ArticleJournal of food science2022
Physico-chemical properties, antioxidant activity, and ACE inhibitory activity of protein hydrolysates from wild jujube seed.
Article in Journal of food science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Peony seed meal supplementation enhances semen quality in aged Qinchuan bulls.Animal biotechnology · 2025Article
- Effect of buckwheat bran protein enzymatic hydrolysates on the rheological, textural and structural properties of non-fermented wheat dough.Food chemistry: X · 2025Article
- Screening of Potential Angiotensin-Converting Enzyme-Inhibitory Peptides in Squid (Marine drugs · 2025Article
- Identification and Functional Validation of Two Novel Antioxidant Peptides in Saffron.Antioxidants (Basel, Switzerland) · 2024Article
- Evaluation of egg white hydrolysates on the hepatoprotective effect in vitro and in vivo.Journal of food science and technology · 2023Article
- Physico-chemical properties, antioxidant activity, and ACE inhibitory activity of protein hydrolysates from wild jujube seed.Journal of food science · 2022Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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-inflammatory 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-chemical properties, antioxidant activity, and angiotensin converting enzyme (ACE) inhibitory activity in vitro have been investigated for the first time. SDS-PAGE electrophoresis and size-exclusion chromatographic results indicate that WJSPHs have lower molecular weight distribution (< 5,000 Da) 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-scavenging ability of 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals (94.60%), 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS
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