Purification of laccase from newly isolated Bacillus Safensis and analysis of biochemical and structural properties of Laccase enzymes
محل انتشار: پنجمین کنگره ملی زیست شناسی و علوم طبیعی ایران
سال انتشار: 1396
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 705
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شناسه ملی سند علمی:
BSCONF05_014
تاریخ نمایه سازی: 22 دی 1396
چکیده مقاله:
laccase (EC 1.10.3.2) is an extracellular oxygenated oxidizer that uses molecular oxygen as the final receptor. In this study, the purity and location of the laccase enzyme from the new Bacillus safensisbacteria. The laccase active protein, expression was performed under aerobic conditions and at low temperature. The recombinant protein by the column tends to customize and determine the molecular gel of the enzyme by 60 SDS-PAGE clients. The enzyme has the best performance at 35 degree. The optimum pH of the enzyme activity is 5.5. This distinguishes its unusual property from other known bacterial laccases.
کلیدواژه ها:
نویسندگان
Atena Mashhadi
Department of Biology, Science and Research Branch, Islamic AzadUniversity,Tehran,Iran
Khosro Khajeh
Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran
Maryam Monsef Shokri
International Sturgeon Research Institute, Agricultural Research, Education & Extension Organization (AREEO), Rasht, Iran.
Bahare Dabirmanesh
Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran