title: Effect of pH on the production of lipolyzed butter oil by a calf pregastric esterase immobilized in a hollow-fiber reactor: II. Multiresponse kinetics.
abstract: The lipolysis of butter oil in a hollow-fiber reactor containing an immobilized calf pregastric esterase was studied at 40 degrees C and at pH values of 4.0, 5.0, 6.0, and 7.0. The concentrations of ten fatty acid species in the lipolyzed product were determined using high-performance liquid chromatography (HPLC). The relative specificity of this esterase depended on pH. Three mathematical models derived from a generalized Michaelis-Menten mechanism were tested for their ability to describe the rates of release of individual specific fatty acids. Loss of enzyme activity was modeled using first order kinetics. The models for deactivation and reaction kinetics were fit simultaneously to the data. The parameters of the model were also tested for dependence on pH. The model was successful in describing the rates of release of all ten fatty acid species for a range of space times and pH values.
authors.affiliation: Department of Chemical Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, Wisconsin 53706, USA.
authors.forename: L P
authors.initials: LP
authors.lastname: Lessard
authors.forename: C G
authors.initials: CG
authors.lastname: Hill
mesh_terms: D000818:Animals; D019149:Bioreactors; D002079:Butter; D002417:Cattle; D004800:Enzymes, Immobilized; D005227:Fatty Acids / Q000737:chemistry; D005524:Food Technology; D005989:Glycerides / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008066:Lipolysis; D008954:Models, Biological; D013379:Substrate Specificity
chemical_list: D004800:Enzymes, Immobilized; D005227:Fatty Acids; D005989:Glycerides; D002079:Butter; D008049:Lipase; C043101:gastric triacylglycerol lipase