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Molecular Characterization and Potential Synthetic Applications of GH1 β-Glucosidase from Higher Termite Microcerotermes annandalei

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Abstract

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.

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Acknowledgements

The authors especially thank Dr. Nonlawat Boonyalai, Kasetsart University, Thailand, for kindly providing the gel filtration calibration kit and Blue Dextran 2000 and Dr. Suraphon Visetson, Kasetsart University, Thailand, for helpful advice.

Funding

The project was partly supported by grants from the Thailand Research Fund (MRG-WII525S034), the Higher Education Research Promotion and National Research University Project of Thailand, Kasetsart University Research and Development Institute (V-T(D)47.53), and the Faculty of Science, Kasetsart University (ScRF-S11/2553). W.J. and E.S. are recipients of the MAG Window II scholarship from the Thailand Research Fund and the Ph.D. scholarship from the Graduate School, Kasetsart University, respectively.

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Authors and Affiliations

  1. Department of Biochemistry, Faculty of Science, and Center for Advanced Studies in Tropical Natural Resources, NRU-KU, Kasetsart University, 50 Paholyotin Road, Chatuchak, Bangkok, 10900, Thailand

    Siriphan Arthornthurasuk, Wantha Jenkhetkan & Prachumporn T. Kongsaeree

  2. Interdisciplinary Graduate Program in Genetic Engineering, Faculty of Graduate School, Kasetsart University, Bangkok, 10900, Thailand

    Eukote Suwan & Prachumporn T. Kongsaeree

  3. Laboratory of Biochemistry, Chulabhorn Research Institute, Bangkok, 10210, Thailand

    Daranee Chokchaichamnankit, Chantragan Srisomsap & Jisnuson Svasti

  4. Department of Chemistry, Center of Excellence for Innovation in Chemistry and Special Research Unit for Advanced Magnetic Resonance, Faculty of Science, Kasetsart University, Bangkok, 10900, Thailand

    Pakorn Wattana-Amorn

  5. Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, 10400, Thailand

    Jisnuson Svasti

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  1. Siriphan Arthornthurasuk
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Arthornthurasuk, S., Jenkhetkan, W., Suwan, E. et al. Molecular Characterization and Potential Synthetic Applications of GH1 β-Glucosidase from Higher Termite Microcerotermes annandalei. Appl Biochem Biotechnol 186, 877–894 (2018). https://doi.org/10.1007/s12010-018-2781-8

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