The effects of limited enzymatic hydrolysis on the physicochemical and emulsifying properties of a lentil protein isolate

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

“…The case of limited hydrolysis is less conclusive. A decline in the surface hydrophobicity with limited hydrolysis has been reported for soybeans (Jung et al, 2005;Surowka, Zmudzinski, & Surowka, 2004), peanuts , and lentil proteins (Avramenko et al, 2013), in agreement with the present study. Jung et al (2005) proposed that the exposure of buried hydrophobic groups upon limited protein hydrolysis was followed by their aggregation via hydrophobic interactions, thus effectively reburying them within the interior of a larger aggregated structure, resulting in the reduction of surface hydrophobicity.…”

“…By comparison with the interfacial tension at 120 s among all the samples, the values of the cream layer peptides from the hydrolysis at 10 min and the aqueous phase peptides from the hydrolysis at 30 and 60 min were close to the lowest interfacial tension (10.23 mN/m) exhibited by the aqueous phase proteins, while the cream layer peptides from the hydrolysis at 30 min had the largest value (18.17 mN/m). Avramenko et al (2013) reported that the interfacial tension of unhydrolyzed lentil protein isolates was significantly greater than that of the hydrolyzed lentil protein isolates. However, the changes in the interfacial tension of the peanut proteins before and after hydrolysis were complicated in this study.…”

“…Many researchers have attempted to understand the effects of enzymatic hydrolysis on the emulsification properties of proteins (Avramenko, Low, & Nickerson, 2013;Guan, Yao, Chen, Shan, & Zhang, 2007;Jung, Murphy, & Johnson, 2005;Nishinari, Fang, Guo, & Phillips, 2014;Yust & Pedroche, 2010;Zhao, Liu, Zhao, Ren, & Yang, 2011). These studies were generally carried out by preparing model emulsions using target proteins at various degrees of hydrolysis (DH).…”

Antioxidant activity of black bean (Phaseolus vulgaris L.) protein hydrolysates

“…The hydrolysis conditions and the specificity of the enzyme are key factors for protein hydrolysis, because these factors influence the sites and the peptide linkages that will be hydrolyzed. The resulted protein hydrolyzed material will have different characteristics and biological and functional properties (Avramenko et al, 2013). Among several reported benefits, the most evidenced are anti-hypertension, antioxidant, antimicrobial and anti-carcinogenic activities and the control of lipid metabolism (Roy et al, 2010).…”

Novel food grade dispersants: Review of recent progress

“…Even relatively small changes in the degree of hydrolysis can very quickly alter the composition on the surface, due to strong competitive adsorption between all the created polypeptide species. have also been seen for lentil protein isolate hydrolysed with heat + trypsin [77]. In this latter study the authors only considered DH=4, 9 and 20%.…”