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Inhibitor activities of chickpeas ( Cicer arietinum L) against bovine, pocine and human trypsin and chymotrypsin
Author(s) -
Saini Harpal S.,
Weder Jürgen K. P.,
Knights Edmund J.
Publication year - 1992
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740600304
Subject(s) - chymotrypsin , trypsin , isoelectric focusing , trypsin inhibitor , biology , enzyme , kunitz sti protease inhibitor , biochemistry , chemistry , food science
Twenty‐two chickpea samples (7 genotypes, 4 desi and 3 kabuli) representing three different sites of cultivation and three years of harvest were examined for their inhibitory activities against bovine, porcine and human trypsin/chymotrypsin, and compared for their isoinhibitor patterns. No significant difference in inhibitor activity between the desi and kabuli seed types was found for any of the enzymes used, when data from different locations and years were averaged. However, some significant differences were observed between individual cultivars when compared at the same location and in the same year. Inhibitor activities against the three trypsins and three chymotrypsins were statistically different with activities against bovine (5.46 ± 1.21) > porcine (5.24 ± 1.18) > human (4.45 ± 0.93) trypsin and those against bovine (4.89 ± 1.27) < porcine (8.91 ± 2.14) < human (10.54 ± 2.50) chymotrypsin (means ± standard deviation, expressed as mg active enzyme completely inhibited per g seed meal). Levels of activity of both trypsin and chymotrypsin inhibitor were influenced by the location and year of cultivation. Isoelectric focusing yielded identical inhibitor patterns for all samples, indicating seven isoinhibitors acting against trypsin and chymotrypsin. Results are discussed in relation to nutritional significance of these inhibitors and perspectives for breeding genotypes low in protcase inhibitors.