Journal of Food Science · 1996 · 17 citations · 38 references
Life SciencesBiochemistryBiotechnologyBiocatalysisEnzymologyLipid BiochemistryEnzyme KineticsLipid AnalysisLipid ChemistryLipid DigestionMilk EnzymesMilk LipidsFatty AcidsLipasesMilk Fat HydrolysisMilk Lipase EnzymesMilk Lipid HydrolysisReverse MicellesTemperature OptimumTemperature-dependent Reaction Rate
ABSTRACT Butterfat was hydrolyzed with lipases contained in lecithin reverse micelles. The influence of pH, temperature, molar ratio of surfactant to water (R) and surfactant concentration on the hydrolytic reaction indicated linear, quadratic, and interactive effects for reaction systems mediated by R. javanicus and C. rugosa lipases. The initial reaction rate was dependent on reaction parameters; however, the degree of hydrolysis was independent of pH. Both enzymes exhibited high thermal stability. The content and composition of milk fat hydrolysates prepared by R. javanicus lipase were most influenced by reaction temperature and R. The optimum conditions for production of free fatty acids, monoacyl‐glycerols, diacylglycerols and specific regio‐isomers were defined.
38
Official Methods of Analysis of
Analytical Chemistry · 1980 · 59.6K citations
Management, Educational Assessment, Information Retrieval +5