{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T10:05:52Z","timestamp":1791281152698,"version":"4.1.0"},"reference-count":87,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2014,2,18]],"date-time":"2014-02-18T00:00:00Z","timestamp":1392681600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Food Science"],"published-print":{"date-parts":[[2014,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Bioactive peptides (BPs) are amino acid sequences derived from food proteins. Their relevance lies in the biological activities they have once they are released from the parent protein. BPs or protein hydrolysates can be commercialized as nutraceutical products or functional ingredients according to their activities. Different food protein sources have been researched for their potential to generate BPs. However, with the exception of lunasin (derived from soy), animal protein sources have been predominantly exploited as commercial BPs sources. On the other hand, pulses have shown diverse BP contents without further impact on their commercialization. Pulses are a rich source of protein in the human diet and their consumption has been associated with the prevention of chronic diseases. The beneficial effect in human health has been related to their micronutrients, phytochemical bioactive compounds, and recently BPs. This article reviews the current literature about pulse protein hydrolysates and BPs with proved angiotensin converting enzyme inhibitory, antioxidant, cancer preventing, and other health promoting activities. Proteolysis process is commonly achieved by digestive and microorganism enzymes. BP purification and identification has consisted mainly on size segregation procedures followed by mass spectrometry techniques. Hydrolysis time, peptide size, and hydrophobicity are employed as process variants and structural features relevant for the BP activities. Finally, some considerations about industrial processing and BPs used as functional food ingredients were reviewed.<\/jats:p>","DOI":"10.1111\/1750-3841.12365","type":"journal-article","created":{"date-parts":[[2014,2,18]],"date-time":"2014-02-18T09:37:15Z","timestamp":1392716235000},"source":"Crossref","is-referenced-by-count":137,"title":["Bioactive Peptides and Hydrolysates from Pulses and Their Potential Use as Functional Ingredients"],"prefix":"10.1111","volume":"79","author":[{"given":"Lidia","family":"L\u00f3pez\u2010Barrios","sequence":"first","affiliation":[{"name":"Centro de Biotecnolog\u00eda FEMSA Depto. de Biotecnolog\u00eda e Ingenier\u00eda de Alimentos Inst. Tecnol\u00f3gico y de Estudios Superiores de Monterrey\u2010Campus Monterrey  Av. Eugenio Garza Sada 2501 Sur Monterrey Nuevo Le\u00f3n C.P. 64849 M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janet A.","family":"Guti\u00e9rrez\u2010Uribe","sequence":"additional","affiliation":[{"name":"Centro de Biotecnolog\u00eda FEMSA Depto. de Biotecnolog\u00eda e Ingenier\u00eda de Alimentos Inst. Tecnol\u00f3gico y de Estudios Superiores de Monterrey\u2010Campus Monterrey  Av. Eugenio Garza Sada 2501 Sur Monterrey Nuevo Le\u00f3n C.P. 64849 M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergio O.","family":"Serna\u2010Sald\u00edvar","sequence":"additional","affiliation":[{"name":"Centro de Biotecnolog\u00eda FEMSA Depto. de Biotecnolog\u00eda e Ingenier\u00eda de Alimentos Inst. Tecnol\u00f3gico y de Estudios Superiores de Monterrey\u2010Campus Monterrey  Av. 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