P-nitrophenyl glycoside-hydrolyzing activities in bifidobacteria and characterization of β-d-galactosidaseof bifidobacterium longum 401

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

Research output: Contribution to journalArticle

66 Citations (Scopus)


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, p-NP α-D-glucoside and p-NP β-D-fucoside. Analysis of the enzymespecies suggested that the β-D-fucoside-hydrolyzing reaction, which is undetectable in otherbacteria, was catalyzed by β-D-galactosidase in many bifidobacteria and by- β-D-glucosidase in somestrains. β-D-Galactosidase, which hydrolyzed p-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 lactoseand the insensitivity of its formation to the carbon source in the culture medium. Some properties ofthe β-D-galactosidase are described and compared with those of the lactase from the sameorganism.

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


All Science Journal Classification (ASJC) codes

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

Cite this