II de Trichoderma reesei ou les amino-acides correspondants d'une autre xylanase de la famille 11, ces amino-acides étant changés respectivement en histidine, méthionine et leucine; 2) substitution des amino-acides dans la région N-terminale avec des amino-acides provenant d'une autre xylanase. Dans une version privilégiée, la substitution de la xylanase naturelle de Bacillus circulans ou de Trichoderma reesei avec une courte séquence d'amino-acides provenant de la xylanase de Thermomonospora fusca a donné des xylanases chimériques plus thermophiles et plus alcaliphiles; 3) extension en amont du N terminal de 10 amino-acides ou moins. Dans une version privilégiée, l'extension du N terminal de la xylanase avec le tripeptide glycine-arginine-arginine a amélioré le rendement.
Ishikawa Kazuhiko
Sung Wing L.
Yaguchi Makoto
Gowling Lafleur Henderson Llp
National Research Council Of Canada
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