Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 act differently toward soluble and insoluble xylans

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• 作者：M.P. van Gool^a ; G.C.J. van Muiswinkel^b ; S.W.A. Hinz^b ; H.A. Schols^a ; ^{henk.schols@wur.nl} ; A.P. Sinitsyn^c ; H. Gruppen^a
• 关键词：GH ; glycoside hydrolase ; C1 ; Myceliophthora thermophila C1 ; LC strain ; specially designed C1-expression host ; CBM ; carbohydrate binding module ; CV ; column volumes ; SDS-PAGE ; sodium dodecyl sulfate polyacrylamide gel electrophoresis ; PAHBAH ; p-hydroxy benz
• 刊名：Enzyme and Microbial Technology
• 出版年：2013
• 出版时间：10 June, 2013
• 年：2013
• 卷：53
• 期：1
• 页码：25-32
• 全文大小：1145 K

文摘

Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 (C1), Xyl7 and Xyl8, were purified and the influence of solubility and molecular structure of various xylans on their efficiency was investigated. Both endo-xylanases were hindered by a high degree of substitution of a xylan. The two GH11 xylanases released different products from the xylans, in which Xyl7 displayed a degradation product composition closer to GH10 xylanases. A correlation of the degradation product composition with a specific residue at position 163 in the amino acid sequence of Xyl8 is suggested: tyrosine in Xyl8; valine in Xyl7. This is confirmed with examples of various endo-xylanases reported in literature.

The C1 GH11 xylanases were more efficient on self-associated xylan compared to C1 GH10 endo-xylanases and they released more small xylooligomers from these xylans. This is contrary to the general assumption that GH10 xylanases degrade xylans to a higher degree than GH11 xylanases.