The contribution of trypsin inhibitors to the nutritional value of chick pea seed protein

Shamanthaka Sastry, M. C. and Murray, D. R. (1987) The contribution of trypsin inhibitors to the nutritional value of chick pea seed protein. Journal of the Science of Food and Agriculture, 40 (3). pp. 253-261.

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Abstract

Trypsin inhibitors (TI) from seeds of a Mediterranean (Kabuli) chick pea (Cicer arietinum L.) were isolated using trypsin-Sepharose 6B affinity chromatography and found to constitute 5.03% of extractable seed protein. The TI consisted predominantly of low mol. wt. spp., estimated at 9000 and 8000 Dalton by disc gel electrophoresis. Polypeptides in these regions of the gel were preferentially labelled by -3-5SO4-2-- fed via the cut stem to fruiting stalks of chick pea plants. A molar ratio of 1.8 was determined for the inhibition of trypsin by these inhibitors, whereas chymotrypsin was almost uninhibited. They are therefore `double-headed' inhibitors with both sites specific for trypsin, rather than with one site specific for each of trypsin and chymotrypsin, as reported for other lines of chick pea. Thus TI may contribute to the quality of the albumin fraction of chick pea seeds with respect to their contents of essential amino acids, and their failure to affect chymotrypsin. [From En summ.]

Item Type:	Article
Uncontrolled Keywords:	TRYPSIN-; chick-peas, trypsin inhibitors & nutritional values of; INHIBITION-; NUTRITIONAL-VALUES; LEGUMES-; chick-peas, chymotrypsin inhibitors absence from; PROTEINASES-
Subjects:	600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins 600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions:	Lipid Science and Traditional Foods
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	23 Jul 2008 04:52
Last Modified:	04 Jun 2019 10:55
URI:	http://ir.cftri.res.in/id/eprint/2159

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