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

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 exp...

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Main Authors: Liew, Kok Jun, Lim, Lily, Woo, Hui Ying, Chan, Kok Gan, Shamsir, Mohd. Shahir, Goh, Kian Mau
Format: Article
Published: Elsevier B.V. 2018
Subjects:
QR Microbiology
Online Access:http://eprints.utm.my/id/eprint/84328/
http://dx.doi.org/10.1016/j.ijbiomac.2018.04.156
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spelling my.utm.843282019-12-28T01:46:49Z http://eprints.utm.my/id/eprint/84328/ Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis Liew, Kok Jun Lim, Lily Woo, Hui Ying Chan, Kok Gan Shamsir, Mohd. Shahir Goh, Kian Mau QR Microbiology 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. Elsevier B.V. 2018-08 Article PeerReviewed 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 http://dx.doi.org/10.1016/j.ijbiomac.2018.04.156
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
topic QR Microbiology
spellingShingle QR Microbiology
Liew, Kok Jun
Lim, Lily
Woo, Hui Ying
Chan, Kok Gan
Shamsir, Mohd. Shahir
Goh, Kian Mau
Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis
description 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.
format Article
author Liew, Kok Jun
Lim, Lily
Woo, Hui Ying
Chan, Kok Gan
Shamsir, Mohd. Shahir
Goh, Kian Mau
author_facet Liew, Kok Jun
Lim, Lily
Woo, Hui Ying
Chan, Kok Gan
Shamsir, Mohd. Shahir
Goh, Kian Mau
author_sort Liew, Kok Jun
title Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis
title_short Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis
title_full Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis
title_fullStr Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis
title_full_unstemmed Purification and characterization of a novel GH1 beta-glucosidase from Jeotgalibacillus malaysiensis
title_sort purification and characterization of a novel gh1 beta-glucosidase from jeotgalibacillus malaysiensis
publisher Elsevier B.V.
publishDate 2018
url http://eprints.utm.my/id/eprint/84328/
http://dx.doi.org/10.1016/j.ijbiomac.2018.04.156
_version_ 1654960072098316288
score 13.211869

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