Molecular cloning and characterization of an enzyme hydrolyzing p-nitrophenyl α-D-glucoside from Bacillus stearothermophilus SA0301

Atsushi Kobayashi, Takashi Tonozuka, Kimihiko Sato, Mikita Suyama, Jun Sasaki, Batbold Nyamdawaa, Masayoshi Sakaguchi, Yoshiyuki Sakano

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Bacillus stearothermophilus SA0301 produces an extracellular oligo-1,6-glucosidase (bsO16G) that also hydrolyzes p-nitrophenyl α-D-glucoside (Tonozuka et al., J. Appl. Glycosci., 45, 397-400 (1998)). We cloned a gene for an enzyme hydrolyzing p-nitrophenyl α-D-glucoside, which was different from the one mentioned above, from B. stearothermophilus SA0301. The k0/Km values of bsO16G for isomaltotriose and isomaltose were 13.2 and 1.39 s-1·mM-1 respectively, while the newly cloned enzyme did not hydrolyze isomaltotriose, and the k0/Km value for isomaltose was 0.81 s -1·mM-1. The primary structure of the cloned enzyme more closely resembled those of trehalose-6-phosphate hydrolases than those of oligo-1,6-glucosidases, and the cloned enzyme hydrolyzed trehalose 6-phosphate. An open reading frame encoding a protein homologous to the trehalose-specific IIBC component of the phopshotransferase system was also found upstream of the gene for this enzyme.

Original languageEnglish
Pages (from-to)495-499
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Volume70
Issue number2
DOIs
Publication statusPublished - 2006 Mar 2

Keywords

  • Bacillus stearothermophilus SA0301
  • Isomaltooligosaccharide
  • Oligo-1,6-glucosidase
  • Trehalose-6-phosphate hydrolase
  • p-nitrophenyl α-D-glucoside

ASJC Scopus subject areas

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

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