An antifungal protease produced by Pseudomonas aeruginosa M-1001 with shrimp and crab shell powder as a carbon source

doi:10.1016/j.enzmictec.2005.11.050

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Title:	An antifungal protease produced by Pseudomonas aeruginosa M-1001 with shrimp and crab shell powder as a carbon source
Authors:	Yen, Yue-Horng;Li, Pei-Ling;Wang, Chuan-Lu;Wang, San-Lang
Contributors:	淡江大學生命科學研究所
Keywords:	Chitin;Fungi;Molecular weight;pH effects;Thermal effects;Antifungal;Protease;Pseudomonas aeruginosa;Shrimp and crab shell powder;Proteins;proteinase;antifungal activity;article;carbon source;controlled study;crab;culture medium;evolutionary homology;fungal spore germination;fungus hyphae;Fusarium solani;inhibition kinetics;marine environment;molecular stability;molecular weight;nonhuman;pH;Pseudomonas aeruginosa;shrimp;supernatant;temperature;Decapoda (Crustacea);Fungi;Fusarium solani;Pseudomonas aeruginosa
Date:	2006-06
Issue Date:	2013-02-27 09:39:35 (UTC+8)
Publisher:	Philadelphia: Elsevier Inc.
Abstract:	Pseudomonas aeruginosa M-1001 produced a protease when it was grown in a medium containing shrimp and crab shell powder (SCSP) of marine wastes. An antifungal protease was purified from the culture supernatant to homology. The protease had a molecular weight of 38,000 and a pI of 5.7. The optimum pH, optimum temperature, and pH stability of the protease were pH 7, 37 °C, and pH 5–8, respectively. Antifungal activity of the protease was found when using assay based upon inhibition of spores germination and hyphal extension of the fungal Fusarium solani.
Relation:	Enzyme and Microbial Technology 39(2), pp.311-317
DOI:	10.1016/j.enzmictec.2005.11.050
Appears in Collections:	[Graduate Institue of Life Sciences] Journal Article

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