Publication: Molecular Characterization and Potential Synthetic Applications of GH1 β-Glucosidase from Higher Termite Microcerotermes annandalei
35
Issued Date
2018-12-01
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15590291
02732289
02732289
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2-s2.0-85047161119
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Mahidol University
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SCOPUS
Bibliographic Citation
Applied Biochemistry and Biotechnology. Vol.186, No.4 (2018), 877-894
Suggested Citation
Siriphan Arthornthurasuk, Wantha Jenkhetkan, Eukote Suwan, Daranee Chokchaichamnankit, Chantragan Srisomsap, Pakorn Wattana-Amorn, Jisnuson Svasti, Prachumporn T. Kongsaeree Molecular Characterization and Potential Synthetic Applications of GH1 β-Glucosidase from Higher Termite Microcerotermes annandalei. Applied Biochemistry and Biotechnology. Vol.186, No.4 (2018), 877-894. doi:10.1007/s12010-018-2781-8 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/44972
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Title
Molecular Characterization and Potential Synthetic Applications of GH1 β-Glucosidase from Higher Termite Microcerotermes annandalei
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Abstract
© 2018, Springer Science+Business Media, LLC, part of Springer Nature. A novel β-glucosidase from higher termite Microcerotermes annandalei (MaBG) was obtained via a screening method targeting β-glucosidases with increased activities in the presence of glucose. The purified natural MaBG showed a subunit molecular weight of 55 kDa and existed in a native form as a dimer without any glycosylation. Gene-specific primers designed from its partial amino acid sequences were used to amplify the corresponding 1,419-bp coding sequence of MaBG which encodes a 472-amino acid glycoside hydrolase family 1 (GH1) β-glucosidase. When expressed in Komagataella pastoris, the recombinant MaBG appeared as a ~ 55-kDa protein without glycosylation modifications. Kinetic parameters as well as the lack of secretion signal suggested that MaBG is an intracellular enzyme and not involved in cellulolysis. The hydrolytic activities of MaBG were enhanced in the presence of up to 3.5-4.5 M glucose, partly due to its strong transglucosylation activity, which suggests its applicability in biosynthetic processes. The potential synthetic activities of the recombinant MaBG were demonstrated in the synthesis of para-nitrophenyl-β-D-gentiobioside via transglucosylation and octyl glucoside via reverse hydrolysis. The information obtained from this study has broadened our insight into the functional characteristics of this variant of termite GH1 β-glucosidase and its applications in bioconversion and biotechnology.