PMID: 38548Jul 1, 1979

Immobilization of aspergillus oryzae aminopeptidase on organic and inorganic carriers

Ukrainskiĭ biokhimicheskiĭ zhurnal
M V KolodzeĭskaiaS V Verbilenko

Abstract

The process of Asp. oryzae aminopeptidase immobilization on organic (AE-cellulose, sepharose 4B, Sephadex G-200) and inorganic (SCh-2, SCh-3 sylochromes and KCK N 1 silicagel) carriers was studied. Aminopeptidase immobilized on Sephadex G-200 contains the largest amount of protein (80 mg per 1 g of carrier) and is the most active of all other preparations. The immobilized preparations retain the temperature optimum, like the soluble form, at 60 degrees C, except the preparation immobilized on AE-cellulose (50 degrees C). At temperatures of 70, 80 degrees C the obtained preparations are more thermostable than the initial enzyme. The pH-stability zone for the preparations immobilized by means of sylochrome-3 and Sephadex G-200 is wider to some extent as compared to the soluble enzyme. When studying the substrate specificity it is established that leucyl-glycyl-glycine is the best substrate for both the soluble form and the immobilized preparations. Multiple application of the immobilized aminopeptidase is shown to be possible.

Related Concepts

Aminopeptidase
Aspergillus
Aspergillus oryzae
Sulfite Cellulose
Drug Stability
Hydrogen-Ion Concentration
Sepharose
Quso G-32

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