Abstract The catalytic behaviour under isothermal conditions of two different membranes loaded with b-galactosidase was . investigated. One membrane M was constituted by a nylon sheet grafted with methylmethacrylate by means of chemical 1 . . grafting. The other, M , was prepared by a double chemical grafting: the first one with styrene Sty and the second one with methylmethacrylate. Membrane activity was characterized as a function of temperature, pH and substrate concentration. The role of Sty in increasing membrane hydrophobicity has been discussed. Membrane M was found to be better suited for was found to be better suited for employment in non-isothermal bioreactors.
Modulation of immobilized enzyme activity by altering the hydrophobicity of nylon-grafted membranes Part 1. Isothermal conditions / M. M., E.M., DE MAIO, A., S., D.M., N., D., U., B., S., R., V., G., P. Canciglia M., P., F. S., G., D. G., M.. - In: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC. - ISSN 1381-1177. - ELETTRONICO. - (2000), pp. 219-230.
Modulation of immobilized enzyme activity by altering the hydrophobicity of nylon-grafted membranes Part 1. Isothermal conditions
DE MAIO, ANNA;
2000
Abstract
Abstract The catalytic behaviour under isothermal conditions of two different membranes loaded with b-galactosidase was . investigated. One membrane M was constituted by a nylon sheet grafted with methylmethacrylate by means of chemical 1 . . grafting. The other, M , was prepared by a double chemical grafting: the first one with styrene Sty and the second one with methylmethacrylate. Membrane activity was characterized as a function of temperature, pH and substrate concentration. The role of Sty in increasing membrane hydrophobicity has been discussed. Membrane M was found to be better suited for was found to be better suited for employment in non-isothermal bioreactors.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
