Angiotensin I converting enzyme inhibition and enzymatic resistance in vitro of casein hydrolysate treated by plastein reaction and fractionated with ethanol/water or methanol/water

In VitroAngiotensin I-Converting Enzyme Inhibition of Casein Hydrolysate Responsible for Plastein Reaction in Ethanol-Water Medium, Solvent Fractionation, and Protease Digestion

“…[25,31] The two values are lower than that of the present one (300.9 µmol/g peptides). This is supported by a previous research, in which addition of organic solvent such as glycerol into plastein reaction system can enhance plastein yield.…”

“…Unlikely, lower Alcalase addition about 3.1 or 7.7 kU/g peptides are applied in water medium. [25,31] …”

“…[30] Plastein reaction is also able to confer casein hydrolysate stronger resistance in ACE-inhibitory activity towards in vitro digestion of some proteases. [31] Plastein reaction in these mentioned studies is carried out in a water medium. Whether a plastein reaction in other mediums (e.g., a mixed solvent system consisting of water and one of miscible organic solvents) has potential impact on ACE inhibition and protease resistance of protein hydrolysates is unknown yet.…”

Towards the design of hypolipidaemic peptides: Deoxycholate binding affinity of hydrophobic peptide aggregates of casein plastein

“…Subsequently, plastein reaction was used in debittering protein hydrolysates (Synowiecki, Jagietka, & Shahidi, 1996); it was thought that the bitterness-contributing hydrophobic amino acid residues of protein hydrolysates are hidden in the peptide aggregate's core, thereby reducing their interaction with taste receptors (Gong et al, 2015). Recently, plastein was reported to possess enhanced bioactivity compared to its hydrolysate precursor including antioxidative (Udenigwe, Wu, Drummond, & Gong, 2014;Zhao, Wu, & Li, 2010) and angiotensin converting enzyme inhibitory activities (Sun & Zhao, 2012), although it is still not known how the aggregate structure contributed to bioactivity. Moreover, plastein reaction was also found to enhance the BA-binding capacity of chicken meat protein hydrolysates and this was associated with an increase in surface hydrophobicity of the peptide aggregates Udenigwe & Rouvinen-Watt, 2015).…”

In vitroangiotensin-converting enzyme inhibition or digestive stability of casein hydrolysates treated by plastein reaction in propanol–water medium

“…The reaction has been used to modify food proteins to improve their functional or nutritive property or mask the bitter taste of protein hydrolysates (Fujimaki et al, 1971;Yamashita et al, 1976). Recent researches also use plastein reaction in water medium to enhance ACE-inhibitory activity Zhao & Li, 2009), digestive stability (Sun & Zhao, 2012), or scavenging activity (Zhao, Wu, & Li, 2010) of casein hydrolysate. Whether the reaction in other media consisting of water and one of the miscible organic solvents (e.g.…”