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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/18860

    Title: Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium
    Authors: Liang, Tzu-Wen;Lin, Jane-Jean;Yen, Yue-Horng;Wang, Chuan-Lu;Wang, San-Lang
    Contributors: 淡江大學生命科學研究所
    Keywords: 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
    Date: 2006-01
    Issue Date: 2013-02-27 09:39:51 (UTC+8)
    Publisher: Philadelphia: Elsevier Inc.
    Abstract: 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.
    Relation: Enzyme and Microbial Technology 38(1-2), pp.74-80
    DOI: 10.1016/j.enzmictec.2005.04.023
    Appears in Collections:[Graduate Institue of Life Sciences] Journal Article

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