ACE Inhibitory Peptides Derived from Enzymatic Hydrolysates of Animal Muscle Protein:  A Review

2005 ◽  
Vol 53 (21) ◽  
pp. 8106-8115 ◽  
Author(s):  
Lieselot Vercruysse ◽  
John Van Camp ◽  
Guy Smagghe
Keyword(s):  
Muscle Protein ◽  
Protein A ◽  
Enzymatic Hydrolysates ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Animal Muscle ◽  
Ace Inhibitory

scholarly journals ACE Inhibitory Peptides from Bellamya bengalensis Protein Hydrolysates: In Vitro and In Silico Molecular Assessment

Processes ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 1316
Author(s):  
Tanmoy Kumar Dey ◽  
Roshni Chatterjee ◽  
Rahul Shubhra Mandal ◽  
Anadi Roychoudhury ◽  
Debjyoti Paul ◽  
...  
Keyword(s):  
In Silico ◽  
Solid Phase ◽  
Muscle Protein ◽  
Peptide Sequence ◽  
Inhibitory Peptides ◽  
Ic50 Value ◽  
Ace Inhibitory Peptides ◽  
Bellamya Bengalensis ◽  
Ace Inhibitory

Bellamya bengalensis muscle meat is known for ethnopharmacological benefits. The present study focuses on the identification of ACE inhibitory peptides from the proteolytic digests of muscle protein of Bellamya bengalensis and its underlying mechanism. After ultrafiltration of 120 min alcalase hydrolysates (BBPHA120) to isolate the small peptide fraction (<3 kDa), in vitro ACE inhibitory activity was analyzed. The IC50 value of the 120 min hydrolysate ultrafiltered fraction was 86.74 ± 0.575 µg/mL, while the IC50 of lisinopril was 0.31 ± 0.07 µg/mL. This fraction was assessed in a MALDI-ToF mass spectrometer and five peptides were identified from the mass spectrum based on their intensity (>1 × 104 A.U.). These peptides were sequenced via de novo sequencing. Based on the apparent hydrophobicity (%), the IIAPTPVPAAH peptide was selected for further analysis. The sequence was commercially synthesized by solid-phase standard Fmoc chemistry (purity 95–99.9%; by HPLC). The synthetic peptide (IC50 value 8.52 ± 0.779 µg/mL) was used to understand the thermodynamics of the inhibition by checking the binding affinity of the peptide to ACE by isothermal titration calorimetry compared with lisinopril, and the results were further substantiated by in silico site-specific molecular docking analysis. The results demonstrate that this peptide sequence (IIAPTPVPAAH) can be used as a nutraceutical with potent ACE inhibition.

scholarly journals Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Wen-Ying Liu ◽  
Jiang-Tao Zhang ◽  
Takuya Miyakawa ◽  
Guo-Ming Li ◽  
Rui-Zeng Gu ◽  
...  
Keyword(s):  
Wheat Gluten ◽  
Antioxidant Properties ◽  
Converting Enzyme ◽  
Antioxidant Peptides ◽  
Active Peptides ◽  
Inhibitory Peptides ◽  
Highly Active ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

AbstractThis study aimed to focus on the high-value utilization of raw wheat gluten by determining the potent antioxidant peptides and angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten oligopeptides (WOP). WOP were analyzed for in vitro antioxidant activity and inhibition of ACE, and the identification of active peptides was performed by reversed-phase high-performance liquid chromatography and mass spectrometry. Quantitative analysis was performed for highly active peptides. Five potent antioxidant peptides, Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (6.07 ± 0.38, 7.28 ± 0.29, 11.18 ± 1.02, 5.93 ± 0.20 and 9.04 ± 0.47 mmol 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox) equivalent/g sample, respectively), and five potent ACE inhibitory peptides, Leu-Tyr, Leu-Val-Ser, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (half maximal inhibitory concentration (IC50) values = 0.31 ± 0.02, 0.60 ± 0.03, 2.00 ± 0.13, 1.47 ± 0.08 and 1.48 ± 0.11 mmol/L, respectively), were observed. The contents of Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser were 155.04 ± 8.36, 2.08 ± 0.12, 1.95 ± 0.06, 22.70 ± 1.35, 0.25 ± 0.01, and 53.01 ± 2.73 μg/g, respectively, in the WOP. Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser are novel antioxidative/ACE inhibitory peptides that have not been previously reported. The results suggest that WOP could potentially be applied in the food industry as a functional additive.

Production of novel ACE inhibitory peptides from β-lactoglobulin using Protease N Amano

2009 ◽  
Vol 19 (2) ◽  
pp. 69-76 ◽  
Author(s):  
Paola Ortiz-Chao ◽  
José A. Gómez-Ruiz ◽  
Robert A. Rastall ◽  
Davinia Mills ◽  
Rainer Cramer ◽  
...  
Keyword(s):  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Β Lactoglobulin ◽  
Ace Inhibitory
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