کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
6451165 1361329 2017 13 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Research review paperGH62 arabinofuranosidases: Structure, function and applications
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Research review paperGH62 arabinofuranosidases: Structure, function and applications
چکیده انگلیسی


- Plant cell wall deconstruction requires several α-l-arabinofuranosidases.
- GH62 α-l-arabinofuranosidases show significantly different substrate preference.
- GH62 α-l-arabinofuranosidases differ importantly in catalytic efficiency.
- GH62 α-l-arabinofuranosidases are abundant in fungal secretomes.
- GH62 α-l-arabinofuranosidases can act on recalcitrant biomass.

Motivated by industrial demands and ongoing scientific discoveries continuous efforts are made to identify and create improved biocatalysts dedicated to plant biomass conversion. α-1,2 and α-1,3 arabinofuranosyl specific α-l-arabinofuranosidases (EC 3.2.1.55) are debranching enzymes catalyzing hydrolytic release of α-l-arabinofuranosyl residues, which decorate xylan or arabinan backbones in lignocellulosic and pectin constituents of plant cell walls. The CAZy database classifies α-l-arabinofuranosidases in Glycoside Hydrolase (GH) families GH2, GH3, GH43, GH51, GH54 and GH62. Only GH62 contains exclusively α-l-arabinofuranosidases and these are of fungal and bacterial origin. Twenty-two GH62 enzymes out of 223 entries in the CAZy database have been characterized and very recently new knowledge was acquired with regard to crystal structures, substrate specificities, and phylogenetics, which overall provides novel insights into structure/function relationships of GH62. Overall GH62 α-l-arabinofuranosidases are believed to play important roles in nature by acting in synergy with several cell wall degrading enzymes and members of GH62 represent promising candidates for biotechnological improvements of biofuel production and in various biorefinery applications.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biotechnology Advances - Volume 35, Issue 6, 1 November 2017, Pages 792-804
نویسندگان
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