Lipase-mediated hydrolysis of blackcurrant oil

Citation
M. Vacek et al., Lipase-mediated hydrolysis of blackcurrant oil, ENZYME MICR, 27(7), 2000, pp. 531-536
Citations number
15
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
ENZYME AND MICROBIAL TECHNOLOGY
ISSN journal
01410229 → ACNP
Volume
27
Issue
7
Year of publication
2000
Pages
531 - 536
Database
ISI
SICI code
0141-0229(200010)27:7<531:LHOBO>2.0.ZU;2-#
Abstract
Four commercially available lipases, both free and immobilized, were tested for their ability to catalyze hydrolysis of blackcurrant (Ribes nigrum) oi l using two different approaches. The lipase from Mucor miehei was studied free and immobilized in two different ways. The former series of enzymic re actions were performed in tap water at 40 degrees C, but the latter series of enzymic processes were carried out in mixtures of isooctane and phosphat e buffer (in a typical 2/1 ratio of the components) at 30 degrees C. These conditions were optimized to increase and/or to maximize the yields of the products, which were priority targets in this study. A rate of hydrolysis a nd a selective preference of the hydrolytic enzymes towards fatty acids, wi th a special focus on enrichment of alpha-linolenic acid and/or gamma-linol enic acid, were studied. Higher rates of hydrolysis of the blackcurrant oil in the former series of reactions were observed with the immobilized lipas e from Pseudomonas cepacia used as biocatalyst. In the latter approach, the most favorable results of the rate of hydrolysis of the target blackcurran t oil were achieved with the immobilized lipase from Mucor miehei employed as biocatalyst. Only three lipases, selected from a series of lipases teste d during this investigation, displayed specificity towards alpha-linolenic acid and gamma-linolenic acid, i.e. the immobilized lipase from P. cepacia, lipase from M. miehei and lipase from P. fluorescens. (C) 2000 Elsevier Sc ience Inc. All rights reserved.