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- W1995870869 abstract "β-Galactosidase (β-gal) from Kluyveromyces fragilis was immobilized on chitosan-based matrices and agarose beads by different protocols to catalyze the hydrolysis of whole milk lactose in a batch system. The best derivative was obtained by immobilizing the enzyme on chitosan coagulated with KOH and activated with glutaraldehyde, both steps carried out at 50 °C. The immobilization yield and recovered activity were 100%. Maximum activity was achieved at pH 7.0 and 45 °C for both soluble and immobilized β-gal. The maximum β-gal load immobilized on chitosan-glutaraldehyde support was around 21 mg of enzyme per gram of support. Immobilized β-gal was 3–5-fold more stable than the soluble enzyme at 40 and 20 °C, respectively. The biocatalyst retained 80% of its initial activity after 3 months at 10 °C and pH 7.0 in the presence of the cofactors Mn2+ and Mg2+, twice more stable than soluble enzyme. The immobilized biocatalyst was capable to efficiently hydrolyze lactose into the whole milk at 25 °C (above 95% conversion), showing similar performance after four consecutive batches." @default.
- W1995870869 created "2016-06-24" @default.
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- W1995870869 date "2013-12-01" @default.
- W1995870869 modified "2023-10-01" @default.
- W1995870869 title "Hydrolysis of lactose in whole milk catalyzed by β-galactosidase from Kluyveromyces fragilis immobilized on chitosan-based matrix" @default.
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- W1995870869 doi "https://doi.org/10.1016/j.bej.2013.10.007" @default.
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