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

Learn More →

Purification and characterization of Streptomyces albidoflavus antifungal components

Purification and characterization of Streptomyces albidoflavus antifungal components Chitinolytic strain Streptomyces albidoflavus was isolated from soil of the central region of Poland. Its identification was based on analysis of 16S rRNA gene sequence. The colloidal chitin was revealed as the finest substrate for the production of chitinases by S. albidoflavus. The enzyme catalyzed the hydrolysis of the disaccharide 4-methylumbelliferyl-β-D-N,N′,N″-triacetylchitotriose most efficiently and was, therefore, classified as an endochitinase. The chitinase of S. albidoflavus was purified by applying the two-step procedure: fractionation with ammonium sulphate and chitin affinity chromatography. The molecular weight of the purified enzyme determined by SDS-PAGE was approximately 50 kDa. The enzyme was characterised as thermostable during 180 min of preincubation at the temperature of 35°C and 40°C. The activity of the enzyme was strongly inhibited in the presence of Hg2+ and Mn2+ ions, SDS but stabilized by Ca2+ and Mg2+ ions. Both purified and crude chitinases from S. albidoflavus inhibited the development of fungal phytopathogens. Purified chitinase inhibited the growth of Alternaria alternata, Fusarium culmorum, Fusarium oxysporum and Botrytis cinerea. Additionally, the crude chitinase inhibited the growth of Fusarium solani. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Purification and characterization of Streptomyces albidoflavus antifungal components

Loading next page...
 
/lp/springer-journals/purification-and-characterization-of-streptomyces-albidoflavus-QUihgitc0S

References (50)

Publisher
Springer Journals
Copyright
Copyright © 2013 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683813050025
Publisher site
See Article on Publisher Site

Abstract

Chitinolytic strain Streptomyces albidoflavus was isolated from soil of the central region of Poland. Its identification was based on analysis of 16S rRNA gene sequence. The colloidal chitin was revealed as the finest substrate for the production of chitinases by S. albidoflavus. The enzyme catalyzed the hydrolysis of the disaccharide 4-methylumbelliferyl-β-D-N,N′,N″-triacetylchitotriose most efficiently and was, therefore, classified as an endochitinase. The chitinase of S. albidoflavus was purified by applying the two-step procedure: fractionation with ammonium sulphate and chitin affinity chromatography. The molecular weight of the purified enzyme determined by SDS-PAGE was approximately 50 kDa. The enzyme was characterised as thermostable during 180 min of preincubation at the temperature of 35°C and 40°C. The activity of the enzyme was strongly inhibited in the presence of Hg2+ and Mn2+ ions, SDS but stabilized by Ca2+ and Mg2+ ions. Both purified and crude chitinases from S. albidoflavus inhibited the development of fungal phytopathogens. Purified chitinase inhibited the growth of Alternaria alternata, Fusarium culmorum, Fusarium oxysporum and Botrytis cinerea. Additionally, the crude chitinase inhibited the growth of Fusarium solani.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Sep 3, 2013

There are no references for this article.