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Enzymatic production of sugar from fungi and fungi-infected lignocellulosic biomass by a new cellulosomal enzyme harboring N-acetyl-beta-D-glucosaminidase activity

Authors
Lee, Myeong-EunShin, Sang KyuOh, Jeong-JooHwang, Dong-HyeokKo, Young JinHyeon, Jeong EunHan, Sung Ok
Issue Date
Jan-2021
Publisher
ELSEVIER SCI LTD
Keywords
N-acetyl-beta-D-glucosaminidase; Chitin; Fungi degradation; Cellulosome; Clostridium cellulovorans
Citation
BIORESOURCE TECHNOLOGY, v.319
Indexed
SCIE
SCOPUS
Journal Title
BIORESOURCE TECHNOLOGY
Volume
319
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/50613
DOI
10.1016/j.biortech.2020.124242
ISSN
0960-8524
Abstract
Cellulosomes are scaffold proteins displaying enzymes on the cell wall to efficiently obtain nutrient sources. CcGlcNAcase is a novel cellulosomal component. Based on sequence analysis, CcGlcNAcase was predicted to be a chitinolytic enzyme based on high homology with the discoidin domain-containing protein and chitobiase/beta-hexosaminidase C terminal domain. CcGlcNAcase expression was notably increased when chitin was present. CcGlcNAcase produced N-acetyl-D-glucosamine from various lengths of N-acetyl-D-glucosamine. CcGlcNAcase bound to chitin (89%) and fungi (54.10%), whereas CcGlcNAcase exhibited a low binding ability to cellulose and xylan. CcGlcNAcase hydrolyzed fungi, yielding maximum 3.90 g/L N-acetyl-D-glucosamine. CcGlcNAcase enhanced cellulase toward fungi-infected lignocellulosic biomass, yielding 18 mg/L glucose (1.32-fold) and 1.72-fold increased total reducing sugar levels, whereas cellulase alone produced 13 mg/L glucose. Taken together, CcGlcNAcase can be utilized to enhance the degradation of fungi-infected lignocellulosic biomass and exhibits potential applications in the wood and sugar industry.
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