Summary
A p-nitrophenyl-α-d-glucopyranosidase from Bacillus thermoamyloliquefaciens KP 1171 capable of growing at 30°–66°C was assigned to an oligo-1,6-glucosidase (dextrin 6-α-d-glucanohydrolase, EC 3.2.1.10). The enzyme was compared with its homologous counterparts from B. cereus NY-14, B. cereus ATCC 7064 (each mesophile), B. coagulans ATCC 7050 (facultative thermophile), B. thermoglucosidasius KP 1006 (DSM 2542, obligate thermophile) and B. flavocaldarius KP 1228 (extreme thermophile) in thermostability and kinetic parameters at suboptimal temperatures for isomaltosaccharides (2–6 glucose units). This analysis showed that the efficiency of each isomaltosaccharide hydrolysis changes in a convex manner with increasing thermostability on the transition, NY-14 → ATCC 7064 → ATCC 7050 → KP 1071 → KP 1006 → KP 1228 enzymes, with a maximum at KP 1071 or ATCC 7050 enzyme.
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Suzuki, Y., Oishi, K. A relationship between efficiency of isomaltosaccharide hydrolysis and thermostability of six Bacillus oligo-1,6-glucosidases. Appl Microbiol Biotechnol 31, 32–37 (1989). https://doi.org/10.1007/BF00252522
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DOI: https://doi.org/10.1007/BF00252522