The effect of interactions between beta-lactoglobulin (βLG) and lauric acid (LA) on the formation of ternary maize starch-LA-protein complexes was investigated. Analysis of the secondary structure of βLG by FTIR… Click to show full abstract
The effect of interactions between beta-lactoglobulin (βLG) and lauric acid (LA) on the formation of ternary maize starch-LA-protein complexes was investigated. Analysis of the secondary structure of βLG by FTIR and changes in fluorescence λmax and intensity indicated that βLG and LA interacted during heating and cooling in a Rapid Visco Analyser (RVA). Results from RVA, DSC and Raman spectroscopy analyses showed that increasing the concentration of βLG from 25 to 200 mg increased the amount of ternary starch-LA-βLG complexes formed. There was little difference in the amounts of the ternary complexes formed when the amount of βLG was 25-150 mg, but a greater amount of starch-LA-βLG complexes was formed when 200 mg of βLG was pre-mixed with LA. From this study, we concluded that prior interaction between βLG and LA had no significant effect on the formation of ternary starch-LA-βLG complexes.
               
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