Journal ArticleDOI
GH11 xylanases: Structure/function/properties relationships and applications
TLDR
In this paper, the authors focus on the GH11 xylanase family, which is one of the best characterized families with bacterial and fungal members considered as true xylanases compared to the other families because of their high substrate specificity.About:
This article is published in Biotechnology Advances.The article was published on 2012-05-01. It has received 341 citations till now. The article focuses on the topics: Enzyme structure & CAZy.read more
Citations
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Journal ArticleDOI
An Arabidopsis Cell Wall Proteoglycan Consists of Pectin and Arabinoxylan Covalently Linked to an Arabinogalactan Protein
Li Tan,Stefan Eberhard,Sivakumar Pattathil,Clayton Warder,John Glushka,Chunhua Yuan,Zhangying Hao,Xiang Zhu,Utku Avci,Jeffrey S. Miller,David Baldwin,Charles Pham,Ron Orlando,Alan G. Darvill,Michael G. Hahn,Marcia J. Kieliszewski,Debra Mohnen +16 more
TL;DR: A cell wall proteoglycan with pectin and arabinoxylan covalently attached to an arabinogalactan protein is described, identifying a cross-linked matrix polysaccharide wall protein architecture with implications for wall structure, function, and synthesis.
Journal ArticleDOI
Microbial xylanases and their industrial application in pulp and paper biobleaching: a review.
TL;DR: This review has focused on the microbial enzyme complex involved in the complete breakdown of xylan and the studies on xylanase regulation and their potential industrial applications with special reference to pulp biobleaching, which is directly related to increasing pulp brightness and reduction in environmental pollution.
Book ChapterDOI
A Review of Xylanase Production by the Fermentation of Xylan: Classification, Characterization and Applications
TL;DR: The primary chain of xylan is composed of β-xylopyranose residues, and its complete hydrolysis requires the action of several enzymes, including endo-1,4-β-D-xylanase (EC3.2.8), which is crucial for xylan depolymerization.
Journal ArticleDOI
Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.
TL;DR: The ability of dietary xylooligosaccharides to function as prebiotics in humans is governed by their substitution patterns, and endoxylanases are excellent tools to tailor prebiotic oligosac charides to stimulate various types of intestinal bacteria and to cause fermentation in different parts of the gastrointestinal tract.
Journal ArticleDOI
Structural Considerations on the Use of Endo-Xylanases for the Production of prebiotic Xylooligosaccharides from Biomass.
TL;DR: Structural and functional aspects are discussed, focusing on the potential applications of endo-xylanases in the production of dif-ferently substituted (A)XOS as emerging prebiotics, as well as their implication in the processing of the raw materials.
References
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Journal ArticleDOI
The Protein Data Bank
Helen M. Berman,John D. Westbrook,Zukang Feng,Gary L. Gilliland,Talapady N. Bhat,Helge Weissig,Ilya N. Shindyalov,Philip E. Bourne +7 more
TL;DR: The goals of the PDB are described, the systems in place for data deposition and access, how to obtain further information and plans for the future development of the resource are described.
Journal ArticleDOI
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
Brandi L. Cantarel,Pedro M. Coutinho,Corinne Rancurel,Thomas Bernard,Vincent Lombard,Bernard Henrissat +5 more
TL;DR: The Carbohydrate-Active Enzyme (CAZy) database is a knowledge-based resource specialized in the enzymes that build and breakdown complex carbohydrates and glycoconjugates and has been used to improve the quality of functional predictions of a number genome projects by providing expert annotation.
Journal ArticleDOI
A classification of glycosyl hydrolases based on amino acid sequence similarities.
TL;DR: With the steady increase in sequence and structural data, it is suggested that the enzyme classification system should perhaps be revised.
Journal ArticleDOI
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
TL;DR: On the basis of a comparison of 482 sequences corresponding to 52 EC entries, 45 families, out of which 22 are polyspecific, can now be defined and has been implemented in the SWISS-PROT protein sequence data bank.