Modulation of immobilized enzyme activity by altering the hydrophobicity of nylon-grafted membranes

Autor:	S. Rossi, Umberto Bencivenga, P. Canciglia, V. Grano, Marianna Portaccio, M.M El-Masry, F.S. Gaeta, Nadia Diano, Damiano Gustavo Mita, S. Di Martino, A. De Maio
Rok vydání:	2000
Předmět:	Immobilized enzyme Process Chemistry and Technology technology industry and agriculture Bioengineering Grafting Biochemistry Catalysis Isothermal process Styrene chemistry.chemical_compound Hydrolysis Membrane chemistry Polymer chemistry Membrane activity
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 9:219-230
ISSN:	1381-1177
DOI:	10.1016/s1381-1177(99)00100-9
Popis:	The catalytic behaviour under isothermal conditions of two different membranes loaded with β-galactosidase was investigated. One membrane (M1) was constituted by a nylon sheet grafted with methylmethacrylate by means of chemical grafting. The other, (M2), 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 M2 was found to be better suited for employment in non-isothermal bioreactors.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c34cb02bf6ac96f4d6a3907be28f2d65 https://doi.org/10.1016/s1381-1177(99)00100-9 Zobrazit plný text záznamu Full Text from ScienceDirect