Immobilization of pregastric esterases in a hollow fiber reactor for continuous production of lipolysed butteroil

Document Type

Journal Article

Publication Date

1-1-1995

Journal

LWT - Food Science and Technology

Volume

28

Issue

3

DOI

10.1016/S0023-6438(95)94035-9

Abstract

Lingual Upases from calf, lamb and goal were semi-purified by cold storage and microfiltralion, and subsequently immobilized by physical adsorption on hollow fibers fabricated of microporous polypropylene. The immobilized lipases were employed in a hollow fiber membrane reactor to effect the continuous hydrolysis of a butterfat fraction that remains liquid at 18°C. The goat lipase showed higher lipolytic activity than the other two, but all three enzymes had good selectivilies for short-chain fatty acids. No deactivalion was observed for any of the immobilized enzymes during 5 d of continuous operation. A process based on this technology offers a number of advantages for the commercial production of lipolysed butteroil. © 1995 Academic Press Limited.

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