Abstract
A water soluble concentrate of chickpea (Cicer arietinum) proteins was hydrolyzed by bromelain and α-chymotrypsin. Hydrolysis was verified by polyacrylamide gel electrophoresis in presence of sodium dodecyl sulfate. The use of ELISA in an inhibition system, conducted with chickpea protein antiserum raised in rabbits, showed that enzymatic hydrolysis resulted in a considerable reduction in the antigenic character of the proteins. Thus, the percentage inhibition by the α-chymotrypsin of hydrolysate was 58 ± 2.3% and that by the bromelain hydrolysate was 45 ± 4.5%. The peptides were measured by size exclusion chromatography. Peptides with molar mass lower than 1000 Da could be fractionated into fraction F1 containing peptides with molar mass higher than 500 Da, fraction F2 containing peptides with molar mass included between 200 and 500 Da, essentially small peptides containing 2, 3, or 4 amino acids, and fraction F3 containing free amino acids. The purified fractions were quantified with the TNBS method (2,...
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
