Hydrolysis of β-Galactosyl Ester Linkage by β-Galactosidases | Zendy

Taro Kiso | Zendy; Hirofumi Nakano | Zendy; Hirofumi NAKAJIMA | Zendy; Tadamasa Terai | Zendy; Katsuyuki Okamoto | Zendy; Sumio Kitahata | Zendy

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Hydrolysis of β-Galactosyl Ester Linkage by β-Galactosidases

Author(s) -

Taro Kiso,

Hirofumi Nakano,

Hirofumi NAKAJIMA,

Tadamasa Terai,

Katsuyuki Okamoto,

Sumio Kitahata

Publication year - 2000

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.64.1702

Subject(s) - bacillus circulans , hydrolysis , chemistry , beta galactosidase , galactoside , galactose , galactosidases , enzyme , substrate (aquarium) , stereochemistry , biochemistry , aspergillus oryzae , escherichia coli , organic chemistry , biology , ecology , gene

p-Hydroxybenzoyl beta-galactose (pHB-Gal) was synthesized chemically to examine the hydrolytic activity of beta-galactosyl ester linkage by beta-galactosidases. The enzyme from Penicillium multicolor hydrolyzed the substrate as fast as p-nitrophenyl beta-galactoside (pNP-Gal), a usual substrate with a beta-galactosidic linkage. The enzymes from Escherichia coli and Aspergillus oryzae hydrolyzed pHB-Gal with almost the same rates as pNP-Gal. The enzymes from Bacillus circulans, Saccharomyces fragilis, and bovine liver showed much lower activities. pH-activity profiles, inhibition analysis, and kinetic properties of the enzymic reaction on pHB-Gal suggested that beta-galactosidase had only one active site for hydrolysis of both galactosyl ester and galactoside. The Penicillium enzyme hydrolyzed pHB-Gal in the presence of H218O to liberate galactose containing 18O. This result suggests the degradation occurs between the anomeric carbon and an adjacent O atom in the ester linkage of pHB-Gal.

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