PMID: 2091531Dec 1, 1990Paper

Preparation and characterization of pancreatic lipase immobilized in Eudragit-matrix

Applied Biochemistry and Biotechnology
A TelefoncuK D Vorlop

Abstract

Pancreatic lipase (EC 3.1.1.3) was immobilized by entrapping in a commercial preparation of acrylic/methacrylic acid ester-based copolymer (Eudragit E 30 D). The activity of the immobilized lipase beads with a diameter of 1.5-2.0 mm was found to be lower than that of the free lipase. The optimum pH was shifted to the alkaline region and the thermal stability increased, whereas the optimum temperature level remained unchanged. The most important reason for the decreased activity was diffusion limitations. The diffusion of the substrate and products became more pronounced, and lipolytic activity increased upon addition of n-hexane into the reaction medium. The storage and operational stabilities of the immobilized lipase were investigated, and both characteristics were found to be increased when compared to the free enzyme. Furthermore, mechanical or magnetic stirring during the operation were found to have no influence on the carrier-matrix as determined by nephelometric measurements.

References

Oct 1, 1975·Journal of Chromatographic Science·R J Hamilton
Oct 1, 1969·The American Journal of Physiology·M H Khayat, J Christophe

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Citations

Mar 11, 2008·Applied Biochemistry and Biotechnology·Wazé Aimée Mireille AllouePhilippe Thonart
Jul 12, 2002·Biomaterials·Seema S Betigeri, Steven H Neau
Oct 11, 2003·Biotechnology Advances·R SharmaU C Banerjee
May 13, 2014·Enzyme Research·Bárbara M BonineGustavo O Bonilla-Rodriguez
Jun 16, 2004·Preparative Biochemistry & Biotechnology·Ayten Sagiroglu, Azmi Telefoncu
Sep 8, 2006·Acta Microbiologica Et Immunologica Hungarica·Satyendra KumarReena Gupta
Jan 1, 1996·Critical Reviews in Biotechnology·G Ozcengiz
Mar 6, 2021·International Journal of Biological Macromolecules·F Rafiee, M Rezaee
Apr 25, 1994·Biotechnology and Bioengineering·J A Bosley, J C Clayton

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