Selective release of ACE-inhibiting tryptophan-containing dipeptides from food proteins by enzymatic hydrolysis

Milk proteins as a source of tryptophan-containing bioactive peptides

“…These analyses indicated that the presence of branched chain amino acids (L and I) or C and G at the Nterminus and R, W, P, K, F or Y at the C terminus are associated with potent ACE inhibitory activity 24,27,30,59 . -CN (f163-164)), IW (α-La (f 59-60) and LF (f 267-268)) and VW (LF (f 346-347) and 50 LF (f 548-549)) were shown to be competitive inhibitors of human ACE 62,63 . The -La-derived peptides, IW and WL (α-La (f 104-105) and α-La (f 118-119)) were identified in milk proteinbased infant formulae 64 and in a whey protein hydrolysate generated with a combination of chymotrypsin and thermolysin 55 62 .…”

“…-CN (f163-164)), IW (α-La (f 59-60) and LF (f 267-268)) and VW (LF (f 346-347) and 50 LF (f 548-549)) were shown to be competitive inhibitors of human ACE 62,63 . The -La-derived peptides, IW and WL (α-La (f 104-105) and α-La (f 118-119)) were identified in milk proteinbased infant formulae 64 and in a whey protein hydrolysate generated with a combination of chymotrypsin and thermolysin 55 62 . The yield for the release of IW was estimated between 4-19% in the infant formulae 64 and at 50% (w/w) in a whey protein hydrolysate 62 .…”

“…The -La-derived peptides, IW and WL (α-La (f 104-105) and α-La (f 118-119)) were identified in milk proteinbased infant formulae 64 and in a whey protein hydrolysate generated with a combination of chymotrypsin and thermolysin 55 62 . The yield for the release of IW was estimated between 4-19% in the infant formulae 64 and at 50% (w/w) in a whey protein hydrolysate 62 . While that of WL was 4% (w/w) in a whey protein hydrolysate 62 .…”

“…The yield for the release of IW was estimated between 4-19% in the infant formulae 64 and at 50% (w/w) in a whey protein hydrolysate 62 . While that of WL was 4% (w/w) in a whey protein hydrolysate 62 . Simulated gastrointestinal digestion (SGID) revealed that AW and IW, when present in an hydrolysate, were 60 stable to the hydrolytic action of pepsin but were significantly degraded (59 and 40% (w/w), respectively) on incubation with pancreatic enzyme activities 62 .…”

Impact of ultrasound on egg white proteins as a pretreatment for functional hydrolysates production

“…The egg white, or albumen, possesses properties that make it attractive as a protein source in human nutrition due to high bioavailability of egg white proteins (EWPs) and high content of essential amino acids [7,8]. Furthermore, it is considered to be a multi-purpose ingredient that imparts multiple functional properties such as gelling, foaming and emulsification in many food products, in addition to their nutritional quality [9].…”