Expression of a secretory α-glucosidase II from Apis cerana indica in Pichia pastoris and its characterization

• Published in: BMC biotechnology Vol. 13; no. 1; p. 16
• Main Authors: Kaewmuangmoon, Jirattikarn, Kilaso, Manlika, Leartsakulpanich, Ubolsree, Kimura, Kiyoshi, Kimura, Atsuo, Chanchao, Chanpen
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 18.02.2013; BioMed Central
• Subjects: alpha-Glucosidases - chemistry; alpha-Glucosidases - genetics; alpha-Glucosidases - metabolism; Amino Acid Sequence; Amino acids; Animals; API; Apis cerana indica; Apis mellifera; Bees - enzymology; Encoding; Enzymes; Gene Expression; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Nucleotides; Optimization; Pichia - metabolism; Pichia pastoris; Protein Isoforms - chemistry; Protein Isoforms - genetics; Protein Isoforms - metabolism; Recombinant Proteins - biosynthesis; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Sequence Alignment; Substrate Specificity; Temperature

α-glucosidase (HBGase) plays a key role in hydrolyzing α-glucosidic linkages. In Apis mellifera, three isoforms of HBGase (I, II and III) have been reported, which differ in their nucleotide composition, encoding amino acid sequences and enzyme kinetics. Recombinant (r)HBGase II from A. cerana indic...