کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
18766 42741 2006 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Kinetic characterization of cresolase activity of Streptomyces antibioticus tyrosinase
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Kinetic characterization of cresolase activity of Streptomyces antibioticus tyrosinase
چکیده انگلیسی

Streptomyces antibioticus tyrosinase was purified using PEG-8000/phosphate phase partitioning and ammonium sulfate fractionation between 0 and 60%, rendering a clear and stable enzyme compared with the black one that is usually obtained when only ammonium sulphate fractionation is used, and with a 93% of recovery. This enzyme shows both monophenolase (also termed cresolase) and diphenolase (catecholase) activities, confirming that it is a real tyrosinase. The monophenolase activity was characterized by a lag period, whose duration depends on the substrate concentration, the pH, and the presence of catalytic amounts of o-diphenol. The enzyme showed substrate inhibition for p-cresol, with a KM of 0.97 mM and a Ksi of 23 mM. By increasing the concentration of o-diphenols, it was possible to evaluate the enzyme activation constant, Kact, which showed a value of 0.2 μM. The diphenolase activity was kinetically characterized with 4-methylcathechol, showed an optimal pH at 6.5 and a KM of 1.3 mM.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 39, Issue 1, 1 June 2006, Pages 158–163
نویسندگان
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