Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Amith Abraham | - |
dc.date.accessioned | 2022-11-24T01:03:48Z | - |
dc.date.available | 2022-11-24T01:03:48Z | - |
dc.date.issued | 2019-10 | - |
dc.identifier.citation | BIOTECHNOLOGY LETTERS, v. 41, no. 10, page. 1201-1211 | en_US |
dc.identifier.issn | 0141-5492; 1573-6776 | en_US |
dc.identifier.uri | https://link.springer.com/article/10.1007/s10529-019-02724-z | en_US |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/177324 | - |
dc.description.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. | en_US |
dc.description.sponsorship | PKV wishes to thank CSIR for providing research fellowship to pursue his PhD studies at NIIST. We are thankful to Department of Biotechnology, Govt. of India for R&D funding to RKS under the project BT/PR20695/BBE/117/211/2016. The P. janthinellum strain is a kind gift from Dr. D. V. Gokhale, from the CSIR-National Chemical Laboratory, Pune, India. We thank Dr. N Ramesh Kumar, MPTD, CSIR-NIIST for sequencing services and Mass Spectrometry and Proteomic Core Facility, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram for the MALDI-TOF analysis. | en_US |
dc.language | en | en_US |
dc.publisher | SPRINGER | en_US |
dc.subject | b-glucosidase; Glucose tolerant; Aspergillus unguis; Biomass hydrolysis; Genome; Homology model | en_US |
dc.title | Characterization of a glucose tolerant beta glucosidase from Aspergillus unguis with high potential as a blend-in for biomass hydrolyzing enzyme cocktails | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1007/s10529-019-02724-z | en_US |
dc.relation.journal | BIOTECHNOLOGY LETTERS | - |
dc.contributor.googleauthor | Valappil, Prajeesh Kooloth | - |
dc.contributor.googleauthor | Rajasree, Kuni Parambil | - |
dc.contributor.googleauthor | Abraham, Amith | - |
dc.contributor.googleauthor | Christopher, Meera | - |
dc.contributor.googleauthor | Sukumaran, Rajeev K. | - |
dc.relation.code | 2019036298 | - |
dc.sector.campus | S | - |
dc.sector.daehak | OFFICE OF ACADEMIC AFFAIRS[S] | - |
dc.sector.department | CENTER FOR CREATIVE CONVERGENCE EDUCATION | - |
dc.identifier.pid | amithabraham | - |
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