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Prikl Biokhim Mikrobiol ; 37(2): 202-8, 2001.
Article in Russian | MEDLINE | ID: mdl-11357426

ABSTRACT

Glucoamylase from Aspergillus awamori 466 was immobilized on various supports. The enzyme sorption depends on its amount, the type of support, and immobilization conditions. The kinetics of acidic inactivation of the native and immobilized enzyme was studied. The immobilized enzyme was more resistant to temperature and pH. The mechanism of the enzyme binding to the support was investigated by IR spectroscopy.


Subject(s)
Aspergillus/enzymology , Enzymes, Immobilized/isolation & purification , Glucan 1,4-alpha-Glucosidase/isolation & purification , Catalysis , Hydrogen-Ion Concentration , Temperature
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