Open AccessPreparation and in vitro bioactive evaluation of cashew-nut proteins hydrolysate as a potential source of anti-allergy peptides
Author(s) -
Di Chen,
Yang Shu,
Jian Chen,
Xianying Cao
Publication year - 2020
Publication title -
journal of food science and technology/journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.656
H-Index - 68
eISSN - 0975-8402
pISSN - 0022-1155
DOI - 10.1007/s13197-020-04838-z
Subject(s) - hydrolysate , chemistry , papain , protease , food science , hydrolysis , hyaluronidase , proteases , cashew nut , digestion (alchemy) , enzyme , proteolytic enzymes , biochemistry , chromatography
This work proposes a novel potential source of antiallergens based on bioactive peptides. Cashew-nut protein hydrolysate with antiallergic activity was prepared from cashew nuts through protease treatment. The change in the antiallergic activity of cashew-nut protein hydrolysate during in vitro simulated digestion was investigated. Cashew-nut protein hydrolysates were prepared through treatment using five different enzymes, namely, Alcalase, Protamex, Neutrase, papain, and bromelin. According to the results of molecular weight distribution, more small molecular weight peptides could be obtained by selecting Alcalase protease than other proteases, and the degree of hydrolysis, trichloroacetic acid-soluble peptide yield and hyaluronidase inhibitory rate of the hydrolysate were 17.0 ± 61.52%, 26.28 ± 0.13% and 62.06% ± 5.07%, which were significantly higher than those of other proteases. Therefore, Alcalase is the most suitable protease for the preparation of cashew-nut hydrolysates. Cashew-nut protein hydrolysates prepared with Alcalase under optimum conditions were fractionated through ultrafiltration. Fractions with low molecular weight exhibited the highest hyaluronidase inhibitory rate (90.57%) among all fractions. The inhibition of hyaluronidase activity during digestion showed that cashew-nut protein hydrolysate III (CPH III) has persistent antiallergic activity. Therefore, CPH III could serve as a potential source of functional peptides with health-promoting effects.