Foods and Raw Materials (Dec 2016)

EVALUATION OF ANTIMUTAGENIC AND ANTIFUNGAL PROPERTIES, PARAMETERS OF ACUTE TOXICITY AND SENSITIZING ACTIVITY OF ENZYMATIC WHEY PROTEIN HYDROLYSATE

  • Golovach T.N.,
  • Dudchik N.V.,
  • Veremeenko E.G.,
  • Tsygankov V.G. ,
  • Bondarchuk A.M.,
  • Filonyuk V.A.,
  • Shevlyakov V.V.,
  • Ushkov A.A.,
  • Sobol` Yu.A.,
  • Erm G.I. ,
  • Kurchenko V.P.

DOI
https://doi.org/10.21179/2308-4057-2016-2-38-47
Journal volume & issue
Vol. 4, no. 2
pp. 38 – 47

Abstract

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Biologically active peptides with antioxidative, antibacterial, immunomodulating and other properties result from the reaction between the whey proteins and proteolytic enzymes of the gastrointestinal tract or purified proteases. This work aims to determine antimutagenic and antifungal effect of the enzymatic hydrolysate of whey protein obtained, to assess its acute toxicity characteristics and sensitizing power. Antimutagenic action of native whey proteins and hydrolysates (test sample and hydrolyzate analog) was assessed by the Ames test using indicator strains of Salmonella typhimurium ТА 98 and ТА 100. When determining the antifungal activity, opportunistic strains of Aspergillus niger and Candida albicans were used. The toxicity degree of samples was defined in studies to evaluate the acute intragastric toxicity in white rats as well as in the single abdominal dose study on the white mice. Irritating influence of whey proteins and peptides on was evaluated when applied to the eye mucosa of rabbits. The sensitizing capacity of samples was evaluated using the experimental model to reproduce the delayed hyperresponsiveness in white mice. It is identified that the developed hydrolisate is classified as the safe agent and has low sensitizing ability. The sample obtained has the comparative values of antioxidant and antimutagenic activity level as compared with the analog «Vital Аrmor H 801 LB» (Armor Proteines, France) used to manufacture functional products. The advantages of the hydrolisate developed include the increase in the content of peptide fraction and more pronounced antifungal activity towards A. niger .

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