NDLI: Expression ofBacillus subtilis JA18 endo-β-1,4-glucanase gene inEscherichia coli and characterization of the recombinant enzyme

Content Provider	Springer Nature Link
Author	Liu, Min Wang, Jun Liu, Jing Yao, Jianming Yu, Zengliang
Copyright Year	2006
Abstract	Endo-β-1,4-glucanase encoded byBacillus subtilis JA18 was expressed inEscherichia coli. The recombinant enzyme was purified and characterized. The purified enzyme showed a single band of 50 kDa by SDS-PAGE. The optimum pH and temperature for this endo-β-1,4-glucanase was pH 5.8 and 60 °C. The endo-β-1,4-glucanase was highly stable in a wide pH range, from 4.0 to 12.0. Furthermore, it remained stable up to 60 °C. The endo-β-1,4-glucanase was completely inhibited by 2 mM Zn$^{2+}$, Cu$^{2+}$, Fe$^{3+}$, Ag$^{+}$, whereas it is activated in the presence of Co$^{2+}$. In addition, the enzyme activity was inhibited by 1 mM Mn$^{2+}$ but stimulated by 10 mM Mn$^{2+}$. At 1% concentration, SDS completely inhibited the enzyme. The enzyme hydrolysed carboxymethylcellulose, lichenan but no activity was detected with regard to avicel, xylan, chitosan and laminarin. For carboxymethylcellulose, the enzyme had a Km of 14.7 mg/ml.
Starting Page	41
Ending Page	45
Page Count	5
File Format	PDF
ISSN	15904261
Journal	Annals of Microbiology
Volume Number	56
Issue Number	1
e-ISSN	18692044
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-01-01
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Bacillus subtilis characterization endo-β-1,4-glucanase heterologous expression Microbiology Microbial Genetics and Genomics Microbial Ecology Fungus Genetics Medical Microbiology Applied Microbiology
Content Type	Text
Resource Type	Article
Subject	Applied Microbiology and Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Cloning and expression of a thermostable β-1,3-1,4-glucanase from Bacillus amyloliquefaciens ATCC 23350

Cloning, heterologous expression, and comparative characterization of a mesophilic α-amylase gene from Bacillus subtilis JN16 in Escherichia coli

Overexpression of type I L-asparaginase ofBacillus subtilis inEscherichia coli, rapid purification and characterisation of recombinant type I L-asparaginase

A novel xyloglucan-specific endo-β-1,4-glucanase: biochemical properties and inhibition studies

Gene cloning and expression of a new acidic family 7 endo-β-1,3-1,4-glucanase from the acidophilic fungus Bispora sp. MEY-1

Cloning and expression of a lipase gene from Bacillus subtilis FS1403 in Escherichia coli

Gene clone and expression of a fibrinolytic enzyme (FE) inEscherichia coli

Cloning and functional characterization of a novel endo-β-1,4-glucanase gene from a soil-derived metagenomic library

Heterologous expression of an endo-β-1,4-glucanase gene from the anaerobic fungus Orpinomyces PC-2 in Trichoderma reesei

Expression ofBacillus subtilis JA18 endo-β-1,4-glucanase gene inEscherichia coli and characterization of the recombinant enzyme

Similar Documents

Cloning and expression of a thermostable β-1,3-1,4-glucanase from Bacillus amyloliquefaciens ATCC 23350

Cloning, heterologous expression, and comparative characterization of a mesophilic α-amylase gene from Bacillus subtilis JN16 in Escherichia coli

Overexpression of type I L-asparaginase ofBacillus subtilis inEscherichia coli, rapid purification and characterisation of recombinant type I L-asparaginase

A novel xyloglucan-specific endo-β-1,4-glucanase: biochemical properties and inhibition studies

Gene cloning and expression of a new acidic family 7 endo-β-1,3-1,4-glucanase from the acidophilic fungus Bispora sp. MEY-1

Cloning and expression of a lipase gene from Bacillus subtilis FS1403 in Escherichia coli

Gene clone and expression of a fibrinolytic enzyme (FE) inEscherichia coli

Cloning and functional characterization of a novel endo-β-1,4-glucanase gene from a soil-derived metagenomic library

Heterologous expression of an endo-β-1,4-glucanase gene from the anaerobic fungus Orpinomyces PC-2 in Trichoderma reesei

Expression ofBacillus subtilis JA18 endo-β-1,4-glucanase gene inEscherichia coli and characterization of the recombinant enzyme