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Operational Stability and Kinetic Study of a Membrane Reactor with Pectinases from Aspergillus niger
Author(s) -
RodríguezNogales J.M.,
Ortega N.,
PerezMateos M.,
Busto M.D.
Publication year - 2005
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2005.tb07081.x
Subject(s) - aspergillus niger , membrane reactor , chemistry , membrane , hydrolysis , pectin , continuous stirred tank reactor , product inhibition , chromatography , kinetics , substrate (aquarium) , chemical engineering , nuclear chemistry , enzyme , biochemistry , non competitive inhibition , physics , oceanography , quantum mechanics , engineering , geology
The kinetic and operational behavior of a free enzyme membrane reactor (FEMR) were analyzed. High conversion (83%) of the pectin could be achieved with a substrate‐to‐enzyme ratio of 23.3 at 46°C and pH 4.8, with a transmembrane pressure of 34.5 kPa and recycling flow rate of 36 L/h. The FEMR showed a 1st‐order deactiva‐tion profile with a calculated half life (t 1/2 ) of 21.7 d in the operation conditions. Akinetic study of the hydrolysis of pectin by free endopectinases from Aspergillus niger was done by the simultaneous use of a stirred‐tank reactor and a FEMR. Kinetic data were fit to a model based on the Michaelis‐Menten rate expression and the design equation for a continuous membrane reactor. The kinetic characteristics observed in the hydrolysis of pectin included a product competitive inhibition. The K m and K i values for the membrane reactor were 2 to 3 times greater those obtained in a stirred‐tank reactor. On the basis of the V max values, the configuration of the FEMR was found to have excellent catalytic efficiency when compared with the stirred‐tank reactor.