Visual spectroscopy method to evaluate entrapment efficiency of electrostatically precipitated proteins in combination with octenyl succinic anhydrate (OSA)-modified polysaccharides
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abstract
2016 Elsevier Ltd The objective of this study was to evaluate the application of visible spectroscopy to discern the entrapment capability of a hydrophobic compound (trans-cinnamaldehyde) by electrostatic precipitation in aqueous solution of pure whey proteins or in combination with octenyl succinic anhydrate (OSA)-modified polysaccharides. Particles were obtained by electrostatic precipitation of complex structures formed at different weight ratios (1:01:10) of proteins and OSA-modified polysaccharides. Trans-cinnamaldehyde 99% (TCNN) was selected as a model hydrophobic bioactive compound, due to its use as an antimicrobial. The entrapment capability of TCNN by the complex structures was evaluated by measuring the remaining TCNN on the supernatant (TCNNsuptt) after centrifugation of the complexes that were electrostatically precipitated at 23C. The insoluble complexes were effectively monitored through absorbance (Abs) measurements at 600nm with a spectrophotometer. Absorbance values corresponded well with total sugar interaction-adsorption of OSA-modified polysaccharides at the electrostatic precipitation of proteins, which in turn corresponded to the entrapment efficiency, based on the amount of protein precipitated. These results validate the use of spectrophotometric measurements as a rapid, toxic-free, and easy, comparative method to evaluate the adsorption interaction between protein and other amphiphilic molecules. In addition, electrostatic precipitation of protein alone or in combination with OSA-modified polysaccharides is a feasible method to entrap volatile and thermolabile compounds.
