Author:
Prieto José Antonio,Bort Bernardo Roque,Martínez Javier,Randez-Gil Francisca,Sanz Pascual,Buesa Carlos
Abstract
A new α-amylase from the extracellular culture of the yeast Lipomyces kononenkoae CBS 5608 has been purified to homogeneity by ammonium sulphate treatment, affinity binding on cross-linked starch, and DEAE–Biogel A chromatography. The enzyme was monomeric, with an apparent Mrof 76 kilodaltons, pI < 3.5, and optimum pH 4.5–5.0, and exhibited intermediate thermal stability. The temperature for optimal enzyme activity was 70 °C. It is a glycoprotein with both N- and O-linked sugars. Kinetic analyses indicate that the enzyme has an endoamylolytic mechanism. The kMfor soluble starch was 0.80 g∙L−1and the kcatwas 622∙s−1. Keywords: α-amylase, glycosylation, intermediate thermal stability, Lipomyces kononenkoae.
Publisher
Canadian Science Publishing
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
43 articles.
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