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/ β-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.
Original language | English |
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Article number | 124242 |
Journal | Bioresource technology |
Volume | 319 |
DOIs | |
Publication status | Published - 2021 Jan |
Bibliographical note
Funding Information:This work was supported by National Research Foundation of Korea (NRF) grant funded by the Korea government (MSIP) (no. 2018R1A2B2003704 ) and Korea University Grant.
Publisher Copyright:
© 2020 Elsevier Ltd
Keywords
- Cellulosome
- Chitin
- Clostridium cellulovorans
- Fungi degradation
- N-acetyl-β-D-glucosaminidase
ASJC Scopus subject areas
- Bioengineering
- Environmental Engineering
- Renewable Energy, Sustainability and the Environment
- Waste Management and Disposal