Abstract
Proteinase inhibitory activity in ten different varieties ofDolichos lablab perpureus. L. was determined. All the varieties tested exhibited appreciable level of proteinase inhibitory activity (PIA). The trypsin inhibitory activity (TIA) (Mean:20170 TIU/g) was relatively higher than the chymotrypsin inhibitory activity (CIA) (Mean: 15380 CIU/g). Effect of temperature and cooking on PIA was studied. The nature of cooking medium and duration of cooking had profound effect on the PIA. The dry fried seeds lost their PIA very rapidly (91% in 20 min). Seeds cooked in slightly alkaline medium lost their PIA quickly (89% in 30 min) compared to those cooked in acidic (80% in 30 min) and neutral pH (83% in 30 min). The PIA in green pods was also determined and they had only one third of the PIA (8200 TIU/g and 8125 CIU/g) found in the dry seeds.
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Laskowski Jr M, Kato I (1980) Protein inhibitors of proteinases. Ann Rev Biochem 49: 593–626.
Liener IE (1979) Nutritional significance of plant protein inhibitors. Proc Nutr Soc 38: 109–118.
Richardson M (1977) The protein inhibitors of plant and microorganisms. Phytochem 16: 159–169.
Prabhu KS, Saldhana K, Pattabiraman TN (1984) Natural enzyme inhibitors: A comparative study of the action of legume inhibitors on bovine and human pancreatic proteinases. J Sci Food Agric 35: 314–321.
Friedman M, Gumbman R (1986) Nutritional improvement of legume proteins through disulfide interchange. In: Friedman M (ed), Nutritional and toxicological significance of enzyme inhibitors in foods. New York: Plenum Press, pp 357–390.
Rackis JJ, Wolf WJ, Baker EC (1986) Proteinase inhibitors in plant foods. In: Friedman M (ed), Nutritional and toxicological significance of enzyme inhibitors in foods. New York: Plenum Press, pp 299–310.
Sastry BN (1952) In: Wealth of India: A dictionary of Indian materials and industrial products. New Delhi, CSIR, Vol. III, pp 106–107.
Banarji AP, Kamala S (1969) Trypsin inhibitors from field bean: Isolation, purification and properties of a trypsin inhibitor from field bean. Enzymologia 36: 137–152.
Kamala S, Ambe AS (1955) Crystalline trypsin inhibitors form Indian field bean and double bean. Nature 175: 108–109.
Weeder JKP (1986) Inhibition of human proteinases by grain legumes. In: Friedman M (ed), Nutritional and toxicological significance of enzyme inhibitors in foods New York: Plenum Press, pp 239–279.
Rayas-Duarte P, Kergeron D, Nielson SS (1992) Screening of heat stable trypsin inhibitors in red kidney beans and their partial purification from great northern beans. J Agric Food Chem 40: 32–42.
Richardson M (1991) Storage proteins of plants. In: Dey PM, Harborne JB (eds), Methods in plant biochem, 5. New York: Academic Press, pp 259–309.
Veerabhadrappa PS, Manjunath NH, Virupaksha TK (1981) Proteinase inhibitors of finger millet. J Sci Food Agric 29: 353–358.
Kakade ML, Simson N, Liener IE (1969) The evaluation of synthetic substrates for measuring antitryptic activity in soybean samples. Cereal Chem 46: 518–526.
Kakade ML, Swenson DH, Liener IE (1970) Note on determination of chymotrypsin inhibitory activity using casein. Anal Biochem 33: 255–258.
Ramasarma PR, Rao R (1991) Nature of tryptic and chymotryptic inhibitors from horse gram. Indian J Biochem Biophys 28: 418–424.
Chadrashekar G, Raju DS, Pattabiraman TN (1982) Natural plant enzyme inhibitors: Proteinase inhibitors in millets. J Sci Food Agric 33: 447–450.
Ambe KS, Kamala S (1956) Studies on trypsin inhibitors in Indian food stuffs. J Sci Industr Res 15C: 136–139.
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Devaraj, V.R., Manjunath, N.H. Effect of cooking on proteinase inhibitors ofDolichos lablab bean (Dolichos lablab perpureus L.). Plant Food Hum Nutr 48, 107–112 (1995). https://doi.org/10.1007/BF01088305
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DOI: https://doi.org/10.1007/BF01088305