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...

Bacillus sp. GUF8, isolated from acidic soil samples of a tea farm was identified as Bacillus cereus, based on 16S rDNA sequencing and standard bacterial identification methods. Following optimization of enzyme production, the resulting α-amylase was purified by acetone precipitation and ion exchange chromatography. Consequently, thermostability and kinetic parameters of the purified enzyme wer...

bacillus sp. guf8, isolated from acidic soil samples of a tea farm was identified as bacillus cereus, based on 16s rdna sequencing and standard bacterial identification methods. following optimization of enzyme production, the resulting α-amylase was purified by acetone precipitation and ion exchange chromatography. consequently, thermostability and kinetic parameters of the purified enzyme wer...

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...

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 ...

Studies on the irreversible thermoinactivation of beta-amylase from Bacillus megaterium B6 exposed to 60 degrees C revealed that the deactivation mechanism probably results from the oxidation of thiols present at the active site of the enzyme. Several attempts were made to increase its thermostability, which indicated that Mn2+ played a key role in determining thermostability and partially reac...

Alpha-amylase E.C.3.2.1.1. (1,4 glucan, 4 glucanohydrolase) can be obtained from salivary glands, pancreas and microorganisms such as Pseudomonas and Asperigllus, as well as muscles and ovarian tubes.1.2 Alpha-amylase from Bacillus Subtilis #1024(A TCC 465)* was purified with a highest degree of purity in our laboratory (31.59 U/mg). The extracellular alpha-amylase was subjected to differe...

BACKGROUND Alpha amylase hydrolyzes α-bonds of polysaccharides such as starch and produces malto-oligosaccharides. Its starch saccharification applications make it an essential enzyme in the textile, food and brewing industries. Commercially available α-amylase is mostly produced from Bacillus or Aspergillus. A hyper-thermostable and Ca 2++ independent α-amylase from Pyrococcus furiosus (PFA) e...

alpha-amylase e.c.3.2.1.1. (1,4 glucan, 4 glucanohydrolase) can be obtained from salivary glands, pancreas and microorganisms such as pseudomonas and asperigllus, as well as muscles and ovarian tubes.1.2 alpha-amylase from bacillus subtilis #1024(a tcc 465)* was purified with a highest degree of purity in our laboratory (31.59 u/mg). the extracellular alpha-amylase was subjected to different pu...

Bacterial amylase from Bacillus subtilis and fungal amylase from Aspergillus niger were potential source for industrial exploitation in the field of amylase production. Hence, this study on bacterial amylase and fungal amylase was done to compare the kinetic parameter of both the types of amylases. 30-60% ammonium sulfate precipitation has done which showed 90 % of purification of both the part...