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-Eun; Shin, Sang Kyu; Oh, Jeong-Joo; Hwang, Dong-Hyeok; Ko, Young Jin; Hyeon, Jeong Eun; Han, 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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Collections - Graduate School > Department of Biotechnology > 1. Journal Articles
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