{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:42:01Z","timestamp":1787013721482,"version":"build-2736575974"},"reference-count":53,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2022,5,3]],"date-time":"2022-05-03T00:00:00Z","timestamp":1651536000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["ift.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Food Science"],"published-print":{"date-parts":[[2022,6]]},"abstract":"<jats:sec>\n                    <jats:title>Abstract<\/jats:title>\n                    <jats:p>\n                      Wild jujube seed protein (WJSP) as one kind of functional food material has attracted much attention due to its highly nutritive and medicinal value in anti\u2010inflammatory and improving immunomodulatory ability. However, owing to its large molecular weight and complex structure, biological activities of WJSP were greatly limited and cannot be fully utilized by the human body. Therefore, how to improve the bioavailability of WJSP and develop promising WJSP nutritious materials is a great challenge. In this work, wild jujube seed protein hydrolysates (WJSPHs) were prepared from WJSP via enzymatic hydrolysis method, and their physico\u2010chemical properties, antioxidant activity, and angiotensin converting enzyme (ACE) inhibitory activity in vitro have been investigated for the first time. SDS\u2013PAGE electrophoresis and size\u2013exclusion chromatographic results indicate that WJSPHs have lower molecular weight distribution\u00a0(&lt;\u00a05,000\u00a0Da) than WJSP. Circular dichroism (CD) spectroscopy and Fourier transform infrared spectroscopy (FTIR) results illustrated that random coil is the main secondary structure of WJSPHs. Antioxidant experiments indicate that WJSPHs exhibit high radicals\u2010scavenging ability of 1,1\u2010diphenyl\u20102\u2010picrylhydrazyl (DPPH) radicals (94.60%), 2,2\u2032\u2010azinobis\u2010(3\u2010ethylbenzthiazoline\u20106\u2010sulfonate) (ABTS\n                      <jats:sup>+<\/jats:sup>\n                      ) radicals (90.84%), superoxide radicals (44.77%), and hydroxyl radicals (47.77%). In vitro, WJSPHs can significantly decrease the accumulation of reactive oxygen species (ROS) and malondialdehyde (MDA), and increase the activity of superoxide dismutase (SOD) and glutathione peroxidase (GSH\u2010Px) in HepG2 cells. Moreover, ACE activity was found that can be significantly inhibited by WJSPHs (73.02%). Therefore, all previously mentioned results suggest that WJSPHs may be a promising antioxidant food to prevent oxidative\u2010related diseases in future.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Practical Application<\/jats:title>\n                    <jats:p>This study shows that WJSPHs exhibit high antioxidant activity and ACE inhibitory activity in vitro, which provide potential application value as antioxidant peptides to prevent oxidative\u2010related diseases.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/1750-3841.16157","type":"journal-article","created":{"date-parts":[[2022,5,3]],"date-time":"2022-05-03T05:31:05Z","timestamp":1651555865000},"page":"2484-2503","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Physico\u2010chemical properties, antioxidant activity, and ACE inhibitory activity of protein 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