Entrapment of beta-galactosidase in polyvinylalcohol hydrogel.

Abstract:

:beta-Galactosidase isolated from Aspergillus oryzae was immobilized in lens-shaped polyvinylalcohol capsules (with activity 25 U g(-1)) giving 32% of its original activity. Immobilization did not change the pH optimum (4.5) of lactose hydrolysis. The relative enzyme activity during product inhibition testing was, in average, 10% higher for immobilized enzyme. No decrease of activity was observed after 35 repeated batch runs and during 530 h of continuous hydrolysis of lactose (10%, w/v) at 45 degrees C. The immobilized enzyme was stable for 14 months without any change of activity during the storage at 4 degrees C and pH 4.5.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Grosová Z,Rosenberg M,Rebros M,Sipocz M,Sedlácková B

doi

10.1007/s10529-007-9606-0

subject

Has Abstract

pub_date

2008-04-01 00:00:00

pages

763-7

issue

4

eissn

0141-5492

issn

1573-6776

journal_volume

30

pub_type

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