Fungal β-Glycosidase Belonging to Subfamily 4 of Glycoside Hydrolase Family 30 with Transglycosylation Activity

2021 ◽  
Author(s):  
Ju-Hee Cha ◽  
Minsun Hong ◽  
Chang-Jun Cha
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Transglycosylation Activity ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

Xylanases of glycoside hydrolase family 30 – An overview

2021 ◽  
Vol 47 ◽  
pp. 107704
Author(s):  
Vladimír Puchart ◽  
Katarína Šuchová ◽  
Peter Biely
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

β-Glucuronidase from Lactobacillus brevis useful for baicalin hydrolysis belongs to glycoside hydrolase family 30

2013 ◽  
Vol 98 (9) ◽  
pp. 4021-4032 ◽  
Author(s):  
Haruko Sakurama ◽  
Shigenobu Kishino ◽  
Yoshie Uchibori ◽  
Yasunori Yonejima ◽  
Hisashi Ashida ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Lactobacillus Brevis ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

scholarly journals Glycoside Hydrolase family 30 harbors fungal subfamilies with distinct polysaccharide specificities

2021 ◽  
Author(s):  
Xinxin Li ◽  
Dimitrios Kouzounis ◽  
Mirjam A. Kabel ◽  
Ronald P. de Vries ◽  
Adiphol Dilokpimol
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

scholarly journals A plasmid borne, functionally novel glycoside hydrolase family 30 subfamily 8 endoxylanase from solventogenic Clostridium

2018 ◽  
Vol 475 (9) ◽  
pp. 1533-1551 ◽  
Author(s):  
Franz J. St John ◽  
Diane Dietrich ◽  
Casey Crooks ◽  
Peter Balogun ◽  
Vesna de Serrano ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Relative Rate ◽  
Salt Bridge ◽  
Crystallographic Structure ◽  
Glycoside Hydrolase Family ◽  
Significant Activity ◽  
Sequence Comparisons ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

Glycoside hydrolase family 30 subfamily 8 (GH30-8) β-1,4-endoxylanases are known for their appendage-dependent function requiring recognition of an α-1,2-linked glucuronic acid (GlcA) common to glucuronoxylans for hydrolysis. Structural studies have indicated that the GlcA moiety of glucuronoxylans is coordinated through six hydrogen bonds and a salt bridge. These GlcA-dependent endoxylanases do not have significant activity on xylans that do not bear GlcA substitutions such as unsubstituted linear xylooligosaccharides or cereal bran arabinoxylans. In the present study, we present the structural and biochemical characteristics of xylanase 30A from Clostridium acetobutylicum (CaXyn30A) which was originally selected for study due to predicted structural differences within the GlcA coordination loops. Amino acid sequence comparisons indicated that this Gram-positive-derived GH30-8 more closely resembles Gram-negative derived forms of these endoxylanases: a hypothesis borne out in the developed crystallographic structure model of the CaXyn30A catalytic domain (CaXyn30A-CD). CaXyn30A-CD hydrolyzes xylans to linear and substituted oligoxylosides showing the greatest rate with the highly arabinofuranose (Araf)-substituted cereal arabinoxylans. CaXyn30A-CD hydrolyzes xylooligosaccharides larger than xylotriose and shows an increased relative rate of hydrolysis for xylooligosaccharides containing α-1,2-linked arabinofuranose substitutions. Biochemical analysis confirms that CaXyn30A benefits from five xylose-binding subsites which extend from the −3 subsite to the +2 subsite of the binding cleft. These studies indicate that CaXyn30A is a GlcA-independent endoxylanase that may have evolved for the preferential recognition of α-1,2-Araf substitutions on xylan chains.

scholarly journals A New Subfamily of Glycoside Hydrolase Family 30 with Strict Xylobiohydrolase Function

2021 ◽  
Vol 8 ◽  
Author(s):  
Casey Crooks ◽  
Nathan J. Bechle ◽  
Franz J. St John
Keyword(s):  
Glycoside Hydrolase ◽  
Glucuronic Acid ◽  
Commercial Production ◽  
Glycoside Hydrolase Family ◽  
Biophysical Parameters ◽  
Reaction Conditions ◽  
Hydrolysis Products ◽  
Clostridium Clariflavum ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

The Acetivibrioclariflavus (basonym: Clostridium clariflavum) glycoside hydrolase family 30 cellulosomal protein encoded by the Clocl_1795 gene was highly represented during growth on cellulosic substrates. In this report, the recombinantly expressed protein has been characterized and shown to be a non-reducing terminal (NRT)-specific xylobiohydrolase (AcXbh30A). Biochemical function, optimal biophysical parameters, and phylogeny were investigated. The findings indicate that AcXbh30A strictly cleaves xylobiose from the NRT up until an α-1,2-linked glucuronic acid (GA)-decorated xylose if the number of xyloses is even or otherwise a single xylose will remain resulting in a penultimate GA-substituted xylose. Unlike recently reported xylobiohydrolases, AcXbh30A has no other detectable hydrolysis products under our optimized reaction conditions. Sequence analysis indicates that AcXbh30A represents a new GH30 subfamily. This new xylobiohydrolase may be useful for commercial production of industrial quantities of xylobiose.

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