| Abstract
| - A water soluble concentrate of chickpea (Cicerarietinum) proteins was hydrolyzed bybromelainand α-chymotrypsin. Hydrolysis was verified by polyacrylamidegel electrophoresis in presence ofsodium dodecyl sulfate. The use of ELISA in an inhibition system,conducted with chickpea proteinantiserum raised in rabbits, showed that enzymatic hydrolysis resultedin a considerable reductionin the antigenic character of the proteins. Thus, the percentageinhibition by the α-chymotrypsinof hydrolysate was 58 ± 2.3% and that by the bromelain hydrolysatewas 45 ± 4.5%. The peptideswere measured by size exclusion chromatography. Peptides withmolar mass lower than 1000 Dacould be fractionated into fraction F1 containing peptides with molarmass higher than 500 Da,fraction F2 containing peptides with molar mass included between 200and 500 Da, essentiallysmall peptides containing 2, 3, or 4 amino acids, and fraction F3containing free amino acids. Thepurified fractions were quantified with the TNBS method(2,4,6-trinitrobenzenesulfonic acid). Thesmall peptides in fraction F2 were separated by reverse phase HPLC andwere sequenced. Keywords: Chickpea; hydrolysates; bromelain; α-chymotrypsin;antigenicity; ELISA; HP SEC
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