Abstract

AbstractA p‐nitrophenyl‐α‐D‐glucopyranoside‐hydrolyzing exo‐oligo‐ 1,6‐glucosidase (dextrin 6‐α‐glucanohydrolase, EC. 3.2.1.10) of a thermophile Bacillus thermoglucosidius was purified to an electrophoretically homogeneous form with a yield of 47% by a rapid and simple four‐step procedure including the enzyme desorption from immunoadsorbents by 3‐M NaSCN. Its specific activity was 421 μmol p‐nitrophenyl‐α‐D‐glucopyranoside hydrolyzed/min/mg protein at 60° C and pH 6.8. The aminoterminal amino acid of the enzyme was determined as methionine.

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