Abstract
A p-nitrophenyl-α-D-glucopyranoside-hydrolyzing exo-oligo-1,6-glucosidase (dextrin 6-α-glucanohydrolase, EC.3.2.1.10) of Bacillus cereus ATCC 7064 was 1,120-fold purified to an electrophoretically- and immunologically-homogeneous form by a simple 4-step method containing as the most efficient step the enzyme elution from immunosorbent with a pH 11 medium including 50% (w/v) glycerol. The final enzyme yield was 47%. The specific activity was 218 μmol p-nitrophenyl-α-D-glucopyranoside hydrolyzed/min/mg protein at 35°C and pH 6.8. The amino-terminal amino acid of the enzyme was determined to be methionine. No antigenic common determinant occurred between this enzyme and each of its homologous counterparts from obligate thermophile Bacillus thermoglucosidius KP 1006 and from facultative thermophile Bacillus coagulans ATCC 7050.
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