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فناوری منابع زیستی
جزئیات رویداد
همایش ، رویداد ، ژورنال
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  • formation of enzyme polymer engineered structure for laccase and cross-linked laccase aggregates stabilization

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    • تاریخ ارائه: 1390/01/01
    • تاریخ انتشار در تی پی بین: 1390/01/01
    • تعداد بازدید: 635
    • تعداد پرسش و پاسخ ها: 0
    • شماره تماس دبیرخانه رویداد: -
     laccase and laccase-based cross-linked enzyme aggregates (cleas) were stabilized through the formation of a surrounding polymeric network made of chitosan and 3-aminopropyltriethoxysilane. the thermoresistance of the resulting enzyme polymer engineered structures of laccase (epes-lac) and cleas (epes-clea) were more than 30 times higher than that of free laccase and cleas at ph 3 and 40 °c. the epes showed higher residual activity than the unmodified biocatalysts against chaotropic salts (up to 10 times), edta (up to 5 times), methanol (up to 15 times) and acetone (up to 20 times). the michaelis–menten kinetic parameters revealed that the affinity for 2,2’-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) has doubled for the epes-lac and epes clea compared to their unmodified forms. the epes-lac structures acted optimally at ph 4 and their activity was nearly temperature-independent, while the laccase activity of epes-clea was optimal at ph 4 and 60 °c. globally, the epes have shown significantly improved properties which make them attractive candidate for the development of laccase-based applications.

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