Loading…

Cellobiose dehydrogenase from the agaricomycete Coprinellus aureogranulatus and its application for the synergistic conversion of rice straw

From the biotechnological viewpoint, the enzymatic disintegration of plant lignocellulosic biomass is a promising goal since it would deliver fermentable sugars for the chemical sector. Cellobiose dehydrogenase (CDH) is a vital component of the extracellular lignocellulose-degrading enzyme system of...

Full description

Saved in:
Bibliographic Details
Published in:Applied biological chemistry 2021, 64(5), , pp.1-11
Main Authors: Nghi, Do Huu, Kellner, Harald, Büttner, Enrico, Huong, Le Mai, Duy, Le Xuan, Giap, Vu Dinh, Quynh, Dang Thu, Hang, Tran Thi Nhu, Verberckmoes, An, Diels, Ludo, Liers, Christiane, Hofrichter, Martin
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:From the biotechnological viewpoint, the enzymatic disintegration of plant lignocellulosic biomass is a promising goal since it would deliver fermentable sugars for the chemical sector. Cellobiose dehydrogenase (CDH) is a vital component of the extracellular lignocellulose-degrading enzyme system of fungi and has a great potential to improve catalyst efficiency for biomass processing. In the present study, a CDH from a newly isolated strain of the agaricomycete Coprinellus aureogranulatus ( Cau CDH) was successfully purified with a specific activity of 28.9 U mg −1 . This pure enzyme (MW = 109 kDa, p I = 5.4) displayed the high oxidative activity towards β-1–4-linked oligosaccharides. Not least, Cau CDH was used for the enzymatic degradation of rice straw without chemical pretreatment. As main metabolites, glucose (up to 165.18 ± 3.19 mg g −1 ), xylose (64.21 ± 1.22 mg g −1 ), and gluconic acid (5.17 ± 0.13 mg g −1 ) could be identified during the synergistic conversion of this raw material with the fungal hydrolases (e.g., esterase, cellulase, and xylanase) and further optimization by using an RSM statistical approach.
ISSN:2468-0834
2468-0842
DOI:10.1186/s13765-021-00637-y