ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)

2008 ◽  
Vol 43 (7) ◽  
pp. 743-747 ◽  
Author(s):  
Jenn-Shou Tsai ◽  
Jia-Ling Chen ◽  
Bonnie Sun Pan
Keyword(s):  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Hard Clam ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Meretrix Lusoria ◽  
Ace Inhibitory

scholarly journals Affinity Purification of Angiotensin Converting Enzyme Inhibitory Peptides from Wakame (Undaria pinnatifida) Using Immobilized ACE on Magnetic Metal Organic Frameworks

Marine Drugs ◽  
2021 ◽  
Vol 19 (3) ◽  
pp. 177
Author(s):  
Xuezhen Feng ◽  
Dankui Liao ◽  
Lixia Sun ◽  
Shanguang Wu ◽  
Ping Lan ◽  
...  
Keyword(s):  
Competitive Inhibition ◽  
Undaria Pinnatifida ◽  
Marine Organism ◽  
Protein Hydrolysate ◽  
Affinity Purification ◽  
Converting Enzyme ◽  
Food Ingredients ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from marine organism have shown a blood pressure lowering effect with no side effects. A new affinity medium of Fe3O4@ZIF-90 immobilized ACE (Fe3O4@ZIF-90-ACE) was prepared and used in the purification of ACE inhibitory peptides from Wakame (Undaria pinnatifida) protein hydrolysate (<5 kDa). The Fe3O4@ZIF-90 nanoparticles were prepared by a one-pot synthesis and crude ACE extract from pig lung was immobilized onto it, which exhibited excellent stability and reusability. A novel ACE inhibitory peptide, KNFL (inhibitory concentration 50, IC50 = 225.87 μM) was identified by affinity purification using Fe3O4@ZIF-90-ACE combined with reverse phase-high performance liquid chromatography (RP-HPLC) and MALDI-TOF mass spectrometry. Lineweaver–Burk analysis confirmed the non-competitive inhibition pattern of KNFL, and molecular docking showed that it bound at a non-active site of ACE via hydrogen bonds. This demonstrates that affinity purification using Fe3O4@ZIF-90-ACE is a highly efficient method for separating ACE inhibitory peptides from complex protein mixtures and the purified peptide KNFL could be developed as a functional food ingredients against hypertension.

scholarly journals Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 179 ◽  
Author(s):  
Siqi Sun ◽  
Xiaoting Xu ◽  
Xue Sun ◽  
Xiaoqian Zhang ◽  
Xinping Chen ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
High Performance ◽  
Protein Hydrolysate ◽  
Molecular Docking Study ◽  
Protein Ratio ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ulva Intestinalis ◽  
Marine Macroalga ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC50 values of 219.35 μM (0.183 mg/mL) and 236.85 μM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides.

Production of goat milk protein hydrolysate enriched in ACE-inhibitory peptides by ultrafiltration

2014 ◽  
Vol 81 (4) ◽  
pp. 385-393 ◽  
Author(s):  
Francisco Javier Espejo-Carpio ◽  
Raúl Pérez-Gálvez ◽  
María del Carmen Almécija ◽  
Antonio Guadix ◽  
Emilia M. Guadix
Keyword(s):  
Inhibitory Activity ◽  
Ceramic Membrane ◽  
Protein Hydrolysate ◽  
Liquid Product ◽  
Goat Milk ◽  
Reduction Factor ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

A global process for the production of goat milk hydrolysates enriched in angiotensin converting enzyme (ACE) inhibitory peptides was proposed. Firstly, the protein fractions (caseins and whey proteins) were separated by ultrafiltration through a 0·14 μm ceramic membrane. The casein fraction obtained in the retentate stream of the above filtration step was subsequently hydrolysed with a combination of subtilisin and trypsin. After 3 h of reaction, the hydrolysate produced presented an IC50 of 218·50 μg/ml, which represent a relatively high ACE inhibitory activity. Finally, this hydrolysate was filtered through a 50 kDa ceramic membrane until reaching a volume reduction factor of 3. The permeate produced presented an improvement of more than 30% in the ACE inhibitory activity. In contrast, the retentate was concentrated in larger and inactive peptides which led to a decrease of more than 80% in its inhibitory activity. The process suggested in this work was suitable to obtain a potent ACE inhibitory activity product able to be incorporated into food formulas intended to control or lower blood pressure. Moreover, the liquid product could be easily stabilised by spray dried if it would be necessary.

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