Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus
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چکیده
منابع مشابه
Cloning 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 کاملEnzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis.
BACKGROUND The maltogenic amylase from Bacillus stearothermophilus (BSMA) is a valuable biocatalyst that has been used to transglycosylate natural glycosides to improve solubility. To ensure safety, BSMA was produced in Bacillus subtilis, using new shuttle vector-based expression vectors. The transglycosylation of puerarin was also conducted with crude BSMA and analyzed. RESULTS Two expressio...
متن کاملInduction of Alpha-amylase of Bacillus Stearothermophilus by Maltodextrins.
Welker, N. E. (Western Reserve University, Cleveland, Ohio) and L. Leon Campbell. Induction of alpha-amylase of Bacillus stearothermophilus by maltodextrins. J. Bacteriol. 86:687-691. 1963.-Technical-grade maltose contained 3.5% glucose, 0.5% maltotriose, and 2.5% of the higher molecular weight maltodextrins. The first five homologues (maltose being the first in the series) of the maltodextrin ...
متن کاملThermostable a-Amylase of Bacillus stearothermophilus
Some general and physical properties and the’ amino acid composition of the thermostable cr-amylase of Bacillus sbarothermophilus have been described in previous papers (l-3). In an effort to further correlate the thermostability of this enzyme with its molecular organization, a study of the structure of this protein has been undertaken. In this paper are reported the results of an investigatio...
متن کاملX-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
The three-dimensional structure of the Bacillus stearothermophilus "maltogenic" alpha-amylase, Novamyl, has been determined by X-ray crystallography at a resolution of 1.7 A. Unlike conventional alpha-amylases from glycoside hydrolase family 13, Novamyl exhibits the five-domain structure more usually associated with cyclodextrin glycosyltransferase. Complexes of the enzyme with both maltose and...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1988
ISSN: 0378-1097
DOI: 10.1016/0378-1097(88)90126-7