Refolding of Misfolded Inclusion Bodies of Recombinant α-Amylase: Characterization of Cobalt Activated Thermostable α-Amylase from Geobacillus SBS-4S
نویسندگان
چکیده
منابع مشابه
Molecular Engineering of the Geobacillus stearothermophilus α-Amylase and Cel5E from Chlostridium thermocellim; In Silico Approach
Background: Considering natural thermal stability, Geobacillus stearothermophilus amylase and Cel5E from Clostridium thermocellum are good candidates for industrial applications. To be compatible with the industrial applications, this enzyme should be stable in the high temperatures, so any improvement in their thermal stability is valuable.Objectives: Us...
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Geobacillus stearothermophilus SR74 is a locally isolated thermophilic bacteria producing thermostable and thermoactive α-amylase. Increased production and commercialization of thermostable α-amylase strongly warrant the need of a suitable expression system. In this study, the gene encoding the thermostable α-amylase in G. stearothermophilus SR74 was amplified, sequenced, and subcloned into P. ...
متن کاملProduction of Thermostable α-Amylase and Cellulase from Cellulomonas sp
A bacterium, isolated from rabbit’s waste and identified as Cellulomonas sp., had cellulase and thermostable α-amylase activity when grown on wheat bran. Maximum activity of thermostable α-amylase was obtained by adding 3% soluble starch. However, soybean oil (1 ml l) could increase the production of α-amylase and cellulase in wheat bran. The α-amylase was characterized by making a demonstratio...
متن کاملPurification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1
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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ژورنال
عنوان ژورنال: Pakistan Journal of Zoology
سال: 2018
ISSN: 0030-9923
DOI: 10.17582/journal.pjz/2018.50.3.1147.1155