Hydrolysis of β-Galactosyl Ester Linkage by β-Galactosidases

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概要

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• p-Hydroxybenzoyl β-galactose (pHB-Gal) was synthesized chemically to examine the hydrolytic activity of β-galactosyl ester linkage by β-galactosidases. The enzyme from Penicillium multicolor hydrolyzed the substrate as fast as p-nitrophenyl β-galactoside (pNP-Gal), a usual substrate with a β-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 β-galactosidase had only one active site for hydrolysis of both galactosyl ester and galactoside. The Penicillium enzyme hydrolyzed pHB-Gal in the presence of H_2^<18>O to liberate galactose containing ^<18>O. This result suggests the degradation occurs between the anomeric carbon and an adjacent O atom in the ester linkage of pHB-Gal.

• 社団法人日本農芸化学会の論文
• 2000-08-23

著者

• KITAHATA Sumio

  Osaka Municipal Technical Research Institute

• KISO TARO

  Osaka Municipal Technical Research Institute

• NAKANO HIROFUMI

  Osaka Municipal Technical Research Institute, and Yashiro Co, Ltd.,

• Kitahata S

  Department Of Bioscience And Biotecnology Shinshu University

• OKAMOTO KATSUYUKI

  Showa Sangyo Co. Ltd.

• NAKAJIMA Hirofumi

  Osaka Institute of Technology

• TERAI Tadamasa

  Osaka Institute of Technology

• Kiso Taro

  Department Of Biochemistry Osaka Municipal Technical Research Institute

• Kobayashi S

  Fukui Univ. Technol. Fukui Jpn

• Nakano H

  Department Of Biochemistry Osaka Municipal Technical Research Institute

• Nakano H

  Kyoto Prefectural Univ. Kyoto Jpn

• Okamoto K

  Showa Sangyo Co. Ltd.

• Nakano Hirofumi

  Osaka Municipal Technical Research Institute

• Nakano Hirofumi

  Department Of Chemistry Faculty Of Science Osaka University

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