Purification and characterization of a new α-amylase of intermediate thermal stability from the yeastLipomyces kononenkoae

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 Mfor soluble starch was 0.80 g∙L−1and the kcatwas 622∙s−1. Keywords: α-amylase, glycosylation, intermediate thermal stability, Lipomyces kononenkoae.