Glucoamylase produced by Rhizopus and by a recombinant yeast containing the Rhizopus glucoamylase gene

• Published in: Agricultural and biological chemistry Vol. 50; no. 7; pp. 1737 - 1742
• Main Authors: Tanaka, Y, Ashikari, T, Nakamura, N, Kiuchi, N, Shibano, Y, Amachi, T, Yoshizumi, H
• Format: Journal Article
• Language: English
• Published: Tokyo Taylor & Francis 1986; Agricultural Chemical Society of Japan
• Subjects: Biological and medical sciences; Biotechnology; enzyme activity; Enzyme engineering; enzymes; exo-1,4- alpha -D-glucosidase; Fermentation; Food industries; Fundamental and applied biological sciences. Psychology; genes; genetic recombination; Methods. Procedures. Technologies; production; Production of selected enzymes; Rhizopus; Starch and starchy product industries; Fungi; Enzymatic activity; Rhizopus; Phycomycetes; Ascomycetes; Biosynthesis; Mutation; Properties; Saccharomyces cerevisiae; Thallophyta; Culture medium; Yeast; Purification; Gene expression; Exo-1,4-α-D-glucosidase; Production; Molecular cloning; Amylolytic enzyme
• ISSN: 0002-1369
• DOI: 10.1080/00021369.1986.10867646

Recombinant Rhizopus glucoamylase produced by a yeast containing the Rhizopus glu-coamylase gene was purified, characterized, and compared with native Rhizopus glucoamylase. The recombinant glucoamylase was similar to Gluc 1, one of three forms of Rhizopus native glucoamylase, but it degraded raw starch more efficiently than the native glucoamylase. Recombinant glucoamylase and Gluc 1 adsorbed to gelatinized soluble starch as well as raw starch. These findings suggested that Rhizopus glucoamylase consists of two domains; one for causing adsorption to the starch and the other for catalyzing degradation of the starch molecule.