{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T14:54:32Z","timestamp":1791816872582,"version":"4.3.4"},"reference-count":50,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2024,9,18]],"date-time":"2024-09-18T00:00:00Z","timestamp":1726617600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Nutr."],"abstract":"<jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Protein hydrolysates derived from food sources contains enormous number of peptides which are composed of amino acid possessess various bioactive properties. However, the use of protein hydrolysates as a nutraceutical is hindered due to their unpleasant flavour. The study aims to enhance the biological activity and palatability of protein hydrolysates.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methodology<\/jats:title>\n                    <jats:p>In the present study, soybean protein hydrolysate (SPH) was prepared using alcalase for 4\u2009h (control). Modification of hydrolysis (MPH) was carried out by reiterating the hydrolysis of the supernatant obtained after 2\u2009h of hydrolysis using an enzyme to 50% of alcalase during each successive hydrolysis. Samples were characterised by their physio-chemical and functional properties. Furthermore, the effect of modification on the protein digestibility and bitterness intensity using e-tongue was studied. The suppressive effect on retrogradation of corn starch was analysed using texture profile analysis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      The results demonstrated increased protein content by 1.6 and 1.9% in MPH compared to SPH and UNH, respectively. MPH showed 1.5- and 1.6-fold higher DH% than SPH before and after gastrointestinal digestion (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&amp;lt;\u20090.05). A decrease in molecular weight was found in the order of UNH\u2009&amp;gt;\u2009SPH\u2009&amp;gt;\u2009MPH. Nevertheless, MPH displayed significantly higher functional properties (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009\u2264\u20090.05). The hardness of retrograded corn starch was significantly reduced in the MPH (1.21N) than SPH (1.55\u2009N) and UNH (1.81N) compared to control (1.71N) during 7-day storage at 4\u00b0C\n                      <jats:italic>(p<\/jats:italic>\n                      \u2009\u2264\u20090.05). E-tongue analysis of MPH showed a 4-fold reduction in bitterness than SPH.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>Modification of hydrolysis of soybean has demonstrated its significance in improved DH% functional properties and palatability. In addition, improved protein digestibility with promising benefits in deferral action on retrogradation of starch over the traditional process of hydrolysis was observed. The outcome of this study contributes to the potential utilisation of MPH as an ingredient in the formulation of nutraceutical products.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fnut.2024.1444329","type":"journal-article","created":{"date-parts":[[2024,9,18]],"date-time":"2024-09-18T00:32:56Z","timestamp":1726619576000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":13,"title":["The role of duel hydrolysis of soybean on functional properties and protein digestibility: a sustainable approach"],"prefix":"10.3389","volume":"11","author":[{"given":"Nishithkumar","family":"Jogi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Somya","family":"Adusumilli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Madhukar","family":"Nagesh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sudheer Kumar","family":"Yannam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bangera Sheshappa","family":"Mamatha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2024,9,18]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"598","DOI":"10.1016\/j.foodres.2014.07.015","article-title":"Functional properties and Angiotensin-I converting enzyme inhibitory activity of soy \u2013 whey proteins and fractions","volume":"64","author":"Lassissi","year":"2014","journal-title":"FRIN"},{"key":"ref2","doi-asserted-by":"publisher","first-page":"8986","DOI":"10.1080\/10408398.2021.1938508","article-title":"Antihypertensive activity of orally consumed ACE-I inhibitory peptides","volume":"62","author":"Jogi","year":"2021","journal-title":"Crit Rev Food Sci Nutr"},{"key":"ref3","doi-asserted-by":"publisher","first-page":"1844","DOI":"10.1111\/1750-3841.14683","article-title":"Antioxidant and antimicrobial activity of porcine liver hydrolysate in meat emulsion and their influence on Physico-chemical and color deterioration during refrigeration storage","volume":"84","author":"Verma","year":"2019","journal-title":"J Food Sci"},{"key":"ref4","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1080\/22311866.2021.1953399","article-title":"Bioactivity and functional properties of protein hydrolysate from muscle and visceral waste of ribbon fish (Lepturacanthus savala)","volume":"11","author":"Yathisha","year":"2021","journal-title":"Extracted Three Differ Proteolytic Enzymes"},{"key":"ref5","doi-asserted-by":"publisher","first-page":"8","DOI":"10.3390\/nu10091211","article-title":"Soybean bioactive peptides and their functional properties","volume":"10","author":"Chatterjee","year":"2018","journal-title":"Nutrients"},{"key":"ref6","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1016\/j.foodres.2018.01.030","article-title":"High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates","volume":"106","author":"Hanafi","year":"2018","journal-title":"Food Res Int"},{"key":"ref7","doi-asserted-by":"publisher","first-page":"112096","DOI":"10.1016\/j.lwt.2021.112096","article-title":"Combining Alcalase hydrolysis and transglutaminase-cross-linking improved bitterness and techno-functional properties of hypoallergenic soybean protein hydrolysates through structural modifications","volume":"151","author":"Zhang","year":"2021","journal-title":"LWT"},{"key":"ref8","doi-asserted-by":"publisher","first-page":"e12978","DOI":"10.1111\/jfbc.12978","article-title":"Bitterness of fish protein hydrolysate and its debittering prospects","volume":"43","author":"Idowu","year":"2019","journal-title":"J Food Biochem"},{"key":"ref9","doi-asserted-by":"publisher","first-page":"3336","DOI":"10.1007\/s13197-014-1394-7","article-title":"Antioxidant and sensory properties of protein hydrolysate derived from Nile tilapia (Oreochromis niloticus) by one- and two-step hydrolysis","volume":"52","author":"Yarnpakdee","year":"2015","journal-title":"J Food Sci Technol"},{"key":"ref10","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1300\/J030v13n02_09","article-title":"Bitterness in fish protein hydrolysates and methods for removal","volume":"13","author":"Dauk\u0161as","year":"2004","journal-title":"J. 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