Analytic and Immunologic Characterization of Chickpea (Cicer arietinum) Protein Hydrolysates Obtained by Bromelain and α-Chymotrypsin

• Published in: Journal of agricultural and food chemistry 1997-12, Vol.45 (12), p.4758-4762
• Main Authors: Hindi-Tamelikecht, F, Dauphin, C, Hamon, M, Grangaud, J. P, Pradeau, D
• Format: Article
• Language: English
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Biological and medical sciences; Food industries; Fundamental and applied biological sciences. Psychology
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf9702555

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 (2,4,6-trinitrobenzenesulfonic acid). The small peptides in fraction F2 were separated by reverse phase HPLC and were sequenced. Keywords: Chickpea; hydrolysates; bromelain; α-chymotrypsin; antigenicity; ELISA; HP SEC