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Two-step purification and partial characterization of an extra cellular alpha-amylase from Bacillus licheniformis
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نویسنده
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زارع میرکآبادی عباس ,قربانپور محمد ,صادقی سحر ,سرزعیم علی
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منبع
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archives of razi institute - 2012 - دوره : 67 - شماره : 2 - صفحه:155 -160
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چکیده
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The aim of this study was production and partial purification of ?-amylase enzyme by bacillus licheniformis. b. licheniformis was allowed to grow in broth culture for purpose of inducing ?-amylase enzyme. optimal conditions for amylase production by b. licheniformis are incubation period of 120 h, temperature of 37 °c and ph 7.0. the ?-amylase enzyme was purified by ion exchange chromatography on deae-sepharose cl-6b and sephadex g-100 gel filtration with a 19.1-fold increase in specific activity as compared to the concentrated supernatant and with a specific activity of 926.47 u/mg. the ?-amylase had the highest activity at ph 7.0 and 65 °c. according to the data on native polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was 72 kda.
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کلیدواژه
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alpha-Amylase ,Bacillus licheniformis ,optimal conditions ,purification
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آدرس
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Razi Vaccine & Serum Research Institute, Karaj, Ir, Department of venomous animals and anti venom production, Razi Vaccine & Serum Research Institute, Karaj, Iran, ایران, amirkabir university of technology, Department of Chemical Engineering, Amirkabir University, Tehran, Iran, ایران, amirkabir university of technology, Department of Chemical Engineering, Amirkabir University, Tehran, Iran, ایران, Department of venomous animals and anti venom production, Razi Vaccine & Serum Research Institute, Karaj, Iran, ایران
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Authors
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