ace inhibitory peptides
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Nutrients ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 151
Author(s):  
Jing Wang ◽  
Guoliang Wang ◽  
Yufeng Zhang ◽  
Runguang Zhang ◽  
Youlin Zhang

In recent years, angiotensin-converting enzyme (ACE) inhibitory peptide has become a research hotspot because of its essential role in maintaining human blood pressure balance. In this study, two novel ACE inhibitory peptides of Val-Glu-Arg-Gly-Arg-Arg-lle-Thr-Ser-Val (Valine-Glutamate-Arginine-Glycine-Arginine-Arginine-Isoleucine-Threonine-Serine-Valine, VERGRRITSV) and Phe-Val-Ile-Glu-Pro-Asn-Ile-Thr-Pro-Ala (Phenylalanine-Valine-Isoleucine-Glutamate-Proline-Asparagine-Isoleucine-Threonine-Proline-Alanine, FVIEPNITPA) were isolated and purified from defatted walnut meal hydrolysates through a series of preparation processes including ultrafiltration, Sephadex G-15 gel chromatography, and reverse high performance liquid chromatography (RP-HPLC). Both peptides showed high ACE inhibitory activities. The molecular docking study revealed that VERGRRITSV and FVIEPNITPA were primarily attributed to the formation of strong hydrogen bonds with the active pockets of ACE. The binding free energies of VERGRRITSV and FVIEPNITPA with ACE were −14.99 and −14.69 kcal/mol, respectively. Moreover, these ACE inhibitory peptides showed good stability against gastrointestinal enzymes digestion and common food processing conditions (e.g., temperature and pH, sugar, and salt treatments). Furthermore, animal experiment results indicated that the administration of VERGRRITSV or FVIEPNITPA exhibited antihypertensive effects in spontaneously hypertensive rats. Our results demonstrated that walnut could be a potential source of bioactive peptides with ACE inhibitory activity.


Processes ◽  
2021 ◽  
Vol 9 (12) ◽  
pp. 2170
Author(s):  
Shanfen Huang ◽  
Yunliang Li ◽  
Chengliang Li ◽  
Siyu Ruan ◽  
Wenjuan Qu ◽  
...  

The promising angiotensin converting enzyme (ACE) inhibitory peptides derived from corn protein usually have strong bitterness and thus limit their use among consumers. To prepare ACE inhibitory peptides with low bitterness, two energy-efficient types of ultrasound pretreatment were introduced into the multi-enzymatic system of corn gluten meal. The results showed that Flavourzyme–Protamex sequential enzymolysis produced the peptides with high ACE inhibitory activity and the lowest bitterness compared with other enzymolysis conditions. During the optimized sequential enzymolysis, the divergent ultrasound pretreatment with a frequency of 40 kHz for 60 min exhibited higher ACE inhibitory activity (65.36%, accounting for 73.84% of the highest ACE inhibitory activity) and lower bitterness intensity of peptides, compared with an energy-gathered ultrasound. The results of the study showed that, on the one hand, divergent ultrasound pretreatment induced the highest intrinsic fluorescence of protein, with more hydrophobic amino acid residues exposed for cleavage by exopeptidases, which leads to a reduction in bitterness. On the other hand, the amino acid composition analysis proved that more Tyr, Ile, and Val moieties, instead of Leu (bitterest substance), and more peptide fractions with a molecular weight >1000 Da should be the structural features of high ACE inhibitory peptides.


Foods ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 2949
Author(s):  
Shounan Wang ◽  
Peng Zhang ◽  
Yibin Xue ◽  
Qiaojuan Yan ◽  
Xue Li ◽  
...  

Rhizomucor miehei is an important fungus that produces aspartic proteases suitable for cheese processing. In this study, a novel aspartic protease gene (RmproB) was cloned from R. miehei CAU432 and expressed in Aspergillus niger. The amino acid sequence of RmproB shared the highest identity of 58.2% with the saccharopepsin PEP4 from Saccharomyces cerevisiae. High protease activity of 1242.2 U/mL was obtained through high density fermentation in 5 L fermentor. RmproB showed the optimal activity at pH 2.5 and 40 °C, respectively. It was stable within pH 1.5–6.5 and up to 45 °C. RmproB exhibited broad substrate specificity and had Km values of 3.16, 5.88, 5.43, and 1.56 mg/mL for casein, hemoglobin, myoglobin, and bovine serum albumin, respectively. RmproB also showed remarkable milk-clotting activity of 3894.1 SU/mg and identified the cleavage of Lys21-Ile22, Leu32-Ser33, Lys63-Pro64, Leu79-Ser80, Phe105-Met106, and Asp148-Ser149 bonds in κ-casein. Moreover, duck hemoglobin was hydrolyzed by RmproB to prepare angiotensin-I-converting enzyme (ACE) inhibitory peptides with high ACE-inhibitory activity (IC50 of 0.195 mg/mL). The duck hemoglobin peptides were further produced at kilo-scale with a yield of 62.5%. High-level expression and favorable biochemical characterization of RmproB make it a promising candidate for cheese processing and production of ACE-inhibitory peptides.


Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2099
Author(s):  
Lucía Abadía-García ◽  
Eduardo Castaño-Tostado ◽  
Anaberta Cardador-Martínez ◽  
Sandra Teresita Martín-del-Campo ◽  
Silvia L. Amaya-Llano

High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at two levels of amplitude (30 and 50%) for 10 min, followed by hydrolysis using the vegetable protease bromelain. The hydrolysates obtained were ultrafiltrated and their fractions were submitted to a simulated gastrointestinal digestion. The conformational changes induced by HIUS on whey proteins were analyzed using Fourier-transform infrared spectroscopy by attenuated total reflectance (FTIR-ATR) and intrinsic spectroscopy. It was found that both levels of ultrasound pretreatment significantly decreased the IC50 value (50% Inhibitory Concentration) of the hydrolysates in comparison with the control (α = 0.05). After this treatment, HIUS-treated fractions were shown as smaller in size and fractions between 1 and 3 kDa displayed the highest ACE inhibition activity. HIUS promoted significant changes in whey protein structure, inducing, unfolding, and aggregation, decreasing the content of α-helix, and increasing β-sheets structures. These findings prove that ultrasound treatment before enzymatic hydrolysis is an innovative and useful strategy that modifies the peptide profile of whey protein hydrolysates and enhances the production of ACE inhibitory peptides.


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