Characterization of a glucose tolerant beta glucosidase from Aspergillus unguis with high potential as a blend-in for biomass hydrolyzing enzyme cocktails
- Title
- Characterization of a glucose tolerant beta glucosidase from Aspergillus unguis with high potential as a blend-in for biomass hydrolyzing enzyme cocktails
- Author
- Amith Abraham
- Keywords
- b-glucosidase; Glucose tolerant; Aspergillus unguis; Biomass hydrolysis; Genome; Homology model
- Issue Date
- 2019-10
- Publisher
- SPRINGER
- Citation
- BIOTECHNOLOGY LETTERS, v. 41, no. 10, page. 1201-1211
- Abstract
- Objectives: Characterization of glucose tolerant beta glucosidase (GT-BGL) secreted by Aspergillus unguis NII 08123, determination of the gene and protein sequences of the enzyme and establishing its performance in blends for lignocellulose hydrolysis.
Results: Supplementation of A. unguis beta glucosidase (BGL) to cellulase released 1.6 times more sugar within 12 h during the hydrolysis of lignocellulosic biomass. The enzyme was determined to be similar to BGL-F from Emericella nidulans by MALDI-TOF analysis, and was found to be a GH3 family protein. Molecular Docking simulation studies showed that the enzyme has lesser affinity for glucose (− 5.7 kcal/mol) compared to its substrate cellobiose (− 7.5 kcal/mol). The residues present in the N-terminal domain are mostly involved in bond formation with both the substrate and the product, while the C-terminal domain contains the catalytic region. In-silico studies showed that its predicted structure is unlike that of previously reported BGLs, which might provide a clue to its exceptional catalytic activity.
Conclusion: The GT-BGL from A. unguis NII 08123 was proven effective as a blend in for biomass hydrolyzing enzyme cocktails and the possible reasons for its glucose tolerance was determined through studies on its modeled structure.
- URI
- https://link.springer.com/article/10.1007/s10529-019-02724-zhttps://repository.hanyang.ac.kr/handle/20.500.11754/177324
- ISSN
- 0141-5492; 1573-6776
- DOI
- 10.1007/s10529-019-02724-z
- Appears in Collections:
- OFFICE OF ACADEMIC AFFAIRS[S](교무처) > Center for Creative Convergence Education(창의융합교육원) > Articles
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