Comparison of Thermal and Guanidine Hydrochloride Denaturation Behaviors of Glucoamylase from the STA1 Gene of Saccharomyces cerevisiae var. diastaticus

Shin ONO; Sumie TANPA; Isao YAMAZAKI; Toshiaki YOSHIMURA; Toshihiko MATSUMOTO; Izumi YAMAURA; Tetsuo KATO; Ichiro YAMASHITA; Choichiro SHIMASAKI

doi:10.1271/bbb.60.1543

Shin ONO, Sumie TANPA, Isao YAMAZAKI, Toshiaki YOSHIMURA, Toshihiko MATSUMOTO, Izumi YAMAURA, Tetsuo KATO, Ichiro YAMASHITA, Choichiro SHIMASAKI

Author information

Shin ONO
Sumie TANPA
Isao YAMAZAKI
Toshiaki YOSHIMURA
Toshihiko MATSUMOTO
Izumi YAMAURA
Tetsuo KATO
Ichiro YAMASHITA
Choichiro SHIMASAKI
Author's Organization：
Department of Chemical and Biochemical Engineering, Toyama University
Department of Chemical and Biochemical Engineering, Toyama University
Yayoi Kagaku Kogyo Co., Ltd.
Department of Chemical and Biochemical Engineering, Toyama University
Department of Applied Microbial Technology, Kumamoto Institute of Technology
Department of Applied Microbial Technology, Kumamoto Institute of Technology
Department of Applied Microbial Technology, Kumamoto Institute of Technology
Center for Gene Science, Hiroshima University
Department of Chemical and Biochemical Engineering, Toyama University

Keywords: S. diastaticus glucoamylase, thermal denaturation, guanidine hydrochloride denaturation, circular dichroism spectroscopy, fluorescence spectroscopy

JOURNAL FREE ACCESS

1996 Volume 60 Issue 9 Pages 1543-1545

DOI https://doi.org/10.1271/bbb.60.1543

Details

Abstract

To investigate the relationships between enzyme inactivation and conformational change, the effects of heat and guanidine hydrochloride (GnHCl) on the STA1 gene glucoamylase (STA1GA) of Saccharomyces cerevisiae var. diastaticus were examined by circular dichroism and fluorescence spectroscopies. A conformational change was observed in the thermal denaturation of STA1GA, while extensive enzyme inactivation occurred in GnHCl denaturation before noticeable conformational change.

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