Process of Zanthoxylum armatum DC. oil by a novel low-temperature continuous phase transition extraction: Evaluation of aroma, pungent compounds and quality

Liu, Fei; Kan, Qixin; Feng, Konglong; Chen, Yuli; Wen, Linfeng; He, Baowen; Zhu, Xiaoyan; Wen, Chenggang; Cao, Yong

doi:10.1016/j.lwt.2023.114523

Cited by 5 publications

(1 citation statement)

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“…In the present study, PSM containing 80.87% protein with oils and polysaccharides removed by continuous phase-transition extraction (CPE), a patented technology that was independently developed by our group for green extraction of food actives , in a relatively low temperature, low pressure, and anaerobic environment was used to prepare antihypertensive peptides through enzymatic hydrolysis followed by purification with ultrafiltration, Sephadex G-15 column chromatography, and reversed-phase high-performance liquid chromatography (RP-HPLC). Two novel hypotensive peptides were sequentially identified, and molecular docking was utilized to study the binding mechanism of the two identified hypotensive peptides with ACE.…”

Section: Introductionmentioning

confidence: 99%

Two Novel Angiotensin-Converting Enzyme (ACE) Inhibitory and ACE2 Upregulating Peptides from the Hydrolysate of Pumpkin (Cucurbita moschata) Seed Meal

Li,

Peng,

Xiao

et al. 2024

J. Agric. Food Chem.

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Pumpkin (Cucurbita moschata) seed meal (PSM), the major byproduct of pumpkin seed oil industry, was used to prepare angiotensin-converting enzyme (ACE) inhibitory and angiotensin-converting enzyme 2 (ACE2) upregulating peptides. These peptides were isolated and purified from the PSM hydrolysate prepared using Neutrase 5.0 BG by ultrafiltration, Sephadex G-15 column chromatography, and reversed-phase high-performance liquid chromatography. Two peptides with significant ACE inhibition activity were identified as SNHANQLDFHP and PVQVLASAYR with IC 50 values of 172.07 and 90.69 μM, respectively. The C-terminal tripeptides of the two peptides contained Pro, Phe, and Tyr, respectively, and PVQVLASAYR also had Val in its Nterminal tripeptide, which was a favorable structure for ACE inhibition. Molecular docking results declared that the two peptides could interact with ACE through hydrogen bonds and hydrophobic interactions. Furthermore, the two peptides performed protective function on EA.hy926 cells by decreasing the secretion of endothelin-1, increasing the release of nitric oxide, and regulating the ACE2 activity. In vitro simulated gastrointestinal digestion showed the two peptides exhibited good stability against gastrointestinal enzyme digestion. In conclusion, PSM is a promising material for preparing antihypertensive peptides.

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Section: Introductionmentioning

confidence: 99%