Purification and Characterization of α-Amylase from Bacillus licheniformis CUMC305
نویسندگان
چکیده
منابع مشابه
Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis
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 ...
متن کاملtwo-step purification and partial characterization of an extra cellular α-amylase from bacillus licheniformis
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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This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...
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Background: a-Amylases (EC 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries. Objectives: The first ever detailed characterization of amylase from any halophilic Engyodontium album is presented. Materials and Methods: An extracellular α-amylase was studied from halophilic E. album TISTR 3645. The enzyme was e...
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Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1983
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.46.2.430-437.1983