Naslov
Extracellular alpha-amylase from Streptomyces rimosus

Autori
Vukelić, Bojana ; Ritonja, Anka ; Renko, Metka ; Pokorny, Mišo ; Vitale, Ljubinka

Izvornik
Applied microbiology and biotechnology (0175-7598) 37 (1992); 202-204

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
alpha-amylase ; Streptomyces rimosus ; purification ; characterization

Sažetak
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 (Mr) 43 000, containing three cysteins 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 givimg rise to maltotriose, maltotetraose and higher oligosaccharides. Starch granules, except those from rice, were not significantly affected by the isolated alpha-amylase.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA