Kinetic study of tyrosinase immobilized on polymeric membrane

Kinetic properties of tyrosinase immobilized on a polymeric membrane for the production of l-3,4-dihydroxyphenylalanine (l-DOPA) were investigated. A comparison with the properties shown by the free enzyme used in a stirred tank reactor was also carried out. The values of the Michaelis-Menten consta...

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Veröffentlicht in:	Journal of membrane science 2014-03, Vol.454, p.346-350
Hauptverfasser:	DONATO, L, ALGIERI, C, RIZZI, A, GIORNO, L
Format:	Artikel
Sprache:	eng
Schlagworte:	Affinity Applied sciences Chemistry Colloidal state and disperse state Constants Enzymes Exact sciences and technology Exchange resins and membranes Forms of application and semi-finished materials General and physical chemistry Membranes Polymer industry, paints, wood Reaction kinetics Reactors Tanks Technology of polymers Tyrosinase
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Zusammenfassung:	Kinetic properties of tyrosinase immobilized on a polymeric membrane for the production of l-3,4-dihydroxyphenylalanine (l-DOPA) were investigated. A comparison with the properties shown by the free enzyme used in a stirred tank reactor was also carried out. The values of the Michaelis-Menten constant indicated that the immobilized tyrosinase exhibited better affinity for the substrate (Km=1.56 mM and 2.10 mM for the immobilized and free enzyme, respectively).
ISSN:	0376-7388 1873-3123
DOI:	10.1016/j.memsci.2013.12.029