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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/85545

    Title: Bacillus subtilis TKU007利用蝦殼廢棄物發酵所產耐介面活性劑及有機溶劑之鹼性蛋白脢其純化及定性
    Authors: 葉佩怡;王三郎
    Contributors: 淡江大學生命科學研究所
    Keywords: Bacillus subtilis;Alkaliphilic protease;Surfactent stable;Solvent stable;Shrimp shell wastes
    Date: 2006
    Issue Date: 2013-04-09 11:39:07 (UTC+8)
    Abstract: An extracellular serine protease with novel properties of surfactant-stable, solvent-stable, and alkaliphilic was purified from the culture supernatant of Bacillus subtilis TKU007 with shrimp shell wastes as the sole carbon/nitrogen source. The TKU007 protease showed suppressing effect on the chitosanase, which appeared at the first day. The molecular mass of TKU007 protease determined by SDS-PAGE and gel filtration was approximately 28 kDa and 30 kDa, respectively. The optimum pH, optimum temperature, pH stability, thermal stability, Km, and Vmax of TKU007 protease was 7-11, 50.degree.C, pH 5-11, 50.degree.C, 0.13 mg/mL, and 0.86 U/mL, respectively. More than 80% of its original activity was retained even after preincubation for 10 days at 25.degree.C in the presence of 25% tested organic solvents. Additionally, the TKU007 protease retained 100%, 100%, 50%, and 65% of its original activity in the presence of 2% Tween 20, 2% Tween 40, 2% Triton X-100, or 0.5 mM SDS, respectively. In conclusion, the novelties of the TKU007 protease include its high stability to the solvents, surfactants, and alkali. These unique properties make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis.
    Relation: 2006 台灣幾丁質幾丁聚醣研討會論文集, 4p.
    Appears in Collections:[Graduate Institue of Life Sciences] Proceeding

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