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Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis

✍ Scribed by Quinn Z.K Zhou; Xiao Dong Chen

Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
222 KB
Volume
9
Category
Article
ISSN
1369-703X

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✦ Synopsis

A study of the cross-linking immobilization of ␤-galactosidase from Kluyveromyces lactis on graphite surfaces is reported here. The cross-linking reagent was glutaraldehyde. Thermal deactivation of the immobilized enzyme at the temperatures from 35 to 55 • C was investigated, and the deactivation rate was found to follow the Arrhenius law with the activation energy of about 200 kJ mol -1 for the deactivation of the immobilized enzyme. The temperature-activity curves are similar for both the free and immobilized enzyme. However, the maximum activity of the immobilized enzyme was shifted up from 40 • C to 50 • C compared with that of the free enzyme. The pH for the maximum activity of the immobilized enzyme to occur has been found to increase by 1.1 to 7.7 U compared with the free enzyme. Lactose hydrolysis in a skim milk using the immobilized enzyme has also been investigated in a continuous enzymatic reactor. The related mechanisms of the hydrolysis process are discussed.

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## Abstract The enzymatic synthesis of __N__‐acetyl‐lactosamine (LacNAc) was studied in aqueous media with high substrate concentrations using the transgalactosylation of __N__‐acetyl‐D‐glucosamine (GlcNAc), starting from lactose as a galactosyl donor. The efficiency and regioselectivity of the β‐g