Nutritional Significance of Lectins and Enzyme Inhibitors from Legumes

Implications of antinutritional components in soybean foods

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evaluation of natural vs. synthetic substrates for measuring the antitryptic activity of soybean samples

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Chemopreventive Agents

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The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent

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The Evidence for Soybean Products as Cancer Preventive Agents

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Grain quality of common beans

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Food legumes in human nutrition: A personal perspective

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Consumption of diets containing raw soya beans (Glycine max), kidney beans (Phaseolus vulgaris), cowpeas (Vigna unguiculata) or lupin seeds (Lupinus angustifolius) by rats for up to 700 days: effect on body composition and organ weights

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Biological Effects of Plant Lectins on the Gastrointestinal Tract: Metabolic Consequences and Applications.

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Single-dose administration of Bowman-Birk inhibitor concentrate in patients with oral leukoplakia.

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Heat inactivation of the Kunitz and Bowman-Birk soybean protease inhibitors

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Physical, Chemical, and Nutritional Properties of Common Bean (Phaseolus) Proteins

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Composition and digestibility of albumin, globulins, and glutelins from Phaseolus vulgaris

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Reversible effect of phytohaemagglutinin on the growth and metabolism of rat gastrointestinal tract.

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Dietary lectins are metabolic signals for the gut and modulate immune and hormone functions.

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Biological Effects and Survival of Trypsin Inhibitors and the Agglutinin from Soybean in the Small Intestine of the Rat

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Red kidney bean lectin is a potent cholecystokinin releasing stimulus in the rat inducing pancreatic growth

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Biochemical basis for the differences in plant protein utilization

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Expression of the Insecticidal Bean α-Amylase Inhibitor Transgene Has Minimal Detrimental Effect on the Nutritional Value of Peas Fed to Rats at 30% of the Diet

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Bowman-Birk Inhibitor Concentrate Reduces Colon Inflammation in Mice with Dextran Sulfate Sodium-Induced Ulcerative Colitis

Ware, J. H., Wan, X. S., Newberne, P. M., et al. (1999) · Digestive Diseases and Sciences · doi:10.1023/a:1026616832119 · Cited by 69 · see citing works

Inhibition of Starch Digestion by α-Amylase Inhibitor Reduces the Efficiency of Utilization of Dietary Proteins and Lipids and Retards the Growth of Rats

Pusztai, A. J., Grant, G., Duguid, T. J., et al. (1995) · Journal of Nutrition · doi:10.1093/jn/125.6.1554 · Cited by 67 · see citing works

The effect of phytohaemagglutinin at different dietary concentrations on the growth, body composition and plasma insulin of the rat

Bardócz, S., Grant, G., Pusztai, A. J., et al. (1996) · British Journal Of Nutrition · doi:10.1079/bjn19960067 · Cited by 67 · see citing works

Inactivation of soya bean trypsin inhibitors by thiols

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Lipid accumulation in obese Zucker rats is reduced by inclusion of raw kidney bean (Phaseolus vulgaris) in the diet

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Trypsin inhibitor activity of conventional foods which are part of the British diet and some soya products

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Unavailability of Cystine from Trypsin Inhibitors as a Factor Contributing to the Poor Nutritive Value of Navy Beans

Kakade, M. L., Arnold, R. L., Liener, I. E., et al. (1969) · Journal of Nutrition · doi:10.1093/jn/99.1.34 · Cited by 49 · see citing works

α‐Amylase inhibitor levels in seeds generally available in Europe

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Effect of the β‐adrenoceptor agonist clenbuterol and phytohaemagglutinin on growth, protein synthesis and polyamine metabolism of tissues of the rat

Bardócz, S., Brown, D. S., Grant, G., Pusztai, A. J., Stewart, J. C., & Palmer, R. M. (1992) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1992.tb14359.x · Cited by 47 · see citing works

Mechanism of porcine pancreatic α‐amylase

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A comprehensive scheme for the isolation of trypsin inhibitors and the agglutinin from soybean seeds

Pusztai, A. J., Watt, W. B., & Stewart, J. C. (1991) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00005a009 · Cited by 37 · see citing works

Gastrointestinal responses to a panel of lectins in rats maintained on total parenteral nutrition

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Influence of naturally acid-soluble proteins from beans (Phaseolus vulgaris L.) on in vitro digestibility determination

Genovese, M. I., & Lajolo, F. M. (1998) · Food Chemistry · doi:10.1016/s0308-8146(97)00224-0 · Cited by 36 · see citing works

Screening of heat-stable trypsin inhibitors in dry beans and their partial purification from Great Northern beans (Phaseolus vulgaris) using anhydrotrypsin-Sepharose affinity chromatography

Rayas‐Duarte, P., Bergeron, D., & Nielsen, S. S. (1992) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00013a007 · Cited by 34 · see citing works

The induction of gut hyperplasia by phytohaemagglutinin in the diet and limitation of tumour growth.

Pryme, I. F., Pusztai, A. J., Bardócz, S., et al. (1998) · PubMed · doi:10.14670/hh-13.575 · Cited by 34 · see citing works

Amylase inhibitors in Phaseolus vulgaris beans

Lajolo, F. M., Filho, F. F., & de Menezes, E. W. (1991) · Food technology · Cited by 33 · see citing works

Characterization of a purified α-amylase inhibitor from white kidney beans (Phaseolus vulgaris)

Gibbs, B. F., & Alli, I. (1998) · Food Research International · doi:10.1016/s0963-9969(98)00074-x · Cited by 31 · see citing works

Wine vinegar production using base wines made with different yeast species

Ciani, M. (1998) · Journal of the Science of Food and Agriculture · doi:10.1002/(sici)1097-0010(199810)78:2 · Cited by 28 · see citing works

Relationship between protease activity and neu oncogene expression in patients with oral leukoplakia treated with the Bowman Birk Inhibitor.

Wan, X. S., Meyskens, F. L., Armstrong, W. B., et al. (1999) · PubMed · Cited by 28 · see citing works

In Vitro Digestibility of Albumin Proteins from Phaseolus vulgaris L. Effect of Chemical Modification

Genovese, M. I., & Lajolo, F. M. (1996) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9507304 · Cited by 27 · see citing works

Twin-Screw Extrusion Cooking of Small White Beans (Phaseolus vulgaris)

Edwards, R. H., Becker, R. R., Mossman, A. P., Gray, G. M., & Whitehand, L. C. (1994) · LWT · doi:10.1006/fstl.1994.1095 · Cited by 26 · see citing works

Nutritional value of cooked beans (Phaseolus vulgaris) and their isolated major protein fractions

Marquez, Ú. M. L., & Lajolo, F. M. (1990) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.2740530211 · Cited by 25 · see citing works

In vivo digestibility of bean (Phaseolus vulgaris L.) proteins: the role of endogenous protein

Marquez, Ú. M. L., & Lajolo, F. M. (1991) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00007a003 · Cited by 22 · see citing works

The use of enzymic hydrolysis in vitro to study the digestibility of some phaseolus seed proteins

Bradbear, N., & Boulter, D. (1984) · Plant Foods for Human Nutrition · doi:10.1007/bf01095068 · Cited by 22 · see citing works

THERMAL EXTRUSION and ALKALI PROCESSING of DRY BEANS (PHASEOLUS VULGARIS L.)

COFFEY, D. G., Uebersax, M. A., HOSFIELD, G. L., et al. (1993) · Journal of Food Processing and Preservation · doi:10.1111/j.1745-4549.1993.tb00220.x · Cited by 21 · see citing works

Polyamine metabolism of enterocyte-like Caco-2 cells after exposure to Phaseolus vulgaris lectin.

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Both free and complexed trypsin inhibitors stimulate pancreatic secretion and change duodenal enzyme levels

Pusztai, A., Grant, G., Bardócz, S., et al. (1997) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1997.272.2.g340 · Cited by 18 · see citing works

Secretion of Pancreatic Digestive Enzymes Induced in Rats by First-Time Oral Exposure to Kidney Bean E2L2 Lectin Is Mediated Only in Part by Cholecystokinin (CCK)

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N'-Acyl and N'-nitroso pyridine alkaloids in alkaloid lines of burley tobacco during growth and air-curing

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Occurrence and purification of .alpha.-amylase isoinhibitors in bean (Phaseolus vulgaris L.) varieties

Iguti, A. M., & Lajolo, F. M. (1991) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00012a006 · Cited by 15 · see citing works

EFFECT OF BEAN (Phaseolus vulgaris) ALBUMINS ON PHASEOLIN IN VITRO DIGESTIBILITY, ROLE OF TRYPSIN INHIBITORS

Genovese, M. I., & Lajolo, F. M. (1996) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.1996.tb00556.x · Cited by 15 · see citing works

Protease Inhibitors in Processed Plant Foods

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ATIVIDADE INIBITÓRIA DE TRIPSINA EM PRODUTOS DERIVADOS DE SOJA (Glycine max) CONSUMIDOS NO BRASIL

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Effect of oral phytohaemagglutinin intake on cell adaptation in the epithelium of the small intestine of the rat.

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[Antinutritional effect of phytohemagglutinins of Phaseolus vulgaris L].

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Resistance of cranberry bean (Phaseolus vulgaris) α-amylase inhibitor to intraluminal digestion and its movement along rat gastrointestine: Further investigation using a radioactive probe and specific antiserum

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Occurrence in leguminous seeds, resistance to protease digestion and antigenicity of an α-amylase inhibitor

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Minor components of pulses and their potential impact on human health

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Pulses for Bread Fortification: A Necessity or a Choice?

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Valorization of Microalgae as Multifunctional Protein Sources in Plant-Based Systems: Structural, Functional, and Processing Challenges

Boza, A., Lemos, E., Bürck, M., Gautério, G. V., & Braga, A. R. C. (2026) · Macromol · doi:10.3390/macromol6030054

REACTION OF LENTIL PROTEINASE INHIBITORS WITH HUMAN AND BOVINE TRYPSIN AND CHYMOTRYPSIN

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STUDY OF PROTEASES AND PROTEASE INHIBITORS FROM STREPTOMYCES STRAINS

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Use of modified superabsorbent polymer dressings for protease modulation in improved chronic wound care.

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KARAKTERISASI PROTEASE DARI ISOLAT BAKTERI ASAL TUMBUHAN RAWA DARI INDRALAYA

Baehaki, A., & Rinto (2012) · Jurnal Pengolahan Hasil Perikanan Indonesia · doi:10.17844/jphpi.v15i1.5335

Ascaridia galli: Trypsin and chymotrypsin inhibitors

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