Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis
محل انتشار: مجله آرشیو رازی، دوره: 67، شماره: 2
سال انتشار: 1391
نوع سند: مقاله ژورنالی
زبان: انگلیسی
مشاهده: 46
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شناسه ملی سند علمی:
JR_ARCHRAZI-67-2_009
تاریخ نمایه سازی: 6 دی 1402
چکیده مقاله:
The aim of this study was production and partial purification of α-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of ۱۲۰ h, temperature of ۳۷ °C and pH ۷.۰. The α-amylase enzyme was purified by ion exchange chromatography on DEAE-sepharose CL-۶B and sephadex G-۱۰۰ gel filtration with a ۱۹.۱-fold increase in specific activity as compared to the concentrated supernatant and with a specific activity of ۹۲۶.۴۷ U/mg. The α-amylase had the highest activity at pH ۷.۰ and ۶۵ °C. According to the data on native polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was ۷۲ kDa.
کلیدواژه ها:
نویسندگان
A. Zare Mirakabadi
Department of venomous animals and anti venom production, Razi Vaccine & Serum Research Institute, Karaj, Iran
M. Ghorbanpour
Department of Chemical Engineering, Amirkabir University, Tehran, Iran
A. Sadeghi
Department of Chemical Engineering, Amirkabir University, Tehran, Iran
A. Sarzaeem
Department of venomous animals and anti venom production, Razi Vaccine & Serum Research Institute, Karaj, Iran