Expression of alpha-amylase in Bacillus licheniformis
نویسندگان
چکیده
منابع مشابه
Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase.
The irreversible thermal inactivation of Bacillus licheniformis alpha-amylase was studied. A two-step behaviour in the irreversible denaturation process was found. Our experimental results are consistent only with the two-step model and rule out the two-isoenzyme one. They suggest that the deactivation mechanism involves the existence of a temperature-dependent intermediate form. Therefore the ...
متن کاملMutagenesis of Bacillus Licheniformis through Ethyl Methanesulfonate for Alpha Amylase Production
The present study is concerned with the improvement of Bacillus licheniformis strain GCB30 for alpha amylase production in 250 ml Erlenmeyer flasks. Chemical mutation using ethyl methanesulfonate (EMS 50-300 μ/ml) was undertaken for 10-60 min. Twenty eight isolates were selected on the basis of clear zones of starch hydrolysis. Only one isolate designated as B. licheniformis EMS-200 gave 102.78...
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 ...
متن کاملSolid State Fermentation of a Raw Starch Digesting Alkaline Alpha-Amylase from Bacillus licheniformis RT7PE1 and Its Characteristics
The thermodynamic and kinetic properties of solids state raw starch digesting alpha amylase from newly isolated Bacillus licheniformis RT7PE1 strain were studied. The kinetic values Q p , Y p/s , Y p/X , and q p were proved to be best with 15% wheat bran. The molecular weight of purified enzyme was 112 kDa. The apparent K m and V max values for starch were 3.4 mg mL(-1) and 19.5 IU mg(-1) prote...
متن کاملCloning and Expression of Thermostable alpha-Amylase Gene from Bacillus stearothermophilus in Bacillus stearothermophilus and Bacillus subtilis.
The structural gene for a thermostable alpha-amylase from Bacillus stearothermophilus was cloned in plasmids pTB90 and pTB53. It was expressed in both B. stearothermophilus and Bacillus subtilis. B. stearothermophilus carrying the recombinant plasmid produced about fivefold more alpha-amylase (20.9 U/mg of dry cells) than did the wild-type strain of B. stearothermophilus. Some properties of the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1986
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.168.2.839-842.1986