Staff View: Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1

Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1

New thermostable beta-1,3-1,4-glucanase (lichenase) designated as Blg29 was expressed and purified from a locally isolated alkaliphilic bacteria Bacillus lehensis G1. The genome sequence of B. lehensis predicted an open reading frame of Blg29 with a deduced of 249 amino acids and a molecular weight...

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Main Authors:	Yajit, Noor Liana Mat, Hashim, Noor Haza Fazlin, Illias, Rosli Mohd, Murad, Abdul Munir Abdul
Format:	Article
Published:	Elsevier 2024
Subjects:	Q Science (General) T Technology (General)
Online Access:	http://eprints.um.edu.my/46976/ https://doi.org/10.1016/j.pep.2024.106486
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spelling	my.um.eprints.469762025-01-09T04:04:25Z http://eprints.um.edu.my/46976/ Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1 Yajit, Noor Liana Mat Hashim, Noor Haza Fazlin Illias, Rosli Mohd Murad, Abdul Munir Abdul Q Science (General) T Technology (General) New thermostable beta-1,3-1,4-glucanase (lichenase) designated as Blg29 was expressed and purified from a locally isolated alkaliphilic bacteria Bacillus lehensis G1. The genome sequence of B. lehensis predicted an open reading frame of Blg29 with a deduced of 249 amino acids and a molecular weight of 28.99 kDa. The gene encoding for Blg29 was successfully amplified via PCR and subsequently expressed as a recombinant protein using the E. coli expression system. Recombinant Blg29 was produced as a soluble form and further purified via immobilized metal ion affinity chromatography (IMAC). Based on biochemical characterization, recombinant Blg29 showed optimal activity at pH9 and temperature 60 degrees C respectively. This enzyme was stable for more than 2 h, incubated at 50 degrees C, and could withstand similar to 50 % of its activity at 70 degrees C for an hour and a half. No significant effect on Blg29 was observed when incubated with metal ions except for a small increase with ion Ca2+. Blg29 showed high substrate activity towards lichenan where V-m, K-m, K-cat,K- and k(cat)/K-m values were 2040.82 mu molmin(-1)mg(-1), 4.69 mg/mL, and 986.39 s(-1) and 210.32 mLs(-1)mg(-1) respectively. The high thermostability and activity make this enzyme useable for a broad prospect in industry applications. Elsevier 2024-07 Article PeerReviewed Yajit, Noor Liana Mat and Hashim, Noor Haza Fazlin and Illias, Rosli Mohd and Murad, Abdul Munir Abdul (2024) Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1. Protein Expression and Purification, 219. p. 106486. ISSN 1046-5928, DOI https://doi.org/10.1016/j.pep.2024.106486 <https://doi.org/10.1016/j.pep.2024.106486>. https://doi.org/10.1016/j.pep.2024.106486 10.1016/j.pep.2024.106486
institution	Universiti Malaya
building	UM Library
collection	Institutional Repository
continent	Asia
country	Malaysia
content_provider	Universiti Malaya
content_source	UM Research Repository
url_provider	http://eprints.um.edu.my/
topic	Q Science (General) T Technology (General)
spellingShingle	Q Science (General) T Technology (General) Yajit, Noor Liana Mat Hashim, Noor Haza Fazlin Illias, Rosli Mohd Murad, Abdul Munir Abdul Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1
description	New thermostable beta-1,3-1,4-glucanase (lichenase) designated as Blg29 was expressed and purified from a locally isolated alkaliphilic bacteria Bacillus lehensis G1. The genome sequence of B. lehensis predicted an open reading frame of Blg29 with a deduced of 249 amino acids and a molecular weight of 28.99 kDa. The gene encoding for Blg29 was successfully amplified via PCR and subsequently expressed as a recombinant protein using the E. coli expression system. Recombinant Blg29 was produced as a soluble form and further purified via immobilized metal ion affinity chromatography (IMAC). Based on biochemical characterization, recombinant Blg29 showed optimal activity at pH9 and temperature 60 degrees C respectively. This enzyme was stable for more than 2 h, incubated at 50 degrees C, and could withstand similar to 50 % of its activity at 70 degrees C for an hour and a half. No significant effect on Blg29 was observed when incubated with metal ions except for a small increase with ion Ca2+. Blg29 showed high substrate activity towards lichenan where V-m, K-m, K-cat,K- and k(cat)/K-m values were 2040.82 mu molmin(-1)mg(-1), 4.69 mg/mL, and 986.39 s(-1) and 210.32 mLs(-1)mg(-1) respectively. The high thermostability and activity make this enzyme useable for a broad prospect in industry applications.
format	Article
author	Yajit, Noor Liana Mat Hashim, Noor Haza Fazlin Illias, Rosli Mohd Murad, Abdul Munir Abdul
author_facet	Yajit, Noor Liana Mat Hashim, Noor Haza Fazlin Illias, Rosli Mohd Murad, Abdul Munir Abdul
author_sort	Yajit, Noor Liana Mat
title	Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1
title_short	Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1
title_full	Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1
title_fullStr	Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1
title_full_unstemmed	Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1
title_sort	expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic bacillus lehensis g1
publisher	Elsevier
publishDate	2024
url	http://eprints.um.edu.my/46976/ https://doi.org/10.1016/j.pep.2024.106486
_version_	1821105747666141184
score	13.244413

Expression and biochemical characterization of a novel thermostable alkaline β-1,3-1,4-glucanase (lichenase) from an alkaliphilic Bacillus lehensis G1

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