Partial purification of ?-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems
نویسندگان
چکیده
منابع مشابه
One-step purification of alpha-amylase from the cultivation supernatant of recombinant bacillus subtilis by high-speed counter-current chromatography with aqueous polymer two-phase systems.
Purification of alpha-amylase from the cultivation supernatant of recombinant Bacillus subtilis by high-speed counter-current chromatography (HSCCC) in polyethylene glycol (PEG) 4000-inorganic salt aqueous polymer two-phase systems was studied. The effects of sodium chloride concentration on the partition coefficients of alpha-amylase and total protein were respectively tested in PEG4000-phosph...
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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 120 h, temperature of 37 °C and pH 7.0. The α-amylase enzyme was purified by ion exchange chromatography ...
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چکیده پلاتین، فلزی نجیب، پایدار و گران قیمت با خاصیت کاتالیزوری زیاد است که کاربرد های صنعتی فراوانی دارد. کمپلکس های پلاتین(ii) به عنوان دارو های ضد سرطان شناخته شدند و در شیمی درمانی بیماران سرطانی کاربرد دارند. خاصیت کاتالیزوری و عملکرد گزینشی پلاتین مستقیماً به اندازه و- شکل ماده ی پلاتینی بستگی دارد. بعضی از نانو ذرات فلزی در سطح مشترک مایع- مایع سنتز شده اند، اما نانو ساختار های پلاتین ب...
Production and Partial Purification of Alpha Amylase from Bacillus subtilis (MTCC 121) Using Solid State Fermentation
Amylase is an enzyme that catalyzes the breakdown of starch into sugars and plays a pivotal role in a variety of areas like use as digestives, for the production of ethanol and high fructose corn syrup, detergents, desiring of textiles, modified starches, hydrolysis of oil-field drilling fluids, and paper recycling. In the present work, solid state fermentation (SSF) for α -amylase production h...
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An extracellular α-amylase from Bacillus subtilis KIBGEHAS was partially purified by ultrafiltration and ammonium sulphate precipitation with 19.2-fold purification and specific activity of 4195 U/mg. The enzyme showed relatively high thermostability and retained 62% of its activity when kept at 70°C for 15 min. α -Amylase was highly stable at −18°C and loss of activity was very low during stab...
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ژورنال
عنوان ژورنال: Bioprocess and Biosystems Engineering
سال: 2004
ISSN: 1615-7591,1615-7605
DOI: 10.1007/s00449-004-0369-x