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Effect of pH on the production of lipolyzed butter oil by a calf pregastric esterase immobilized in a hollow-fiber reactor: I. Uniresponse kinetics

✍ Scribed by Louis P. Lessard; Charles G. Hill Jr.

Publisher: John Wiley and Sons
Year: 2000
Tongue: English
Weight: 308 KB
Volume: 69
Category: Article
ISSN: 0006-3592
DOI: 10.1002/(sici)1097-0290(20000720)69:2<183::aid-bit7>3.0.co;2-2

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✦ Synopsis

A calf pregastric esterase immobilized in a hollow-fiber reactor was employed to hydrolyze milkfat, thereby producing a lipolyzed butteroil. The reaction kinetics can be modeled by a two-parameter model of the general Michaelis-Menten form based on a ping-pong bi-bi mechanism; the rate of enzyme deactivation can be modeled as a first-order reaction.

The initial concentration of accessible glyceride bonds, [G] 0 , was estimated by complete saponification of the substrate butteroil as 2400 mM. An extra sum of squares test indicated that not only the parameters of the kinetic generalized Michaelis-Menten model, but also the deactivation-rate constant varied significantly with pH. The optimum pH, for lypolysis is near 6.0 at a temperature of 40°C because at this pH the rate of deactivation of the esterase is minimized.

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