Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis

Liew, Kok Jun and Lim, Lily and Woo, Hui Ying and Chan, Kok Gan and Shamsir, Mohd Shahir and Goh, Kian Mau (2018) Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis. International Journal of Biological Macromolecules, 115. pp. 1094-1102. ISSN 0141-8130

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Official URL: https://doi.org/10.1016/j.ijbiomac.2018.04.156

Abstract

Beta-glucosidase (BGL) is an important industrial enzyme for food, waste and biofuel processing. Jeotgalibacillus is an understudied halophilic genus, and no beta-glucosidase from this genus has been reported. A novel beta-glucosidase gene (1344 bp) from J. malaysiensis DSM 28777T was cloned and expressed in E. coli. The recombinant protein, referred to as BglD5, consists of a total 447 amino acids. BglD5 purified using a Ni-NTA column has an apparent molecular mass of 52 kDa. It achieved the highest activity at pH 7 and 65 °C. The activity and stability were increased when CaCl2 was supplemented to the enzyme. The enzyme efficiently hydrolyzed salicin and (1 → 4)-beta-glycosidic linkages such as in cellobiose, cellotriose, cellotetraose, cellopentose, and cellohexanose. Similar to many BGLs, BglD5 was not active towards polysaccharides such as Avicel, carboxymethyl cellulose, Sigmacell cellulose 101, alpha-cellulose and xylan. When BglD5 blended with Cellic® Ctec2, the total sugars saccharified from oil palm empty fruit bunches (OPEFB) was enhanced by 4.5%. Based on sequence signatures and tree analyses, BglD5 belongs to the Glycoside Hydrolase family 1. This enzyme is a novel beta-glucosidase attributable to its relatively low sequence similarity with currently known beta-glucosidases, where the closest characterized enzyme is the DT-Bgl from Anoxybacillus sp. DT3-1.

Item Type: Article
Uncontrolled Keywords: beta-Glucosidase; Biotechnology; Cellobiose; Cloning, Molecular; Computational Biology; Kinetics; Molecular Weight; Planococcaceae; Substrate Specificity
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Ms. Juhaida Abd Rahim
Date Deposited: 17 Jun 2019 04:26
Last Modified: 17 Jun 2019 04:26
URI: http://eprints.um.edu.my/id/eprint/21471

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