6533b82bfe1ef96bd128e25b

RESEARCH PRODUCT

Contribution to the study of the alteration of lipase activity ofCandida rugosa by ions and buffers

P. MedinaJ.m. Sánchez-monteroMaría L. RúaJ. V. SinisterraMaría J. HernáizB. Celda

subject

TrisChromatographyMolecular StructurebiologyTriacylglycerol lipaseFluorescence spectrometryBioengineeringLipaseGeneral MedicineBuffersApplied Microbiology and BiotechnologyBiochemistryEnzyme assayCandida rugosachemistry.chemical_compoundHydrolysisSpectrometry FluorescencechemistryIonic strengthCationsbiology.proteinLipaseMolecular BiologyCandidaBiotechnology

description

A semipurified C. rugosa lipase (LS) has been prepared from commercial lipase (LC) using an economical procedure. The presence of sugars and glycopeptides has been detected in LS and LC. Pure lipase only has covalently bonded sugars. The hydrolysis of olive oil catalyzed by LS and commercial lipase (LC) is sensitive to the presence of cations Na(I), Mg(II), Ca(II), and Ba(II) and to the nature of buffer. Highest enzyme activity is obtained with 0.1M Tris/HCl buffers and the combination of NaCl 0.11M and CaCl2 0.11M. Fluorescence spectroscopy analysis of LC, LS, and both pure isoenzymes lipases A and B, was used to analyze the interaction of the lipase with these effectors. Inorganic cations Na or Ca do not interact with pure enzyme LA but do interact with LC and LS and do so slightly with LB. The organic cations (morfolinium or tris) interact with pure lipases. We postulate that the increase in the lipase activity produced by Na(I) or Ca(II) is related with interfacial phenomena, but the increase might be more specific in the hydrolysis of olive oil in the presence of Tris-HCl or morfoline-HCl buffer, owing to enzyme-buffer interaction.

yearjournalcountryeditionlanguage
1994-03-01Applied Biochemistry and Biotechnology
https://doi.org/10.1007/bf02779658