GH62 arabinofuranosidases: Structure, function and applications

Abstract

Motivated by industrial demands and ongoing scientific discoveries continuous efforts are made to identify and create improved biocatalysts dedicated to plant biomass conversion. --1,3 arabinofuranosyl specific -L-arabinofuranosidases (EC 3.2.1.55) are debranching enzymes catalyzing hydrolytic release -L-arabinofuranosyl residues, which decorate xylan or arabinan backbones in lignocellulosic and pectin constituents of plant cell walls. The CAZy database classifies -L-arabinofuranosidases in Glycoside Hydrolase (GH) families GH2, GH3, GH43, GH51, GH54 and GH62. Only GH62 contains exclusively -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 -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.3

A Glycoside Hydrolase Family 62 A-L-Arabinofuranosidase from Trichoderma Reesei and Its Applicable Potential during Mashing

“…In this paper, only one AFase, which belongs to GH62, has been purified and identified, which is consistent with previous results [18]. The family GH62 exclusively contains AFases secreted by fungi or bacteria [15]. Family GH62 AFase is often not identified in the culture filtrate of T. reesei.…”

“…AFase is a debranching enzyme. AFase catalyzes the hydrolysis of the arabinofuranosyl substituent from the arabinoxylan backbone, while β-D-xylosidase removes β-1,4-D-xylopyranosy moieties from the terminal end of arabinoxylo-oligosaccharides and plays a key role in the complete hydrolysis of arabinoxylan [15]. To our knowledge, there has been no investigation on the arabinoxylan degradation of barley malt by microbial AFases.…”

Screening of a Novel Glycoside Hydrolase Family 51 α-L-Arabinofuranosidase from Paenibacillus polymyxa KF-1: Cloning, Expression, and Characterization

“…α-L-arabinofuranosidase (Abf, EC. 3.2.1.55), which catalyzes the α-1,2-, α-1,3-, or α-1,5-linked L-arabinose or oligoarabinose side chains from the xylose backbone of hemicellulose [8], synergizes with other hemicelluloses to increase degradation efficiency. There has been growing interest in α-L-arabinofuranosidases due to their role in the degradation of hemicellulose, and their potential application in many biotechnological applications, such as the production of L-arabinose, improvement of wine flavors, clarification of fruit juices, and enhanced digestion of animal feedstuffs [8][9][10].…”

Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 Å resolution

“…CAZY family GH62 contains many enzymes that act as arabinoxylan-active arabinofuranosidases (extensively reviewed in Wilkens et al, 2017). The first three-dimensional structures of GH62 enzymes appeared in 2014, with structures reported from the bacteria Streptomyces coelicolor (Maehara et al, 2014) and S. thermoviolaceus (Wang et al, 2014) and of two fungal enzymes from Ustilago maydis and Podospora anserina (Siguier et al, 2014).…”