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STABILIZATION OF THE ACTIVITY OF β‐GALACTOSIDASE IN PERMEABILIZED IMMOBILIZED CELLS FOR HYDROLYSIS OF LACTOSE IN MILK
Author(s) -
JORDãO RIANA EARROSO,
BRANDI IGOR VIANA,
PASSOS FLÁVIA MARIA LOPES
Publication year - 2001
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2001.tb00738.x
Subject(s) - calcium alginate , kluyveromyces lactis , lactose , chemistry , hydrolysis , kluyveromyces , glycerol , chromatography , calcium , immobilized enzyme , yeast , biocatalysis , enzyme , food science , biochemistry , catalysis , organic chemistry , saccharomyces cerevisiae , ionic liquid
A potentially low cost β‐galactosidase was prepared as a crude permeabil‐ized cell mass of the yeast Kluyveromyces lactis that had been grown in ultrafiltered cheese whey. The enzyme preparation was immobilized in alginate beads. Milk lactose hydrolysis rates were 25% higher in manganese alginate beads than in calcium alginate beads. The immobilized biocatalyst lost activity when stored in calcium chloride solution, however, storage in 5 mM DTT or 50% glycerol allowed the biocatalyst to be recycled at least 5 times without any loss of activity.