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Ace Inhibitor - Wiley Online Library

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Last Updated: 10 May 2022

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Physico‐chemical properties, antioxidant activity, and ACE inhibitory activity of protein hydrolysates from wild jujube seed

Because of its high nutritive and medicinal value in anti-inflammatory treatment and improving immunomodulatory function, Wild jujube seed protein, one form of functional food product, has attracted considerable interest. Hence, a big challenge is finding how to increase the bioavailability of WJSP and produce promising WJSP nutritious materials. For the first time, wild jujube seed protein hydrolysates were isolated from WJSP via enzymatic hydrolysis process, antioxidant capacity, and angiotensin converting enzyme inhibitory activity in vitro were investigated in this study. WJSPHs have lower molecular weight distribution than WJSP, according to SDS–PAGE electrophoresis and size–exclusion chromatographic data. In vitro, WJSPHs can significantly reduce reactive oxygen species and malondialdehyde formation, as well as increase the activity of superoxide dismutase and glutathione peroxidase in HepG2 cells. Therefore, all of the above listed findings indicate that WJSPHs may be a promising antioxidant food to prevent future oxidative-related diseases.

Source link: https://onlinelibrary.wiley.com/doi/10.1111/1750-3841.16157


Physicochemical characterisation of ACE‐inhibitory and antioxidant peptides from Alcalase® whey protein hydrolysates using fractionation strategies

Antioxidant activity and ACE inhibitor activity were obtained by enzymatic hydrolysis of bovine whey using food grade Alcalase®. AHA-related peptides with high molecular weight peptides were responsible for AHA, according to the results, low molecular weight peptides with high amounts of cationic and aromatic amino acid residues were responsible for AHA, whereas those related to AOA would have anionic and all nonpolar aliphatic and aromatic amino acid residues within their sequence.

Source link: https://onlinelibrary.wiley.com/doi/10.1111/1471-0307.12872


Angiotensin‐converting enzyme (ACE) inhibitory peptides from fermented sausages inoculated with Lactobacillus plantarum CD101 and Staphylococcus simulans NJ201

Natural ACE inhibitory peptides derived from food are considered to be a useful treatment for blood pressure lowering. In fermented sausages, this research investigated the effects of Lactobacillus plantarum CD101 and Staphylococcus simulans NJ201 on proteolysis and sequence composition of ACE inhibitory peptides. During the production of fermented sausages, the ACE inhibitory activity of the inoculated group reached its highest values on day 35. In the inoculated group, sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a more promising effect in hydrolysis of the sarcoplasmic and myofibrillar protein. In the inoculated group, the molecular weight increase showed a significant rise in peptides with molecular weight less than 1 kDa. These findings showed that mixed starters were prone to protein degradation and the production of peptides with high ACE inhibitory capacity, especially peptides less than 1 kDa, and could be used as functional material for antihypertensive drugs.

Source link: https://onlinelibrary.wiley.com/doi/10.1111/ijfs.15765

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions