ρ-Nitrophenyl Glycoside-hydrolyzing Activities in Bifidobacteria and Characterization of β-D-Galactosidase of Bifidobacterium longum 401

Tatsurokuro Tochikura, Kenji Sakai, Takako Fujiyoshi, Takashi Tachdci, Hidehiko Kumagai

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Bifidobacteria showed higher hydrolyzing activity toward various p-nitrophenyl glycosides (p-NP glycosides) than some other intestinal bacteria. The reactions commonly found in the organisms involved p-NP β-D-galactoside, ρ-NP a-D-glucoside and p-NP β-D-fucoside. Analysis of the enzyme species suggested that the β-D-fucoside-hydrolyzing reaction, which is undetectable in other bacteria, was catalyzed by β-D-galactosidase in many bifidobacteria and by- β-D-glucosidase in some strains. β-D-Galactosidase, which hydrolyzed ρ-NP β-D-fucoside (with 12% of its reactivity to p-NP β-D-galactoside), was purified to homogeneity from Bifidobacterium longum 401. The enzyme was distinct from other bacterial β-D-galactosidases in its higher activity toward lactulose than lactose and the insensitivity of its formation to the carbon source in the culture medium. Some properties of the β-D-galactosidase are described and compared with those of the lactase from the same organism.

Original languageEnglish
Pages (from-to)2279-2286
Number of pages8
JournalAgricultural and Biological Chemistry
Volume50
Issue number9
DOIs
Publication statusPublished - Jan 1 1986
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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