Extracellular alpha-amylase from Streptomyces rimosus.

Abstract:

: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.

authors

Vukelić B,Ritonja A,Renko M,Pokorny M,Vitale L

doi

10.1007/BF00178171

subject

Has Abstract

pub_date

1992-05-01 00:00:00

pages

202-4

issue

2

eissn

0175-7598

issn

1432-0614

journal_volume

37

pub_type

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