ABSTRACT
Valorisation of food by-products, like spent brewer's yeast and fruit pomaces, represents an important strategy for contributing to sustainable food production. The aims of this study were to obtain Maillard conjugates based on spent yeast protein hydrolysate (SYH) with dextran (D) or maltodextrin (MD) by means of ultrasound treatment and to use them for developing encapsulation systems for the anthocyanins from aronia pomace. The ultrasound-assisted Maillard conjugation promoted the increase of antioxidant activity by about 50% compared to conventional heating and SYH, and was not dependent on the polysaccharide type. The ability of the conjugates to act as wall material for encapsulating various biologically active compounds was tested via a freeze-drying method. The retention efficiency ranged between 58.25 ± 0.38%-65.25 ± 2.21%, while encapsulation efficiency varied from 67.09 ± 2.26% to 88.72 ± 0.33%, indicating the strong effect of the carrier material used for encapsulation. The addition of the hydrolysed yeast cell wall played a positive effect on the encapsulation efficiency of anthocyanins when used in combination with the SYH:MD conjugates. On the other hand, the stability of anthocyanins during storage, as well as their bioavailability during gastrointestinal digestion, were higher when using the SYH:D conjugate. The study showed that hydrolysis combined with the ultrasound-assisted Maillard reaction has a great potential for the valorisation of spent brewer's yeast as delivery material for the encapsulation of bioactive compounds.
ABSTRACT
Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree of hydrolysis (DH) results, the egg yolk proteins are better substrates for all the tested enzymes (DH of 6.2-20.1%) compared to those from egg whites (DH of 2.0-4.4%). The SDS-PAGE analysis indicated that pepsin and proteinase K were more efficient compared to trypsin in breaking the intramolecular peptide bonds of the high molecular weight egg proteins. For all the tested substrates, enzyme-assisted hydrolysis resulted in a significant increase in antioxidant activity, suggesting that many bioactive peptides are encrypted in inactive forms in the parent proteins. The hydrolysates obtained with proteinase K exhibited the highest DPPH radical scavenging activity (124-311 µM Trolox/g protein) and the lowest residual IgE-binding capacity. The bioinformatics tools revealed that proteinase K is able to break the integrity of the main linear IgE-binding epitopes from ovalbumin and ovomucoid. It can be concluded that proteinase K is a promising tool for modulating the intrinsic properties of egg proteins.
