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KMID : 0043320160390070878
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Archives of Pharmacal Research
2016 Volume.39 No. 7 p.878 ~ p.886
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Purification and characterization of chitinase showing antifungal and biodegradation properties obtained from Streptomyces anulatus CS242
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Mander Poonam
Cho Seung-Sik
Choi Yun-Hee
Panthi Sandesh
Choi Yoon-Seok
Kim Hwan-Mook
Yoo Jin-Cheol
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Abstract
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In an effort to identify a microbial enzyme that can be useful as a fungicide and biodegradation agent of chitinous wastes, a chitinase (Chi242) was purified from the culture supernatant of Streptomyces anulatus CS242 utilizing powder of shrimp shell wastes as a sole carbon source. It was purified employing ammonium sulfate precipitation and gel permeation chromatography techniques. The molecular weight of the purified chitinase was ~38 kDa by SDS-PAGE. The N-terminal amino acid sequence (A-P-G-A-P-G-T-G-A-L) showed close similarity to those of other Streptomyes chitinases. The purified enzyme displayed optimal activity at pH 6.0 and 50 °C respectively. It showed substantial thermal stability for 2 h at 30?60 °C, and exhibited broad pH stability in the range 5.0?13.0 for 48 h at 4 °C. Scanning electron microscopy confirmed the ability of this enzyme to adsorb onto solid shrimp bio-waste and to degrade chitin microfibers. Chi242 could proficiently convert colloidal chitin to N-acetyl glucosamine (GlcNAc) and N-acetyl chitobiose (GlcNAc)2 signifying that this enzyme is suitable for bioconversion of chitin waste. In addition, it exerted an effective antifungal activity towards fungal pathogen signifying its role as a biocontrol agent. Thus, a single microbial cell of Streptomyces anulatus CS242 justified its dual role.
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KEYWORD
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Antifungal enzyme, Chitinase, Chitinous shrimp waste, Chitooligosaccharide, Streptomyces anulatus
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