Ontology highlight
ABSTRACT:
SUBMITTER: Ali I
PROVIDER: S-EPMC4477103 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Ali Imran I Ali Imran I Akbar Ali A Anwar Mohammad M Prasongsuk Sehanat S Lotrakul Pongtharin P Punnapayak Hunsa H
BioMed research international 20150609
An extracellular α-amylase from the obligate halophilic Aspergillus penicillioides TISTR3639 strain was produced and enriched to apparent homogeneity by ammonium sulfate precipitation and Sephadex G100 gel filtration column chromatography. The mass of the purified amylase was estimated to be 42 kDa by SDS-PAGE. With soluble starch as the substrate it had a specific activity of 118.42 U · mg(-1) and Vmax and Km values of 1.05 µmol · min(-1) · mg(-1) and 5.41 mg · mL(-1), respectively. The enzyme ...[more]