Lipolysis of butter oil by immobilized lamb pregastric esterase: I. Uniresponse kinetics-pH and temperature effects.
Lamb pregastric esterase, immobilized by physical adsorption on microporous polypropylene in a hollow fiber reactor, has been employed to effect the continuous hydrolysis of the triglycerides in butter oil. Experimental data were obtained at temperatures from 35 to 45 degrees C and pH values from 5.5 to 6.5. The overall rate of hydrolysis was fastest at 40 degrees C and a pH of 6.0. Nonlinear regression methods were employed to determine the kinetic parameters of rate expressions based on a generic Ping-Pong Bi Bi mechanism. The best nonlinear fit of the data was consistent with a mechanism that assumes that acylation of the enzyme is the rate-limiting step in the hydrolysis reaction.
Hill
C G
CG
Department of Chemical Engineering, University of Wisconsin-Madison, 53706, USA. hill@engr.wisc.edu
Ghannouchi
S
S
Garcia
H S
HS
D000818:Animals; D019149:Bioreactors; D002079:Butter; D004042:Dietary Fats, Unsaturated / Q000302:isolation & purification* / Q000378:metabolism; D004800:Enzymes, Immobilized; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008066:Lipolysis; D008954:Models, Biological; D012756:Sheep / Q000378:metabolism; D013696:Temperature
D004042:Dietary Fats, Unsaturated; D004800:Enzymes, Immobilized; D002079:Butter; D008049:Lipase; C043101:gastric triacylglycerol lipase