NDLI: The effect of immobilization on the hydrolytic/interesterification activity of lipase from Rhizopus niveus

Content Provider	Springer Nature Link
Author	Kermasha, S. Bisakowski, B.
Copyright Year	1998
Abstract	Lipase from Rhizopus niveus was immobilized by physical adsorption on Celite 545 and glass beads. The results showed that the highest immobilization efficiency and specific hydrolytic activity of 96% and 9.2 meq/mg protein/min, respectively, were obtained with Celite as the carrier. However, the specific hydrolytic activity of lipase adsorbed on glass beads by acetone precipitation was similar to that obtained by the Celite carrier, although the protein loading capacity was relatively low. The results showed that lipase immobilized on glass beads exhibited similar activity profiles with respect to reaction time, different enzyme concentrations, and water content, using trimyristin and tripalmitin as substrates, to those obtained with the free enzyme. In contrast, the immobilized lipase on Celite exhibited a considerably lower hydrolytic activity. However, the results also showed that the lipase activities of the free enzyme and the immobilized Celite enzyme were similar when the more hydrophilic triolein was used as the substrate. The interesterification of a mixture of tripalmitin and trimyristin or triolein was carried out using both the free and immobilized enzymes. The results indicated that the hydrolytic activity of lipase was similar in both cases for the first 24 h, after which it decreased dramatically. These findings suggest that at this late stage an equilibrium between the hydrolytic and interesterification reactions was reached.
Starting Page	1791
Ending Page	1799
Page Count	9
File Format	PDF
ISSN	0003021X
Journal	Journal of the American Oil Chemists' Society
Volume Number	75
Issue Number	12
e-ISSN	15589331
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-01-01
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Hydrolytic immobilization interesterification lipase microemulsion Industrial Chemistry/Chemical Engineering Analytical Chemistry Chemistry/Food Science Biotechnology Biomaterials Agriculture
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Chemical Engineering

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