2009 Volume 45 Issue 3 Pages 81-87
Modification of lipoprotein lipase (LPL) with copoly (L-glutamicacid / L-alanine) (EA) was carriedout to stabilize the enzyme and preserve its activity retaining its solubility in water.The modificationbetween LPL and EA was based on covalent bonding.The relative activity (RA) and stability wereevaluated on the modified LPL (EA-LPL) compared to those of free LPL.High RA was found forEA-LPL toward a small ester substrate, p-nitrophenyl laurate(pNPL).Estimation of Michaelisconstants, Km and Vm revealed that the apparent Km, was larger than that of native LPL, while theapparent Vm was smaller than that of free LPL.The thermal and storage stabilities of EA-LPLwerehigher than those of free LPL inspite of their lower RA than that of free LPL.It is concluded thatthe modified LPL (EA-LPL) displayed higher stability than free LPL.
