Extracellular α-amylase from Streptomyces rimosus

A purification procedure for an extracellular alpha-amylase from Streptomyces rimosus, oxytetracycline-producing strain, is described. The enzyme obtained was shown to be an acidic (pI 4.75) monomer with a relative molecular mass (M(r)) of 43,000, containing three cysteines involved in the catalytic...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1992-05, Vol.37 (2), p.202-204
Main Authors: VUKELIC, B, RITONJA, A, RENKO, M, POKORNY, M, VITALE, L
Format: Article
Language:English
Subjects:
activity
alpha -amylase
alpha-Amylases - chemistry
alpha-Amylases - isolation & purification
alpha-Amylases - metabolism
Amino Acid Sequence
Biological and medical sciences
Biotechnology
Calcium - metabolism
characterization
Cysteine - chemistry
Enzyme engineering
extracellular enzymes
Fundamental and applied biological sciences. Psychology
Improved methods for extraction and purification of enzymes
Isoelectric Point
Methods. Procedures. Technologies
Molecular Sequence Data
Molecular Weight
purification
Streptomyces - enzymology
Streptomyces rimosus
Temperature
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Summary:A purification procedure for an extracellular alpha-amylase from Streptomyces rimosus, oxytetracycline-producing strain, is described. The enzyme obtained was shown to be an acidic (pI 4.75) monomer with a relative molecular mass (M(r)) of 43,000, containing three cysteines involved in the catalytic activity of the enzyme. Its amino-terminal part has 57-67% homology with amylases from other Streptomyces species. S. rimosus alpha-amylase is sensitive to higher temperatures, and partially stabilized by Ca2+ ions. It hydrolyses starch (optimum at pH 5.0-6.0) in an endohydrolase manner giving rise to maltotriose, maltotetraose and higher oligosaccharides. Starch granules, except those from rice, were not significantly affected by the isolated alpha-amylase.
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00178171