Purification and Characterization of 6-Phospho-β-galactosidase from Lactobacillus gasseri JCM 1031

Masakatsu Suzuki, Tadao Saito, Takatoshi Itoh

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

6-Phospho-β-galactosidase from Lactobacillus gasseri JCM 1031 was purified from lactobacilli to homogeneity, about 118-fold, with 0.5% recovery by several chromatographies. The molecular mass and isoelectric point of the purified enzyme were 58 kDa and pl 5.5, respectively. The K m and V max for o-nitrophenyl-β-1)-ga- lactopyranoside-6-phosphate were 0.8 mm and 116.4 μmol/min/mg, respectively. Reducing agent, Fe2 + ion, and EDTA activated but PCMB, Zn2 + and Hg2 + ions strongly inhibited the enzymatic activity.

Original languageEnglish
Pages (from-to)139-141
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume60
Issue number1
DOIs
Publication statusPublished - 1996 Jan

Keywords

  • 6-phospho-β-galactosidase
  • Lactohacillus xassai
  • Purification

ASJC Scopus subject areas

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

Fingerprint Dive into the research topics of 'Purification and Characterization of 6-Phospho-β-galactosidase from Lactobacillus gasseri JCM 1031'. Together they form a unique fingerprint.

Cite this