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Purification and Characterization of Extremely Thermostable Exo ‐oligo‐1,6‐glucosidase from a Caldoactive Bacillus sp. KP 1228
Author(s) -
Suzuki Y.,
Fujii H.,
Uemura H.,
Suzuki M.
Publication year - 1987
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19870390106
Subject(s) - thermostability , thermophile , bacillus cereus , bacillus coagulans , enzyme , mesophile , bacillales , bacillus (shape) , bacillaceae , biochemistry , biology , hyperthermophile , chemistry , bacteria , microbiology and biotechnology , bacillus subtilis , archaea , genetics , fermentation , gene
A p ‐nitrophenyl‐α‐ D ‐glycopyranoside‐hydrolyzing oligo‐1,6‐glucosidase (dextrin 6‐α‐glucanohydrolase, EC 3.2.1.10) of a caldoactive Bacillus sp. KP 1228 capable of growing at 51–82°C was purified to homogeneity. The molecular weight was estimated as 140,000. The enzyme consisted of two identical subunits each comprising a threonine residue at the NH 2 ‐terminus. The enzyme was most active at 85°C and pH 5.1, and stable for 10 min up to 85°C at pH 6.8. The enzyme had no antigenic determinant common to oligo‐1,6‐glucosidases from Bacillus cereus ATCC 7064 (mesophile), Bacillus coagulans ATCC 7050 (facultative thermophile) and Bacillus thermoglucosidasius KP 1006 (DSM 2542) (obligate thermophile). A strong correlation between the increase in proline content and the rise in thermostability of these 4 proteins was observed.