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 language | English |
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Pages (from-to) | 495-499 |
Number of pages | 5 |
Journal | Bioscience, Biotechnology and Biochemistry |
Volume | 70 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2006 |
Externally published | Yes |
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