Purification and identification of Angiotensin-I Converting Enzyme (ACE) inhibitory peptide from lizard fish (Saurida elongata) hydrolysate

Wu, Shanguang; Feng, Xuezhen; Lan, Xin; Xu, Yuanjin; Liao, Dankui

doi:10.1016/j.jff.2014.12.051

Cited by 52 publications

(23 citation statements)

References 15 publications

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“…In the current study, RYRP is composed of four amino acid residues with hydrophobic residue, proline as the C -terminal residue, exhibiting strong ACE-inhibitory activity (IC 50 of 52 μM). Its ACE inhibitory activity was stronger than RVCLP [23], but weaker than SPRCR [22]. This phenomenon is in accordance with the QSAR studies.…”

Section: Resultssupporting

confidence: 80%

Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni2+

Sun

Zhou

et al. 2017

Marine Drugs

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Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (Saurida elongata) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC-Ni2+). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC50 of 0.116 mg·mL−1) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC50 value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate.

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Section: Resultssupporting

confidence: 80%

Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni2+

Sun

Zhou

et al. 2017

Marine Drugs

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“…Bioactive peptides derived from food protein are increasingly becoming important as starting points for the development of functional ingredients and drugrelated compounds. Among various bioactive peptides, ACE inhibitory peptides have been studied extensively and a large number of ACE inhibitory peptides have been purified and identified from various food sources such as cereals (De Leo, Panarese, Gallerani, & Ceci, 2009;Shamloo, Eck, & Beta, 2015), egg (Majumder et al, 2015), milk (Zhou et al, 2012), casein (Holder et al, 2013;Yamada et al, 2013), porcine muscle (Castellano, Aristoy, Sentandreu, & Vignolo, 2013) and marine source such as oyster and lizard fish (Wu, Feng, Lan, Xu, & Liao, 2015;Xie, Kim, Ha, Choung, & Choi, 2014).…”

Section: Introductionmentioning

confidence: 99%

In silico investigation of action mechanism of four novel angiotensin-I converting enzyme inhibitory peptides modified with Trp

Xie

Choung

Cao

et al. 2015

Journal of Functional Foods

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“…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%

“…It has been reported that ACE inhibitory peptides contain hydrophobic amino acids residues and also that the three amino acid sequence of C-terminal in these peptides can affect the ability of peptides to combine with ACE. If these sequences contain hydrophobic amino acids, it is highly likely that they had high ACE inhibitory activity [16,26]. Table 3 shows that the hydrophobic and aromatic amino acids in peak I account for 51.21% and 9.59% of the total amino acid, respectively.…”

Section: Amino Acid Composition Analysis Of Coasm Peptidementioning

confidence: 99%

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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Purification and identification of Angiotensin-I Converting Enzyme (ACE) inhibitory peptide from lizard fish (Saurida elongata) hydrolysate

Cited by 52 publications

References 15 publications

Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni2+

Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni2+

In silico investigation of action mechanism of four novel angiotensin-I converting enzyme inhibitory peptides modified with Trp

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

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