Enzymatic synthesis of ethyl hexanoate by transesterification.

Chowdary, G. V. and Prapulla, S. G. (2003) Enzymatic synthesis of ethyl hexanoate by transesterification. International Journal of Food Science and Technology, 38 (2). 127-133 ; 28 ref..

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Abstract

Enzymic synthesis of the flavour compound, ethyl hexanoate, by means of an acyl transfer reaction in n-hexane, was investigated using immobilized lipase. Reaction parameters studied included lipase source (Rhizomucor miehei, Aspergillus niger, Penicillium roquefortii, Candida cylindracea and porcine pancreas), substrate concn. (0.05-0.5M), reaction temp. (30-70C) and concn. of hexanoic acid or ethyl caprate (<less than or equal to>0.8M). R. miehei lipase showed more specificity than the other lipases and was used in further studies. Max. ester synthesis was obtained with a substrate concn. of 0.5M at 45-55C. Higher molar concn. of hexanoic acid inhibited the enzyme, but no inhibitory effect of ethyl caprate, even at higher molar concn., was observed. Apparent kinetic parameters were found to be as follows: Km (ester), 00135M; Km (acid), 0.08466; Ki (ester), 3.07M; Ki (acid), 0.550M; Vmax, 1.861 mumol/min/mg enzyme.

Item Type:	Article
Uncontrolled Keywords:	ESTERIFICATION-; FLAVOUR-COMPOUNDS; LIPASES-; RHIZOMUCOR-; TEMPERATURE-; ETHYL-HEXANOATE; KINETICS-; RHIZOMUCOR-MIEHEI; TEMP.-; TRANSESTERIFICATION-
Subjects:	600 Technology > 08 Food technology > 09 Food Microbiology
Divisions:	Fermentation Technology and Bioengineering
Depositing User:	Users 197 not found.
Date Deposited:	22 Jun 2011 11:01
Last Modified:	28 Dec 2011 09:52
URI:	http://ir.cftri.res.in/id/eprint/6353

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