Hydrolytic action on the mixture of maltose and soluble starch by α-glucosidase from mucor javanicus ifo 4570

Manabu Sugimoto; Yukio Suzuki

doi:10.1080/bbb.58.1535

Hydrolytic action on the mixture of maltose and soluble starch by α-glucosidase from mucor javanicus ifo 4570

Manabu Sugimoto, Yukio Suzuki

Institute of Plant Science and Resources

Research output: Contribution to journal › Comment/debate › peer-review

7 Citations (Scopus)

Abstract

The active site of α-glucosidase from Mucor javanicus IFO 4570 was investigated by kinetic studies. Competition between maltose and soluble starch, and linearity of Lineweaver-Burk plots for the mixed substrates were observed. The dependence of the apparent maximum velocities agreed with those predicted for a single active site mechanism. These results suggest that the enzyme hydrolyzes maltose and soluble starch at a single active site.

Original language	English
Pages (from-to)	1535-1536
Number of pages	2
Journal	Bioscience, Biotechnology and Biochemistry
Volume	58
Issue number	8
DOIs	https://doi.org/10.1080/bbb.58.1535
Publication status	Published - Jan 1994

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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abstract = "The active site of α-glucosidase from Mucor javanicus IFO 4570 was investigated by kinetic studies. Competition between maltose and soluble starch, and linearity of Lineweaver-Burk plots for the mixed substrates were observed. The dependence of the apparent maximum velocities agreed with those predicted for a single active site mechanism. These results suggest that the enzyme hydrolyzes maltose and soluble starch at a single active site.",

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AB - The active site of α-glucosidase from Mucor javanicus IFO 4570 was investigated by kinetic studies. Competition between maltose and soluble starch, and linearity of Lineweaver-Burk plots for the mixed substrates were observed. The dependence of the apparent maximum velocities agreed with those predicted for a single active site mechanism. These results suggest that the enzyme hydrolyzes maltose and soluble starch at a single active site.

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Hydrolytic action on the mixture of maltose and soluble starch by α-glucosidase from mucor javanicus ifo 4570

Abstract

ASJC Scopus subject areas

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