Archives of Pharmacal Research 2014-12-01

An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501.

Md Arifur Rahman, Yun Hee Choi, G C Pradeep, Jin Cheol Yoo

Index: Arch. Pharm. Res. 37(12) , 1522-9, (2014)

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Abstract

A chitinase from Streptomyces sp. CS501 was isolated from the Korean soil sample, purified by single-step chromatography, and biochemically characterized. The extracellular chitinase (Ch501) was purified to 4.60 fold with yield of 28.74 % using Sepharose Cl-6B column. The molecular mass of Ch501 was approximately 43 kDa as estimated by SDS-PAGE and zymography. The enzyme (Ch501) was found to be stable over a broad pH range (5.0-10.0) and temperature (up to 50 °C), and have an optimum temperature of 60 °C. N-terminal sequence of Ch501 was AAYDDAAAAA. Intriguingly, Ch501 was highly sensitive to ammonium sulfate but it's completely suppressed activity was recovered after desalting out. TLC analysis of Ch501 showed the production of N-acetyl D-glucosamine (GlcNAc) and Diacetylchitobiose (GlcNAc)2, as a principal hydrolyzed product. Ch501 shows antifungal activity against Fusarium solani and Aspergillus brasiliensis, which can be used for the biological control of fungus. As has been simple in purification, stable in a broad range of pH, ability to produce oligosaccharides, and antifungal activity showed that Ch501 has potential applications in industries as for chitooligosaccharides production used as prebiotics and/or for the biological control of plant pathogens in agriculture.