Abstract
White kidney beans (Phaseolus vulgaris), cv Processor, contain a relatively high content of phaseolin (storage protein), lectins and a special group of glycoproteins as well as a considerable amount of protein-type trypsin inhibitors. Protein digestion of raw ‘Processor’ beans in monogastrics, for example pigs, is disturbed by poorly digested, phaseolin lectins, which can bind to carbohydrates in brush border membranes of the small intestinal epithelium, and trypsin inhibitors. The effect of the germination of white kidney beans on lectins, phaseolin and trypsin inhibitors was studied in order to achieve a degradation of lectins, phaseolin and trypsin inhibitors and an increase ofin vitro enzymatic hydrolysis of the protein of bean flour. Therefore, whole bean extracts were examined throughout a germination period of up to seven days for their lectin and phaseolin pattern, lectin content, binding capacities of functional lectins towards brush border membranes and trypsin inhibitor content. In addition thein vitro enzymatic hydrolysis by pepsin and pancreatin of the protein from flours of (un)germinated white kidney beans was studied. SDS-PAGE demonstrated a degradation of E-lectins and a disappearance of L-lectins and phaseolin during germination. Results indicated a decrease of the lectin content by 85%, a loss of binding capacities of functional lectins towards brush border membranes by 91%, and a decrease of trypsin inhibitors by 76%, in bean flour after germination for seven days. A maximum inin vitro enzymatic hydrolysis of protein from bean flour was already established after germination for half a day.
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References
Boylan MT, Sussex JM (1987) Purification of an endopeptidase involved with storage-protein degradation inPhaseolus vulgaris L., cotelydons. Planta 170: 343–352
Chang KC, Harrold RL (1988) Changes in selected biochemical components, in vitro protein digestibility and amino acids in two bean cultivars during germination. J Food Sci 56: 783–787
Feldsted RL, Leavitt RD, Bachur NR (1975) Purification of the phytohemagglutinin family of proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatography. Biochim Biophys Acta 405: 72–81
Felsted RL. Leavitt RD, Chen C, Bachur NR, Dale RMK (1981) Phytohemagglutinin isolectin subunit composition. Biochim Biophys Acta 668: 132–140
Goldstein IJ, Poretz RD (1986) Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins. in: The Lectins. Academic Press, London, pp. 33–247
Hamer RJ, Koninkx JFJG, van Oort MG, Mouwen JMVM, Huisman J (1988) New developments in lectin analysis. In: Recent Advances of Research in Antinutritional Factors in Legume Seeds. Pudoc, Wageningen, pp. 30–33
Hill HD, Straka JG (1988) Protein determination using bicinchoninic acid in the presence of sulfhydryl reagents. Anal Biochem 170: 203–208
Jacob RT, Pattabiraman TN (1986) Natural plant enzyme inhibitors: isolation and properties of a trypsin/chymotrypsin inhibitor from kidney bean (Phaseolus vulgaris). Ind J Biochem Biophys 23: 105–109
Kik MJL, Rojer JM, Mouwen JMVM, Koninkx JFJG, van Dijk JE, van der Hage MH (1989) The interaction between plant lectins and the small intestinal epithelium: A primary cause of intestinal disturbance. Vet Quart 11: 108–115
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 22: 680–685
Liener IE (1989) Antinutritional factors in legume seeds: state of the art. In: J Huisman, AFB Van der Poel and IE Liener (eds.): Recent advances of research in antinutritional factors in legume seeds. Pudoc, Wageningen, pp 6–14
Moreno J, Altabella T, Chrispeels MJ (1990) Characterization of α-amylase-inhibitor, a lectin-like protein in the seeds ofPhaseolus vulgaris. Plant Physiol 92: 703–709
Müntz K, Bassüner R, Lichtenfeld C, Schölz G, Weber E (1985) Proteolytic cleavage of storage proteins during embryogenesis and germination of legume seeds. Physiol Veg 23: 75–94
Nielson SS, Liener IE (1984) Degradation of the major storage protein ofPhaseolus vulgaris during germination. Plant Physiol 74: 494–498
Nielson SS, Liener IE (1988) Effect of germination on trypsin inhibitor and hemagglutinating activities inPhaseolus vulgaris. J Food Sci 53: 298–301
Pusztai A, Stewart JC (1978) Isolectins ofPhaseolus vulgaris. Physicochemal studies. Biochim Biophys Acta 536: 38–49
Pusztai A, Watt WB (1974) Isolectins ofPhaseolus vulgaris: A comprehensive study of fractionation. Biochim Biophys Act 365: 57–71
Roberts DD, Goldstein IJ (1984) Isolation from Lima bean lectin of a peptide containing a cysteine residue essential for carbohydrate binding activity. J Biol Chem 256: 909–914
Roozen RJ, de Groot J (1992) Analysis of trypsin inhibitors and lectins in white kidney beans (Phaseolus vulgaris var Processor) in a combined method. AOAC, in press
Savelkoul FHMG, Van der Poel AFB, Tamminga S (1992) The presence and inactivation of trypsin inhibitors, tannins, lectins and amylase inhibitors in legume seeds during germination. Plant Fds Hum Nutr 42: 71–85
Savelkoul FHMG, Schepers AJ, Boer H, Tamminga S (1990) The in vitro protein digestibility of germinated legumes. 41st Annual Meeting E A A P, Toulouse 1: 334–335
Savelkoul FHMG, Boer H, Tamminga S, Schepers AJ, Elburg L (1992) In vitro enzymatic hydrolysis of protein and protein pattern change of soya and faba beans during germination. Plant Fd Hum Nutr 42: 275–284
Tsukamoto I, Miyoshi M, Hamaguchi Y (1983) Purification and characterization of three trypsin inhibitors from beans,Phaseolus vulgaris ‘Kintoki’. Cereal Chem 60: 281–286
Van der Burg WJ, Bekendam J, van Geffen A, Heuver M (1983) Project seed laboratory 2000–5000. Seed Sci Technol 11: 157–227
Van der Poel AFB (1990) Effects of processing on bean (Phaseolus vulgaris L.) protein quality. Ph.D Thesis, Ponsen & Looyen, Wageningen
Van der Poel AFB, Mollee PW, Huisman J, Liener IE (1990) Variations among species of animals in response to the feeding of heat-processed beans (Phaseolus vulgaris L.). Livest Prod Sci 25: 121–150
Wilson KA, Laskowski M (1972) Isolation of three isoinhibitors of trypsin from garden bean,Phaseolus vulgaris, having either lysine or arginine at the reactive site. J Biol Chem 248: 756–762
Wilson KA, Papastoitis G, Hartl P, Tan-Wilson AL (1988) Survey of the proteolytic activities degrading the Kunitz trypsin inhibitor and glycinin in germinating soybeans (Glycine max). Plant Physiol 88: 355–360
Wiseman J, Cole DJA (1988) European legumes in diets for non-ruminants. In: Recent Advances in Animal Nutrition. Butterworths, London, pp 13–37
Yomo H, Srinivasan K (1973) Protein breakdown and formation of protease in attached and detached cotyledons ofPhaseolus vulgaris L. Plant Physiol 52: 671–673
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Savelkoul, F.H.M.G., Tamminga, S., Leenaars, P.P.A.M. et al. The degradation of lectins, phaseolin and trypsin inhibitors during germination of white kidney beans,Phaseolus vulgaris L.. Plant Food Hum Nutr 45, 213–222 (1994). https://doi.org/10.1007/BF01094091
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DOI: https://doi.org/10.1007/BF01094091