title: Study of an enzyme membrane reactor with immobilized fumarase for production of L-malic acid.
abstract: The conversion of fumaric acid into L-malic acid by fumarase immobilized in a membrane reactor was analyzed experimentally. The enzyme was entrapped in asymmetric capillary membranes made of polysulfone. The performance of the reactor was evaluated in terms of conversion degree, reaction rate, and stability. The influence of operating conditions, such as amount of immobilized enzyme, substrate concentration, residence time, and axial flow rate, were investigated. The kinetic parameters K(m), V(max), and k(+2) were also measured. The stability of the immobilized enzyme was very good, showing no activity decay during more than 2 weeks of continuous operation.
authors.affiliation: Research Institute on Membranes and Modelling of Chemical Reactors, IRMERC-CNR, University of Calabria, Via P. Bucci 17/C, 87030 Rende, CS, Italy. giorno@irmerc.cs.cnr.it
authors.forename: L
authors.initials: L
authors.lastname: Giorno
authors.forename: E
authors.initials: E
authors.lastname: Drioli
authors.forename: G
authors.initials: G
authors.lastname: Carvoli
authors.forename: A
authors.initials: A
authors.lastname: Cassano
authors.forename: L
authors.initials: L
authors.lastname: Donato
mesh_terms: D000818:Animals; D019149:Bioreactors; D001709:Biotechnology / Q000295:instrumentation / Q000379:methods; D002197:Capillary Action; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004867:Equipment Design; D005649:Fumarate Hydratase / Q000378:metabolism*; D007700:Kinetics; D008293:Malates / Q000138:chemical synthesis* / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology; D011108:Polymers; D013450:Sulfones; D013552:Swine
chemical_list: D004800:Enzymes, Immobilized; D008293:Malates; D011108:Polymers; D013450:Sulfones; C017662:polysulfone P 1700; C030298:malic acid; D005649:Fumarate Hydratase