Molecular Cloning and Characterization of an α-Amylase fromPichia burtonii15-1

• DOI: 10.1271/bbb.70407
• Publication Date: 2007-12-25T05:49:39Z
• Authors: Saemi KATO; Akiko SHIMIZU-IBUKA; Kiyoshi MURA; Akiko TAKEUCHI; Chiyoko TOKUE; Soichi ARAI
• Keywords: Enzyme Kinetics; Aspergillus oryzae; Pichia

An α-amylase secreted by Pichia burtonii 15-1 isolated from a traditional starter murcha of Nepal, named (PBA), was studied. The gene cloned and its nucleotide sequence determined. PBA deduced to consist 494 amino acid residues. It shared certain degrees identity with other homologous proteins: 60% Schwanniomyces occidentalis α-amylase, 58% Saccharomycopsis sp. 47% Taka-amylase A Aspergillus oryzae. three-dimensional structural model generated using the known structure as template suggested high similarity between them. Kinetic analysis revealed that Km values were lower than those for oligosaccharides. Although kcat oligosaccharide substrates, kcat/Km higher.