Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium

doi:10.1016/j.enzmictec.2005.04.023

淡江大學機構典藏 > 理學院 > 生命科學研究所 > 期刊論文 > Item 987654321/18860

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题名:	Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium
作者:	Liang, Tzu-Wen;Lin, Jane-Jean;Yen, Yue-Horng;Wang, Chuan-Lu;Wang, San-Lang
贡献者:	淡江大學生命科學研究所
关键词:	Chitin;Molecular weight;pH effects;Purification;Monascus;Protease;Shrimp and crab cells;Enzymes;proteinase;article;crab;culture medium;enzyme analysis;enzyme isolation;enzyme purification;enzyme stability;Eurotiales;molecular weight;Monascus;Monascus purpureus;nonhuman;pH;powder;sequence homology;shrimp;supernatant;thermostability;vegetable;Decapoda (Crustacea);Eurotiales;Monascus;Monascus purpureus
日期:	2006-01
上传时间:	2013-02-27 09:39:51 (UTC+8)
出版者:	Philadelphia: Elsevier Inc.
摘要:	Monascus purpureus CCRC31499 produced a protease when it was grown in a medium containing shrimp and crab shell powder (SCSP) of marine wastes. An extracellular protease was purified from the culture supernatant to homology. The protease had a molecular weight of 40,000 and a pI of 7.9. The optimal pH, optimum temperature, pH stability, and thermal stability of the protease were pH 7–9, 40 °C, pH 5–9, and 40 °C, respectively. In addition to protease activity, CCRC31499 also exhibited activity of enhancing vegetable growth in culture supernatant. This is also the first report of isolation of a protease from Monascus species.
關聯:	Enzyme and Microbial Technology 38(1-2), pp.74-80
DOI:	10.1016/j.enzmictec.2005.04.023
显示于类别:	[生命科學研究所] 期刊論文

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