References

• Adler-Nissen, J. (2002). Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry, 27, 1256–1262.
   Google Scholar
• Amadou, I., Gounga, M. E., & Le, G. W. (2013). Millets: Nutritional composition, some health benefits and processing – A review. Emirates Journal of Food and Agriculture, 25(7), 501–508.
   Web of Science ®Google Scholar
• Becker, A., Boulaaba, A., Pingen, S., Krischek, C., & Klein, G. (2016). Low temperature cooking of pork meat — Physicochemical and sensory aspects. Meat Science, 118, 82–88.
   PubMed Web of Science ®Google Scholar
• Bora, P., Ragaee, S., & Marcone, M. (2019). Effect of parboiling on decortication yield of millet grains and phenolic acids and in vitro digestibility of selected millet products. Food Chemistry, 274, 718–725.
   PubMed Web of Science ®Google Scholar
• Burris, R. L., Ng, H. P., & Nagarajan, S. (2014). Soy protein inhibits inflammation-induced VCAM-1 and inflammatory cytokine induction by inhibiting the NF-κB and AKT signaling pathway in apolipoprotein E-deficient mice. European Journal of Nutrition, 53(1), 135–148.
   PubMed Web of Science ®Google Scholar
• Charlier, C., & Michaux, C. (2003). Dual inhibition of cyclooxygenase-2 (COX-2) and 5-lipoxygenase (5-LOX) as a new strategy to provide safer non-steroidal anti-inflammatory drugs. European Journal of Medicinal Chemistry, 38(7–8), 645–659.
   PubMed Web of Science ®Google Scholar
• Chung, J. H., Kong, J. N., Choi, H. E., & Kong, K. H. (2018). Antioxidant, anti-inflammatory, and anti-allergic activities of the sweet-tasting protein brazzein. Food Chemistry, 267, 163–169.
   PubMed Web of Science ®Google Scholar
• Clausen, M. P., Christensen, M., Hveisel, T., Duelund, L., & Mouritsen, O. G. (2018). The quest for umami: Can sous vide contribute? International Journal of Gastronomy and Food Science, 13, 129–133.
   Web of Science ®Google Scholar
• Co, F., Bri, A., Mestres, C., Alter, P., Durand, N., & Bohuon, P. (2018). Multi-response modeling of reaction-diffusion to explain alpha-galactosidase behavior during the soaking-cooking process in cowpea. Food Chemistry, 242, 279–287.
   PubMed Web of Science ®Google Scholar
• Conforti, F., & Menichini, F. (2011). Foods of plant origin as source of nitric oxide production inhibitors. Handbook of nutritional biochemistry: genomics, metabolomics, and food supply. Nova Science Publishers, Inc.
   Google Scholar
• Cuniberti, B., Odore, R., Barbero, R., Cagnardi, P., Badino, P., Girardi, C., & Re, G. (2012). In vitro and ex vivo pharmacodynamics of selected non-steroidal anti-inflammatory drugs in equine whole blood. Veterinary Journal, 191, 327–333.
   PubMed Web of Science ®Google Scholar
• Czolpinska, M., & Rurek, M. (2018). Plant glycine-rich proteins in stress response: An emerging, still prospective story. Frontiers in Plant Science, 9, 1–13.
   PubMed Web of Science ®Google Scholar
• de la Garza, A. L., Milagro, F. I., Boque, N., Campión, J., & Martínez, J. A. (2011). Natural inhibitors of pancreatic lipase as new players in obesity treatment. Planta Medica, 77(8), 773–785.
   PubMed Web of Science ®Google Scholar
• Durak, A., Baraniak, B., Jakubczyk, A., & Świeca, M. (2013). Biologically active peptides obtained by enzymatic hydrolysis of Adzuki bean seeds. Food Chemistry, 141(3), 2177–2183.
   PubMed Web of Science ®Google Scholar
• El, M. T., El-Sharief, M. A. M. S., Zarie, E. S., Morsy, N. M., Elsheakh, A. R., Voronkov, A., … Hassan, G. S. (2018). Design, synthesis, anti-inflammatory activity and molecular docking of potential novel antipyrine and pyrazolone analogs as cyclooxygenase enzyme (COX) inhibitors. Bioorganic & Medicinal Chemistry Letters, 28(5), 952–957.
   PubMed Web of Science ®Google Scholar
• Gonzalez, R. R., Fong, T., Belmar, N., Saban, M., Felsen, D., & Te, A. (2005). Modulating bladder neuro-inflammation: RDP58, a novel anti-inflammatory peptide, decreases inflammation and nerve growth factor production in experimental cystitis. Journal of Urology, 173(2), 630–634.
   PubMed Web of Science ®Google Scholar
• González-Montoya, M., Hernández-Ledesma, B., Silván, J. M., Mora-Escobedo, R., & Martínez-Villaluenga, C. (2018). Peptides derived from in vitro gastrointestinal digestion of germinated soybean proteins inhibit human colon cancer cells proliferation and inflammation. Food Chemistry, 242, 75–82.
   PubMed Web of Science ®Google Scholar
• Gonzalez-Rey, E., Anderson, P., & Delgado, M. (2007). Emerging roles of vasoactive intestinal peptide: A new approach for autoimmune therapy. Annals of the Rheumatic Diseases, 66, 70–76.
   PubMed Web of Science ®Google Scholar
• Gulati, P., Li, A., Holding, D., Santra, D., Zhang, Y., & Rose, D. (2017). Heating reduces proso millet protein digestibility via formation of hydrophobic aggregates. Journal Of Agricultural and Food Chemistry, 65, 1952–1959. doi: 10.1021/acs.jafc.6b05574.
   PubMed Web of Science ®Google Scholar
• Gulati, P., Sabillón, L., & Rose, D. J. (2018). Effects of processing method and solute interactions on pepsin digestibility of cooked proso millet flour. Food Research International, 109, 583–588.
   PubMed Web of Science ®Google Scholar
• Gunderson, C. C., Ding, K., Dvorak, J., Moore, K. N., McMeekin, D. S., & Benbrook, D. M. (2016). The pro-inflammatory effect of obesity on high grade serous ovarian cancer. Gynecologic Oncology, 143(1), 40–45.
   PubMed Web of Science ®Google Scholar
• Gupta, N., Srivastava, A. K., & Pandey, V. N. (2012). Biodiversity and nutraceutical quality of some Indian millets. Proceedings of the National Academy of Sciences India Section B - Biological Sciences, 82(2), 265–273.
   Web of Science ®Google Scholar
• Gupta, S., Sharma, A. K., Shastri, V., Madhu, M. K., & Sharma, V. K. (2017). Prediction of anti-inflammatory proteins/peptides: An insilico approach. Journal of Translational Medicine, 15, 1–11.
   PubMed Web of Science ®Google Scholar
• Hansen, F. K., Khankischpur, M., Tolaymat, I., Mesaros, R., Dannhardt, G., & Geffken, D. (2012). Efficient synthesis and 5-LOX/COX-inhibitory activity of some 3-hydroxybenzo-β-thiophene-2-carboxylic acid derivatives. Bioorganic and Medicinal Chemistry Letters, 22(15), 5031–5034.
   PubMed Web of Science ®Google Scholar
• Hasegawa, S., Ichiyama, T., Sonaka, I., Ohsaki, A., Okada, S., Wakiguchi, H., … Furukawa, S. (2012). Cysteine, histidine and glycine exhibit anti-inflammatory effects in human coronary arterial endothelial cells. Clinical and Experimental Immunology, 167(2), 269–274.
   PubMed Web of Science ®Google Scholar
• Jakubczyk, A., Karaś, M., Złotek, U., & Szymanowska, U. (2017). Identification of potential inhibitory peptides of enzymes involved in the metabolic syndrome obtained by simulated gastrointestinal digestion of fermented bean (Phaseolus vulgaris L.) seeds. Food Research International, 100, 489–496.
   PubMed Web of Science ®Google Scholar
• Janus, A., Szahidewicz-Krupska, E., Mazur, G., & Doroszko, A. (2016). Insulin resistance and endothelial dysfunction constitute a common therapeutic target in cardiometabolic disorders. Mediators of Inflammation, 2016, 10. Article ID 3634948
   Web of Science ®Google Scholar
• Jawed, A., Singh, G., Kohli, S., Sumera, A., Haque, S., Prasad, R., & Paul, D. (2018). Therapeutic role of lipases and lipase inhibitors derived from natural resources for remedies against metabolic disorders and lifestyle diseases. South African Journal of Botany, 120, 25–32.
   Web of Science ®Google Scholar
• Kamara, M. T., Ming, Z. H., & Kexue, Z. (2009). Extraction, characterization and nutritional properties of two varieties of defatted foxtail millet flour (Setaria italica L.) grown in China. Asian Journal of Biochemistry,4, 88–98. doi:10.3923/ajb.2009.88.98
   Google Scholar
• Karaś, M., Baraniak, B., Rybczyńska, K., Gmiński, J., Gaweł-Bęben, K., & Jakubczyk, A. (2015). The influence of heat treatment of chickpea seeds on antioxidant and fibroblast growth-stimulating activity of peptide fractions obtained from proteins digested under simulated gastrointestinal conditions. International Journal of Food Science and Technology, 50(9), 2097–2103.
   Web of Science ®Google Scholar
• Karaś, M., Jakubczyk, A., Szymanowska, U., Złotek, U., & Zielińska, E. (2017). Digestion and bioavailability of bioactive phytochemicals. International Journal of Food Science and Technology, 52(2), 291–305.
   Web of Science ®Google Scholar
• Kim, M. Y., Jang, G. Y., Lee, Y. J., Woo, K. S., Hwang, B. Y., Lee, J., & Jeong, H. S. (2018). Identification of anti-inflammatory active peptide from black soybean treated by high hydrostatic pressure after germination. Phytochemistry Letters, 27, 167–173.
   Web of Science ®Google Scholar
• Kmiecik, W., Lisiewska, Z., Słupski, J., & Gȩbczyński, P. (2008). Effect of preliminary and culinary processing on amino acid content and protein quality in frozen French beans. International Journal of Food Science and Technology, 43(10), 1786–1791.
   Web of Science ®Google Scholar
• Korhonen, H., & Pihlanto, A. (2006). Bioactive peptides: Production and functionality. International Dairy Journal, 16, 945–960.
   Web of Science ®Google Scholar
• Maestri, E., Pavlicevic, M., Montorsi, M., & Marmiroli, N. (2018). Meta-analysis for correlating structure of bioactive peptides in foods of animal origin with regard to effect and stability. Comprehensive Reviews in Food Science and Food Safety, 18, 3–30.
   Web of Science ®Google Scholar
• Margier, M., Georgé, S., Hafnaoui, N., Remond, D., Nowicki, M., Du Chaffaut, L., … Reboul, E. (2018). Nutritional composition and bioactive content of legumes: Characterization of pulses frequently consumed in France and effect of the cooking method. Nutrients, 10(11), 1–12.
   Web of Science ®Google Scholar
• Martinez-Villaluenga, C., Rupasinghe, S. G., Schuler, M. A., & De, E. G. (2010). Peptides from purified soybean β-conglycinin inhibit fatty acid synthase by interaction with the thioesterase catalytic domain. Food Chemistry, 277, 1481–1493.
   Google Scholar
• Medici, L. O., Gonçalves, F. V., Da Fonseca, M. P. S., Gaziola, S. A., Schmidt, D., Azevedo, R. A., & Pimentel, C. (2018). Growth, yield and grain nutritional quality in three Brazilian pearl millets (Pennisetum americanum L.) with African or Indian origins. Anais Da Academia Brasileira de Ciencias, 90(2), 1749–1758.
   PubMed Web of Science ®Google Scholar
• Mittendorfer, B. (2013). Origins of metabolic complications in obesity: Adipose tissue and free fatty acid trafficking. Current Opinion in Clinical Nutrition and Metabolic Care, 14(6), 535–541.
   Web of Science ®Google Scholar
• Montoya-Rodríguez, A., & de Mejía, E. G. (2015). Pure peptides from amaranth (Amaranthus hypochondriacus) proteins inhibit LOX-1 receptor and cellular markers associated with atherosclerosis development in vitro. Food Research International, 77, 204–214.
   Web of Science ®Google Scholar
• Nosworthy, M. G., Medina, G., Franczyk, A. J., Neufeld, J., Appah, P., Utioh, A., … House, J. D. (2018). Effect of processing on the in vitro and in vivo protein quality of beans (Phaseolus vulgaris and Vicia Faba). Nutrients, 10(6), 1–13.
   Web of Science ®Google Scholar
• Nour, A. A. M., Ahmed, I. A. M., Babiker, E. E., & Ibrahim, M. A. E. M. (2015). Effect of supplementation and cooking on in vitro protein digestibility and anti-nutrients of pearl millet flour. American Journal of Food Science and Health, 1(3), 69–75.
   Google Scholar
• Pan, A., Zeng, H., Bi, G., Claude, F., & Feng, B. (2016). Heat-pretreatment and enzymolysis behavior of the lotus seed protein. Food Chemistry, 201, 230–236.
   PubMed Web of Science ®Google Scholar
• Qi, X., Cheng, L., Li, X., Zhang, D., Wu, G., Zhang, H., … Wang, Y. (2019). Effect of cooking methods on solubility and nutrition quality of brown rice powder. Food Chemistry, 274, 444–451.
   PubMed Web of Science ®Google Scholar
• Ribeiro, D., Freitas, M., Tomé, S. M., Silva, A. M. S., Porto, G., Cabrita, E. J., … Fernandes, E. (2014). Inhibition of LOX by flavonoids: A structure-activity relationship study. European Journal of Medicinal Chemistry, 72, 137–145.
   PubMed Web of Science ®Google Scholar
• Rombouts, I., Lagrain, B., Scherf, K. A., Koehler, P., & Delcour, J. A. (2015). Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation. Scientific Reports, 5, 1–12.
   Web of Science ®Google Scholar
• Rotondo, S., Dell, G., Manarini, S., Cerletti, C., & Evangelista, V. (2006). The lipoxygenase – Cyclooxygenase inhibitor licofelone prevents thromboxane A2-mediated cardiovascular derangement triggered by the inflammatory peptide fMLP in the rabbit. European Journal of Pharmacology, 546, 95–101.
   PubMed Web of Science ®Google Scholar
• Schneider, C., Pratt, D. A., Porter, N. A., & Brash, A. R. (2009). Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. Chemistry & Biology, 14(5), 473–488.
   Google Scholar
• Schulte, H., von Eckardstein, A., Cullen, P., & Assmann, G. (2001). Obesity and cardiovascular risk. Herz, 26(3), 170–177.
   PubMed Web of Science ®Google Scholar
• Silva-Sánchez, C., de la Rosa, A. P. B., León-Galván, M. F., de Lumen, B. O., de León-Rodríguez, A., & de Mejía, E. G. (2008). Bioactive peptides in amaranth seed. Journal of Agricultural and Food Chemistry, 56(4), 1233–1240.
   PubMed Web of Science ®Google Scholar
• Szymanowska, U., Jakubczyk, A., Baraniak, B., & Kur, A. (2009). Characterisation of lipoxygenase from pea seeds (Pisum sativum var. Telephone L.). Food Chemistry, 116(4), 906–910.
   Web of Science ®Google Scholar
• Toita, R., Kawano, T., Murata, M., & Kang, J. (2016). Biomaterials anti-obesity and anti-inflammatory effects of macrophage-targeted interleukin-10-conjugated liposomes in obese mice. Biomaterials, 110. 81–88. doi: 10.1016/j.biomaterials.2016.09.018
   PubMed Web of Science ®Google Scholar
• Wada, Y., & Lönnerdal, B. (2014). Bioactive peptides derived from human milk proteins – Mechanisms of action. Journal of Nutritional Biochemistry, 25(5), 503–514.
   PubMed Web of Science ®Google Scholar
• Weiner, H. L., Lemere, C. A., Maron, R., Spooner, E. T., Grenfell, T. J., Mori, C., & Issazadeh, S. (2000). Nasal Administration of amyloid-β peptide decreases cerebral amyloid burden in a mouse model of Alzheimer’s Disease. Annals of Neurology, 48, 567–579.
   PubMed Web of Science ®Google Scholar
• Werz, O., & Steinhilber, D. (2005). Development of 5-lipoxygenase inhibitors – Lessons from cellular enzyme regulation. Biochemical Pharmacology, 70(3), 327–333.
   PubMed Web of Science ®Google Scholar
• Wheeler, M. D., Ikejema, K., Enomoto, N., Stacklewitz, R. F., Seabra, V., Zhong, Z., … Thurman, R. G. (1999). Glycine: A new anti-inflammatory immunonutrient. Cellular and Molecular Life Sciences, 56(9–10), 843–856.
   PubMed Web of Science ®Google Scholar
• White, J. A., Fry, J. C., & Hart, R. J. (1986). An evaluation of the Waters Pico Tag System for the amino acid analysis of food materials. Journal of Automatic Chemistry, 8(4), 170–177.
   PubMedGoogle Scholar