Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Screening of chitin deacetylase from Mucoralean strains (Zygomycetes) and its relationship to cell growth rate

Screening of chitin deacetylase from Mucoralean strains (Zygomycetes) and its relationship to... Chitin deacetylase (CDA) is an enzyme that catalyzes the hydrolysis of acetamine groups of N-acetyl-d-glucosamine in chitin, converting it to chitosan in fungal cell walls. In the present study, the activity in batch culture of CDA from six Mucoralean strains, two of them wild type, isolated from dung of herbivores of Northeast Brazil, was screened. Among the strains tested, Cunninghamella bertholletiae IFM 46114 showed a high intracellular enzyme activity of 0.075 U/mg protein after 5 days of culture, and a wild-type strain of Mucor circinelloides showed a high intracellular enzyme activity of 0.060 U/mg protein, with only 2 days of culture, using N-acetylchitopentaose as substrate. This enzyme showed optimal activity at pH 4.5 in 25 mM glutamate-sodium buffer at 50°C, and was stable over 1 h preincubation at the same temperature. The kinetic parameters of CDA did not follow Michaelis-Menten kinetics, but rather Hill affinity distribution, showing probable allosteric behavior. The apparent K HILL and V max of CDA were 288±34 nmol/l and 0.08±0.01 U mg protein−1 min−1, respectively, using N-acetylchitopentaose as substrate at pH 4.5 at 50°C. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Industrial Microbiology & Biotechnology Springer Journals

Screening of chitin deacetylase from Mucoralean strains (Zygomycetes) and its relationship to cell growth rate

Download PDF
5 pages

Loading next page...
 
/lp/springer-journals/screening-of-chitin-deacetylase-from-mucoralean-strains-zygomycetes-gDpkpMklIc

References (20)

Publisher
Springer Journals
Copyright
Copyright © 2005 by Society for Industrial Microbiology
Subject
LifeSciences
ISSN
1367-5435
eISSN
1476-5535
DOI
10.1007/s10295-004-0197-7
pmid
15668816
Publisher site
See Article on Publisher Site

Abstract

Chitin deacetylase (CDA) is an enzyme that catalyzes the hydrolysis of acetamine groups of N-acetyl-d-glucosamine in chitin, converting it to chitosan in fungal cell walls. In the present study, the activity in batch culture of CDA from six Mucoralean strains, two of them wild type, isolated from dung of herbivores of Northeast Brazil, was screened. Among the strains tested, Cunninghamella bertholletiae IFM 46114 showed a high intracellular enzyme activity of 0.075 U/mg protein after 5 days of culture, and a wild-type strain of Mucor circinelloides showed a high intracellular enzyme activity of 0.060 U/mg protein, with only 2 days of culture, using N-acetylchitopentaose as substrate. This enzyme showed optimal activity at pH 4.5 in 25 mM glutamate-sodium buffer at 50°C, and was stable over 1 h preincubation at the same temperature. The kinetic parameters of CDA did not follow Michaelis-Menten kinetics, but rather Hill affinity distribution, showing probable allosteric behavior. The apparent K HILL and V max of CDA were 288±34 nmol/l and 0.08±0.01 U mg protein−1 min−1, respectively, using N-acetylchitopentaose as substrate at pH 4.5 at 50°C.

Journal

Journal of Industrial Microbiology & Biotechnology – Springer Journals

Published: Jan 25, 2005

There are no references for this article.