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  • purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from trametes pubescens

    جزئیات بیشتر مقاله
    • تاریخ ارائه: 1390/01/01
    • تاریخ انتشار در تی پی بین: 1390/01/01
    • تعداد بازدید: 786
    • تعداد پرسش و پاسخ ها: 0
    • شماره تماس دبیرخانه رویداد: -

    extracellular laccase (tplac) from trametes pubescens was purified to homogeneity by a three-step method, which resulted in a high specific activity of 18.543 u mg−1, 16.016-fold greater than that of crude enzyme at the same level. tplac is a monomeric protein that has a molecular mass of 68 kda. the enzyme demonstrated high activity toward 1.0 mm abts at an optimum ph of 5.0 and temperature of 50 °c, and under these conditions, the catalytic efficiency (kcat/km) is 8.34 s−1 μm−1. tplac is highly stable and resistant under alkaline conditions, with ph values ranging from 7.0 to 10.0. interestingly, above 88% of initial enzyme activity was maintained in the presence of metal ions at 25.0 mm, leading to an increase in substrate affinity, which indicated that the laccase is highly metal-tolerant. these unusual properties demonstrated that the new fungal laccase tplac has potentials for the specific industrial or environmental applications.

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