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Purification and characterization of chitinase showing antifungal and biodegradation properties obtained from Streptomyces anulatus CS242

Authors
Mander, PoonamCho, Seung SikChoi, Yun HeePanthi, SandeshChoi, Yoon SeokKim, Hwan MookYoo, Jin Cheol
Issue Date
Jul-2016
Publisher
PHARMACEUTICAL SOC KOREA
Keywords
Antifungal enzyme; Chitinase; Chitinous shrimp waste; Chitooligosaccharide; Streptomyces anulatus
Citation
ARCHIVES OF PHARMACAL RESEARCH, v.39, no.7, pp.878 - 886
Journal Title
ARCHIVES OF PHARMACAL RESEARCH
Volume
39
Number
7
Start Page
878
End Page
886
URI
https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/8147
DOI
10.1007/s12272-016-0747-3
ISSN
0253-6269
Abstract
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 similar to 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 A degrees C respectively. It showed substantial thermal stability for 2 h at 30-60 A degrees C, and exhibited broad pH stability in the range 5.0-13.0 for 48 h at 4 A degrees 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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