1887

Abstract

Summary: α-Glucosidase has been purified from culture fluid and from lysed cells of NCIB 6346. The enzymes from these two sources were virtually identical in molecular weight as judged by SDS-PAGE (63 000) and catalytic properties. The enzymes were unstable at high temperature and lost all activity after incubation at 60 °C for 10 min. Of the substrates examined, isomaltose gave maximal activity, followed by maltotriose, -nitrophenyl α-D-glucopyranoside, sucrose and maltose. With isomaltose or maltotriose as substrate, transglucosylation activity was evident.

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/content/journal/micro/10.1099/00221287-130-12-3135
1984-12-01
2019-10-22
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-130-12-3135
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