Separation and identification of ACE inhibitory peptides from cashew nut (<i>Anacardium occidentale</i> Linnaeus) protein

Yao, Guanglong; Chai, Yu Shuang; Chen, Jian; Wu, Yougen

doi:10.1080/10942912.2017.1325902

Cited by 8 publications

(9 citation statements)

References 19 publications

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“…ey found that the IC 50 value is the minimum for the peptide in 1 kDa membrane ultrafiltration [20]. Our laboratory also demonstrates that the cashew nut peptides exhibiting ACE inhibitory activity had molecular weight lower than 3000 Da [22]. e above results also verified the conclusion that ACE inhibitory peptides are mainly composed of peptides below 1 kDa.…”

Section: Analysis Of Ace Inhibitorysupporting

confidence: 78%

“…Ultrafiltration of ACE Inhibitory Peptides. e COASM protein hydrolytic liquid was filtered using three (10, 5, and 1 kDa) ultrafiltration membranes and separated by a Vivaflow ultrafiltration system [22,26]. e fractions were collected and freeze-dried, and their IC 50 values were measured.…”

Section: Separation and Identification Of Ace Inhibitory Peptidesmentioning

confidence: 99%

“…Type and content of amino acids in ACE inhibitory peptides from COASM was determined by the method established in our laboratory [22]. 1 mL of the filtrate was taken into a 5 mL volumetric flask and dried in a vacuum drier.…”

Section: Amino Acid Analysis Of Ace Inhibitory Peptidesmentioning

confidence: 99%

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Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

Yao

et al. 2019

Journal of Food Quality

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China is a large country that produces Camellia oleifera Abel seed meal (COASM), a by-product of tea-seed oil, which is only used as an organic fertilizer, resulting in a serious waste of high-quality resources. The preparation of the ACE inhibitory peptide from COASM and the study of its functional properties are of practical importance in improving the comprehensive utilization of COASM. Our manuscript presents an optimized preparation of ACE inhibitory peptides with alkaline protease and enzyme kinetics parameters. Ultrafiltration, gel chromatography, and RP-HPLC purification were conducted for ACE inhibitory peptides, and peptide molecular weight distribution and amino acid composition were analyzed in the enzymolysis liquid. The following were the conditions of the optimized enzymatic hydrolysis to obtain ACE inhibitory peptides from COASM: 15 times of hydrolysis in distilled water for 3.5 h at 50°C, pH = 8.5, substrate concentration of 17 mg/g, and addition of 6% (w/w) alkaline protease. Under this condition, the peptides produced exhibited an ACE inhibition rate of 79.24%, and the reaction kinetics parameters are as follows: Km = 0.152 mg/mL and Vmax = 0.130 mg/mL·min. The majority of ACE inhibitory peptides from COASM have molecular weight below 1 kDa, and a high ACE inhibitory rate was achieved after dextran gel chromatography separation and purification (whose IC50 was 0.678 mg/mL). The hydrophobic amino acid content in this fraction reached 51.21%.

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Section: Analysis Of Ace Inhibitorysupporting

confidence: 78%

Section: Separation and Identification Of Ace Inhibitory Peptidesmentioning

confidence: 99%

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Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

Yao

et al. 2019

Journal of Food Quality

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“…), or the different analytical method used for the determination of the ACE‐inhibitory activity. Literature data on ACE‐inhibitory activity of nuts hydrolysates are numerous and our experimental data are in good agreement with the majority of them …”

Section: Resultsmentioning

confidence: 99%

Preparation and antagonistic effect of ACE inhibitory peptide from cashew

2019

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BACKGROUND Angiotensin‐converting enzyme (ACE) inhibitory peptides were found to alleviate acute hepatitis significantly. In this study, we purified and identified ACE inhibitory peptide from cashew to evaluate its protective role on alcohol‐induced acute hepatitis in mice. RESULTS The ACE inhibitory peptides were purified by using consecutive chromatographic techniques. One of these peptides (FETISFK) exhibited the highest ACE inhibition rate (91.04 ± 0.31%). In vivo, the results showed that ACE inhibitory peptide decreased levels of alanine aminotransferase (ALT) and aspartate aminotransferase (AST) caused by alcohol exposure. Moreover, it could increase the activities of superoxide dismutase (SOD) and glutathione (GSH), and decrease the level of malondialdehyde (MDA). It was also found to down‐regulate markedly the expression of interleukin‐6 (IL‐6) and tumor necrosis factor‐α (TNF‐α). It could also decrease the expression of ACE, angiotensin II (AngII) and angiotensin II type 1 receptor (AT1R). CONCLUSION These findings support the view that the ACE inhibitory peptide alleviated acute hepatitis by down‐regulating the ACE–AngII–AT1R axis, broadening the research approach to prevent acute hepatitis, and providing experimental data for the development and utilization of cashews. © 2019 Society of Chemical Industry

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“…The results showed that the optimal enzymatic hydrolysis conditions were 70 g/L substrate concentration and 1% enzyme. The M2 component with the highest ACE inhibitory peptide activity was identified at pH of 6.5, time of 7 h, and temperature of 55 • C. The amino acid sequence was Gly-Arg-Phe [2]. Extracted CMAPs were used in the cell experiments for analyzing the role of Camellia vietnamensis active peptides (CMAPs) in liver cells with alcoholic liver injury through metabolomics.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Active Peptides from Camellia vietnamensis and Their Metabolic Effects in Alcohol-Induced Liver Injury Cells

Chen

Yan

et al. 2022

Molecules

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Liver damage seriously affects human health. Over 35% of cases of acute liver damage are caused by alcohol damage. Thus, finding drugs that can inhibit and effectively treat this disease is necessary. This article mainly focuses on the effect of the metabolome physical activity of active peptides in Camellia vietnamensis active peptide (CMAP) and improving liver protection. DEAE Sepharose FF ion-exchange column chromatography was used in separating and purifying crude peptides from Camellia vietnamensis Two components, A1 and A2, were obtained, and the most active A1 was selected. Sephadex G-100 gel column chromatography was used in A1 separation and purification. Three components, Al-1, Al-2, and Al-3, were obtained. Through antioxidant activity in vitro as an index of inspection, the relatively active component A1-2 was removed. Reverse-phase high-performance liquid chromatography showed that the purity of component A1-2 was 93.45%. The extracted CMAPs acted on alcoholic liver injury cells. Metabolomics studies revealed that the up-regulated metabolites were ribothymidine and xanthine; the down-regulated metabolites were hydroxyphenyllactic acid, creatinine, stearoylcarnitine, and inosine. This study provides an effective theoretical support for subsequent research.

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Separation and identification of ACE inhibitory peptides from cashew nut (Anacardium occidentale Linnaeus) protein

Cited by 8 publications

References 19 publications

Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

Preparation and antagonistic effect of ACE inhibitory peptide from cashew

Preparation of Active Peptides from Camellia vietnamensis and Their Metabolic Effects in Alcohol-Induced Liver Injury Cells

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