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    Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/18844

    Title: Optimization of conditions for protease production by Chryseobacterium taeanense TKU001
    Authors: Wang, San-lang;Yang, Chun-hsiang;Liang, Tzu-wen;Yen, Yue-horng
    Contributors: 淡江大學化學學系
    Keywords: Chryseobacterium taeanense;Protease;Shrimp shell wastes
    Date: 2008-06
    Issue Date: 2013-02-27 09:31:32 (UTC+8)
    Publisher: Amsterdam: Elsevier BV
    Abstract: A protease-producing bacterium was isolated and identified as Chryseobacterium taeanense TKU001. An extracellular metalloprotease with novel properties of solvent- and surfactant-stable was purified from the culture supernatant of C. taeanense TKU001 with shrimp shell wastes as the sole carbon/nitrogen source. The optimized condition for protease production was found when the culture was shaken at 37 °C for 3 days in 50 mL of medium containing 0.5% shrimp shell powder (SSP) (w/v), 0.1% K2HPO4, and 0.05% MgSO4 · 7H2O. Two extracellular proteases (FI and FII) were purified and characterized, and their molecular weights, pH and thermal stabilities were determined. The molecular masses of TKU001 protease FI and FII determined by SDS-PAGE and gel filtration were approximately 41 kDa and 75 kDa, respectively.
    The optimum pH, optimum temperature, pH stability, and thermal stability of TKU001 protease FI were 8, 60 °C, pH 6–9, and 60 °C, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of TKU001 protease FII were 7, 60 °C, pH 7–9, and 50 °C, respectively. TKU001 protease FI and FII were both inhibited completely by EDTA, indicating that the TKU001 protease FI and FII were metalloproteases. TKU001 protease FI and FII retained more than 75% of its original protease activity after preincubation for 10 days at 4 °C in the presence of 25% most tested organic solvents. Additionally, the TKU001 protease FI retained 79%, 80%, and 110% of its original activity in the presence of 2% Tween 20, 2% Tween 40, and 2% Triton X-100, respectively. However, at the same condition, the activity of TKU001 protease FII retained 100%, 100%, and 121% of its original activity, respectively. This is the first report of C. taeanense being able to use shrimp shell wastes as the sole carbon/nitrogen source for proteases production. The novelties of the TKU001 protease include its high stability to the solvents and surfactants. These unique properties make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis.
    Relation: Bioresource Technology 99(9), pp.3700-3707
    DOI: 10.1016/j.biortech.2007.07.036
    Appears in Collections:[Graduate Institute & Department of Chemistry] Journal Article

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