Response surface methodology applied to the generation of casein hydrolysates with antioxidant and dipeptidyl peptidase IV inhibitory properties.

• Autores: Alice B Nongonierma, Solène Le Maux, Claire Esteveny, Richard J FitzGerald
• Localización: Journal of the science of food and agriculture, ISSN 0022-5142, Vol. 97, Nº 4, 2017, págs. 1093-1101
• Idioma: inglés
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• Resumen

  • Background: Hydrolysis parameters affecting the release of dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant peptides from milk proteins have not been extensively studied. Therefore, a multifactorial (i.e. pH, temperature and hydrolysis time) composite design was used to optimise the release of bioactive peptides (BAPs) with DPP-IV inhibitory and antioxidant [oxygen radical absorbance capacity (ORAC)] properties from sodium caseinate.; Results: Fifteen sodium caseinate hydrolysates (H1-H15) were generated with ProtamexTM , a bacillus proteinase activity. Hydrolysis time (1 to 5 h) had the highest influence on both DPP-IV inhibitory properties and ORAC activity (P < 0.05). Alteration of incubation temperature (40 to 60 °C) and pH (6.5 to 8.0) had an effect on the DPP-IV inhibitory properties but not the ORAC activity of the Protamex sodium caseinate hydrolysates. A multi-functional hydrolysate, H12, was identified having DPP-IV inhibitory (actual: 0.82 ± 0.24 vs. predicted optimum: 0.68 mg mL-1 ) and ORAC (actual: 639 ± 66 vs. predicted optimum: 639 µmol TE g-1 ) activity of the same order (P > 0.05) as the response surface methodology (RSM) predicted optimum bioactivities.; Conclusion: Generation of milk protein hydrolysates through multifactorial design approaches may aid in the optimal enzymatic release of BAPs with serum glucose lowering and antioxidant properties. © 2016 Society of Chemical Industry.; © 2016 Society of Chemical Industry.