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- Netto, Flavia M., et al. Show all 7 Authors
- Journal of functional foods 2018 v.51 pp. 121-129
- allergenicity; allergens; caffeic acid; calorimetry; circular dichroism spectroscopy; enthalpy; epigallocatechin gallate; fluorescence; heat production; hydrophobicity; milk; pH; protein structure; tea; thermal stability; titration; whey protein
- ... Structural changes and allergenicity of whey proteins (WPI) upon complexation with caffeic acid (CA) and (-)-epigallocatechin gallate (EGCG) at acidic and neutral pH conditions were investigated. WPI-phenolic compounds interactions were evidenced by fluorescence quenching, accompanied by red-shift (32 nm in WPI-CA and 3 nm in WPI-EGCG). Negative exothermic enthalpy obtained by isothermal titration ...
- Netto, Flavia M., et al. Show all 6 Authors
- Food research international 2016 v.83 pp. 112-120
- allergens; beta-lactoglobulin; enzymatic hydrolysis; heat; hydrolysates; hydrolysis; hydrophilicity; hydrophobicity; immobilized enzymes; lactalbumin; milk; molecular weight; subtilisin; whey protein isolate
- ... Protein antigenicity can be reduced by enzymatic hydrolysis, which can be performed either by free or immobilized enzyme. The immobilized enzyme is removed from the reaction medium and reused, while the free enzyme must be inactivated to stop the reaction, generally by heating. Here we have shown that hydrolysates produced with free or immobilized Alcalase on glyoxyl-agarose bead presented differe ...