Search results for "Candida rugosa"

showing 3 items of 3 documents

Optimization of the Hydrolysis of Safflower Oil for the Production of Linoleic Acid, Used as Flavor Precursor

2015

Commercial lipases, from porcine pancreas (PPL),Candida rugosa(CRL), andThermomyces lanuginosus(Lipozyme TL IM), were investigated in terms of their efficiency for the hydrolysis of safflower oil (SO) for the liberation of free linoleic acid (LA), used as a flavor precursor. Although PPL, under the optimized conditions, showed a high degree of hydrolysis (91.6%), its low tolerance towards higher substrate concentrations could limit its use for SO hydrolysis. In comparison to the other investigated lipases, Lipozyme TL IM required higher amount of enzyme and an additional 3 h of reaction time to achieve its maximum degree of SO hydrolysis (90.2%). On the basis of the experimental findings, C…

0106 biological sciencesArticle SubjectLinoleic acidlcsh:TX341-64101 natural sciencesHydrolysischemistry.chemical_compound010608 biotechnology[SDV.IDA]Life Sciences [q-bio]/Food engineeringFlavorchemistry.chemical_classificationChromatographylcsh:TP368-456010405 organic chemistryChemistrySubstrate (chemistry)0104 chemical sciencesCandida rugosalcsh:Food processing and manufactureEnzymeBiochemistryBiocatalysisLiberationlcsh:Nutrition. Foods and food supply[SDV.AEN]Life Sciences [q-bio]/Food and NutritionResearch ArticleFood ScienceInternational Journal of Food Science
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Contribution to the study of the alteration of lipase activity ofCandida rugosa by ions and buffers

1994

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…

TrisChromatographyMolecular StructurebiologyTriacylglycerol lipaseFluorescence spectrometryBioengineeringLipaseGeneral MedicineBuffersApplied Microbiology and BiotechnologyBiochemistryEnzyme assayCandida rugosachemistry.chemical_compoundHydrolysisSpectrometry FluorescencechemistryIonic strengthCationsbiology.proteinLipaseMolecular BiologyCandidaBiotechnologyApplied Biochemistry and Biotechnology
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Study of a lipase from Candida rugosa Diddens and Lodder

1993

Lipasic system of Candida rugosa (CBS 613) strain was studied. The enzyme was purified in one step by hydrophobic chromatography. The properties of this lipase were determined. It is an oligomeric enzyme composed of five identical monomers of 46 kg · mol−1. Its optimum reaction conditions are pH = 7 and temperature = 40°C. This enzyme presents a rapid thermal denaturation and then a more stable form. It is a cell-bound lipase which is induced by triacyl glycerols. This enzyme presents a high specificity for external positions on glycerol. Unterschung einer Lipase aus Candida rugosa Diddens und Lodder Die Reinigung einer Lipase aus Candida rugosa (CBS 613) wurde in einer einzigen Stufe durch…

chemistry.chemical_classificationbiologyStereochemistry[SDV]Life Sciences [q-bio]Triacylglycerol lipaseFungi imperfectibiology.organism_classificationYeastCandida rugosa[SDV] Life Sciences [q-bio]EnzymechemistryBiochemistrybiology.proteinSubstrate specificityLipase
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