NDLI: Purification and characterization of carboxymethyl cellulase and protease by Ulocladium botrytis Preuss ATCC 18042 using water hyacinth as a substrate under solid state fermentation

Content Provider	Springer Nature Link
Author	Abo Elmagd, Heba I. Housseiny, Manal M.
Copyright Year	2012
Abstract	The potential of 12 fungal strains to produce carboxymethyl cellulase (CMCase) and protease on Eichhornia crassipes (water hyacinth) wastes was investigated under conditions of solid state fermentation. Ulocladium botrytis (Preuss) was selected as the best fungus for the production of both enzymes. The best nitrogen sources for production of CMCase and protease were yeast extract and malt extract, respectively. CMCase and protease were purified by isopropanol (1:1) precipitation and column chromatography on Sephadex G-100 and DEAE-cellulose. Purification fold of 47.34 and 51.78, with 852.11 and 1,469.38 U/mg specific activity was achieved with 40.3 and 56.25% recovery after purification of CMCase and protease, respectively. The purified CMCase expressed its maximal activity at 60°C and pH 5.2, showed good stability in the pH range of 5.2–5.4 and its midpoint of thermal inactivation (Tm) was 60°C after 75 min exposure. The purified protease expressed its maximal activity at 35°C and pH 5.2, showed good stability in the pH range of 5.6–6.0 and its midpoint of thermal inactivation (Tm) was 35°C after 75 min exposure. The best substrate concentration for CMCase was 1.2% (w/v) Na-CMC and for protease, it was 0.8% (w/v) casein. The best enzyme concentration for the two tested enzymes was 0.4 U/ml. Ions of Ca$^{2+}$, Na$^{+}$ and K$^{+}$ showed a stimulatory effect but sodium arsenate and iodoacetate showed an inhibitory effect. Moreover, Ag$^{2+}$ and Hg$^{2+}$ inhibited both enzyme activities completely. The purified enzymes from Ulocladium botrytis had molecular weights of 50 and 83 kDa for CMCase, and 47 kDa for protease on SDS-PAGE.
Starting Page	1547
Ending Page	1556
Page Count	10
File Format	PDF
ISSN	15904261
Journal	Annals of Microbiology
Volume Number	62
Issue Number	4
e-ISSN	18692044
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-02-11
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Carboxymethyl cellulase Protease Ulocladium Eichhornia crassipes Microbial Genetics and Genomics Medical Microbiology Applied Microbiology Microbiology Microbial Ecology Fungus Genetics
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