Current attention focuses on mechanisms of controlling blood pressure through the inhibition of angiotensin I-converting enzyme (ACE). Bioactive antihypertensive peptides of food origin are increasingly gaining importance as alternates to synthetic drugs in hypertension therapy. The ACE inhibito...detailed
Arachin, the major seed storage protein of groundnut, showed polymorphism. The polymorphic forms were due to differences in molecular size, net charge and polypeptide composition of the native protein. Purified arachin at low ionic strength resolved into monomeric and dimeric forms both on sucro...detailed
In silico analysis of the sequences of arachin, the major storage protein of peanut suggests that it is laden with antihypertensive peptides. Physiological proteases pepsin, trypsin, chymotrypsin and pancreatin were used to release these peptides. The degree of proteolysis and in vitro angiotens...detailed
Arachin and conarachin-rich fractions of peanut protein were extracted by using cryoprecipitation followed by centrifugation. These two fractions were individually crosslinked using transglutaminase (TG). The physicochemical characteristics including aggregation due to crosslinking, solubility, ...detailed
A process for the optimization of arachin from defatted peanut cakes had been developed. The process included pre-treatment, extraction by Tris–HCl buffer solution, pH adjustment and final separation by centrifugation. A Box–Behnken design including independent variables such as extraction tem...detailed
The influence of k-carrageenan on the stability of arachin was analyzed. K-carrageenan could significantly enhance the stability of arachin solution. 0.04% k-carrageenan was the most effective when the concentration of arachin was 2.0%. The pH value, ionic strength and temperature significantly ...detailed