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

2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Guang-long Yao ◽  
Wei He ◽  
You-gen Wu ◽  
Jian Chen ◽  
Xin-wen Hu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Alkaline Protease ◽  
Seed Meal ◽  
Gel Chromatography ◽  
Camellia Oleifera ◽  
Kinetics Parameters ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

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%.

Predicting the Activity of ACE Inhibitory Peptides with a Novel Mode of Pseudo Amino Acid Composition

2011 ◽  
Vol 18 (12) ◽  
pp. 1233-1243 ◽  
Author(s):  
Mao Shu ◽  
Xiaoming Cheng ◽  
Yunru Zhang ◽  
Yuanqiang Wang ◽  
Yong Lin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Pseudo Amino Acid Composition ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

scholarly journals Novel Angiotensin-Converting Enzyme Inhibitory Peptides Identified from Walnut Glutelin-1 Hydrolysates: Molecular Interaction, Stability, and Antihypertensive Effects

Nutrients ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 151
Author(s):  
Jing Wang ◽  
Guoliang Wang ◽  
Yufeng Zhang ◽  
Runguang Zhang ◽  
Youlin Zhang
Keyword(s):  
Angiotensin Converting Enzyme ◽  
High Performance ◽  
Gel Chromatography ◽  
Converting Enzyme ◽  
Pressure Balance ◽  
Molecular Docking Study ◽  
Inhibitory Peptide ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

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.

scholarly journals Ultrasound-Assisted Multi-Enzymatic System for the Preparation of ACE Inhibitory Peptides with Low Bitterness from Corn Gluten Meal

Processes ◽  
2021 ◽  
Vol 9 (12) ◽  
pp. 2170
Author(s):  
Shanfen Huang ◽  
Yunliang Li ◽  
Chengliang Li ◽  
Siyu Ruan ◽  
Wenjuan Qu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Inhibitory Activity ◽  
Enzymatic System ◽  
Corn Gluten Meal ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Corn Gluten ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory ◽  
Ultrasound Pretreatment

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.

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

Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human αs1-casein expressed in Escherichia coli

1999 ◽  
Vol 66 (3) ◽  
pp. 431-439 ◽  
Author(s):  
YOO-KYEONG KIM ◽  
SUN YOON ◽  
DAE-YEUL YU ◽  
BO LÖNNERDAL ◽  
BONG-HYUN CHUNG
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Sequences ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Treatment Of Hypertension ◽  
Ace Inhibitory

Recombinant human αs1-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II, B-II and C, were isolated and their amino acid sequences identified as Tyr–Pro–Glu–Arg (residues 8–11), Tyr–Tyr–Pro–Gln–Ile–Met–Gln–Tyr (residues 136–143) and Asn–Asn–Val–Met–Leu–Gln–Trp (residues 164–170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132·5, 24·8 and 41·0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.

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