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

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• 作者：Poonam Mander ; Seung Sik Cho ; Yun Hee Choi…
• 刊名：Archives of Pharmacal Research
• 出版年：2016
• 出版时间：July 2016
• 年：2016
• 卷：39
• 期：7
• 页码：878-886
• 全文大小：1,629 KB
• 刊物主题：Pharmacy; Pharmacology/Toxicology;
• 出版者：Springer Netherlands
• ISSN：1976-3786
• 卷排序：39

文摘

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.KeywordsAntifungal enzymeChitinaseChitinous shrimp wasteChitooligosaccharideStreptomyces anulatus