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Cloning and characterization of bgl6111 gene encoding ??glucosidase from bagasse metagenome
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Document Title
Cloning and characterization of bgl6111 gene encoding ??glucosidase from bagasse metagenome
Author
Prayogo F.A. Bunterngsook B. Kanokratana P. Kusumaningrum H.P. Wulandari D. Budiharjo A.
Affiliations
Biomedical Sciences Study Program Karya Husada University Jl. R. Kompol Soekanto No.46 Semarang 50276 Indonesia; Enzyme Technology Laboratory National Centre for Genetic Engineering and Biotechnology (BIOTEC) National Science and Technology Development Agency 113 Thailand Science Park Phahonyothin Road Khlong Luang Pathumthani 12120 Thailand; Biotechnology Study Program Diponegoro University Jl. Prof Soedharto SH Semarang 50275 Indonesia; Molecular and Applied Microbiology Laboratory Central Laboratory of Research and Service Diponegoro University Jl. Prof. SudhartoSH Semarang 50275 Indonesia
Type
Article
Source Title
Indonesian Journal of Biotechnology
ISSN
8538654
Year
2023
Volume
28
Issue
4
Page
200-208
Open Access
All Open Access Gold
Publisher
Universitas Gadjah Mada Research Center for Biotechnology
DOI
10.22146/ijbiotech.81536
Abstract
??Glucosidase (BGL) is an essential enzyme for the hydrolysis of cellulose in industrial processes but natural BGL enzymes are poorly understood. Metagenomics is a robust tool for bioprospecting in the search for novel enzymes from the entire community s genomic DNA present in nature. The metagenomics approach simplifies the process of searching for new BGL enzymes by extracting DNA and retrieving its gene information through a series of bioinformatic analyses. In this study we report the gene cloning heterologous expression of the bgl6111 gene (accession number MW221260) in Pichia pastoris KM71 and the biochemical characterization of the recombinant enzyme. We successfully identified the bgl6111 sequence of 2 520 bp and 839 amino acids with a molecular size of 89.4 kDa. The amino acid sequence of the bgl6111 gene showed 67.61% similarity to BGL from an uncultured bacterium (ABB51613.1). The BGL product has the highest activity on the third day at 1.210 U/mL categorized as low production. The enzymatic activity could enhance up to 539.8% of 7.742 U/mL by using the ultrafiltration method. Our findings provide insightful information that bgl6111 obtained from bagasse metagenome could be an alternative candidate for industrial applications in the future. Copyright ? 2023 THE AUTHOR(S). This article is distributed under a Creative Commons Attribution?ShareAlike 4.0 International license.
Keyword
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
License
CC BY-SA
Rights
Authors
Publication Source
Scopus