Extraction, Purification and Characterization of Thermostable, Alkaline Tolerant α-Amylase from Bacillus cereus

Purification 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...

purification and characterization of an extracellular thermostable alkaline α-amylase from the moderately halophilic bacterium, bacillus persicus

background: today a large number of bacterial amylases are available commercially in industry. the goal of the present study was purification and biochemical characterization of an extracellular thermostable alkaline α-amylase from the novel moderately halophilic, bacillus persicus from the aran-bidgol, iran.   methods : purification of enzyme, was carried out by acetone precipitation, ultrafil...

Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

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 ...

Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68

An alkaliphilic and highly thermostable α-amylase producing Bacillus sp. was isolated from Van soda lake. Enzyme synthesis occurred at temperatures between 25°C and 40°C. Analysis of the enzyme by SDS-PAGE revealed a single band which was estimated to be 66 kDa. The enzyme was active in a broad temperature range, between 20°C and 90°C, with an optimum at 50°C; and maximum activity was at pH 10....