Effects of temperature and pH on the catalytic activity of the immobilized [beta]-galactosidase from Kluyveromyces lactis Export

@article{citeulike:2920364, abstract = {A study of the cross-linking immobilization of [beta]-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.}, author = {Zhou, Quinn Z. and Chen, Xiao D.}, citeulike-article-id = {2920364}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S1369-703X(01)00118-8}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6V5N-449TJ84-5/1/ad2ed2161491bde479681c3115d2ca9d}, doi = {10.1016/S1369-703X(01)00118-8}, journal = {Biochemical Engineering Journal}, keywords = {alkaline\_phosphatase, biochem\_lab}, month = {November}, number = {1}, pages = {33--40}, posted-at = {2008-06-24 07:26:58}, priority = {2}, title = {Effects of temperature and pH on the catalytic activity of the immobilized [beta]-galactosidase from Kluyveromyces lactis}, url = {http://dx.doi.org/10.1016/S1369-703X(01)00118-8}, volume = {9}, year = {2001} }

TY - JOUR ID - citeulike:2920364 L3 - citeulike-article-id:2920364 N2 - A study of the cross-linking immobilization of [beta]-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. IS - 1 JF - Biochemical Engineering Journal EP - 40 TI - Effects of temperature and pH on the catalytic activity of the immobilized [beta]-galactosidase from Kluyveromyces lactis VL - 9 SP - 33 KW - alkaline_phosphatase KW - biochem_lab AU - Zhou, Quinn AU - Chen, Xiao PY - 2001/11// UR - http://dx.doi.org/10.1016/S1369-703X(01)00118-8 ER -