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

Paper ID Volume ID Publish Year Pages File Format Full-Text
17176 42649 2013 8 PDF Available
Title
Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 act differently toward soluble and insoluble xylans
Abstract

•Intrafamily differences are found for C1 GH11 endo-xylanases.•GH11 endo-xylanases are influenced by solubility and molecular structure of xylan.•Valine instead of tyrosine at position 163 causes GH10-like degradation products.•GH11 xylanases release many small degradation products from self-associated xylans.

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.

Keywords
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
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Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 act differently toward soluble and insoluble xylans
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 53, Issue 1, 10 June 2013, Pages 25–32
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us