scholarly journals Optimization of Goat Milk with ACE Inhibitory Peptides Fermented by Lactobacillus bulgaricus LB6 Using Response Surface Methodology

Molecules ◽  
2017 ◽  
Vol 22 (11) ◽  
pp. 2001 ◽  
Author(s):  
Guowei Shu ◽  
Xiaoyu Shi ◽  
He Chen ◽  
Zhe Ji ◽  
Jiangpeng Meng
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Goat Milk ◽  
Lactobacillus Bulgaricus ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

scholarly journals Proteomic Analysis of ACE Inhibitory Peptides extracted from Fermented Goat Milk

2018 ◽  
Author(s):  
Muhammad Zohaib Aslam ◽  
Sana Shoukat ◽  
Zhao Hongfei ◽  
Zhang Bolin
Keyword(s):  
Incubation Time ◽  
Goat Milk ◽  
Aromatic Amino Acids ◽  
Lactobacillus Helveticus ◽  
Size Exclusion ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Pm 10 ◽  
Ace Inhibitory

AbstractProtein extracted from goat milk was hydrolyzed with LH (Lactobacillus Helveticus-cicc22171). Angiotensin Converting Enzyme (ACE) inhibitory peptides were purified from fermented samples of goat milk protein with LH by optimizing incubation time to 8 hours (S-8), 16 hours (S-16), 24 hours (S-24) and 36 hours (S-36), via ultrafiltration. Molecular weight cut-off; 10000 Da (PM-10) membrane was used to perform size exclusion chromatography. Sample with 24 h incubation time was considered as best hydrolyzed as compared to others, by applying Nin-Hydrin reaction and SDS-PAGE analysis. ACE inhibitory assay validated the authenticity of S-24 in inhibiting ACE, in vitro. Furthermore, Q executive Hybrid Quadrapole-Orbitrap Mass Spectrometry was used to determine molecular structure and amino acid sequence of ACE inhibitory peptides. Two protein groups VLPVPQKAVPQ and VLPVPQKVVPQ containing PVP, VVP along with one most abundant peptide TQTPVVVPPFLQPEIMGVPKVKE containing VPP has been identified with highest ACE inhibitory activity on the basis of intensity, small structure and higher concentration of hydrophobic and aromatic amino acids. Fermented goat milk containing these novel bioactive peptides, can be used as nutraceuticals to inhibit ACE and control hypertension.

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.

Peptidomic Analysis of ACE Inhibitory Peptides Extracted from Fermented Goat Milk

2018 ◽  
Vol 25 (4) ◽  
pp. 1259-1270 ◽  
Author(s):  
Muhammad Zohaib Aslam ◽  
Sana Shoukat ◽  
Zhao Hongfei ◽  
Zhang Bolin
Keyword(s):  
Goat Milk ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Peptidomic Analysis ◽  
Ace Inhibitory

scholarly journals Production of Angiotensin-I-Converting Enzyme inhibitory peptide from goat milk casein: optimization conditions of complex protease hydrolysate by response surface methodology and purification

2018 ◽  
pp. 742
Author(s):  
Li Chen ◽  
Juan Wang, Guowei Shu, He Chen
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Inhibitory Activity ◽  
Goat Milk ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Milk Casein ◽  
Ace Inhibitory

Food-derived Angiotensin-I-Converting Enzyme (ACE)-inhibitory peptides have safety advantages over synthetic peptides. The application of complex enzymatic (alcalase and trypsin) in producing such peptides from goat milk casein seldom be focused. In this study, the pH, complex protease ratio (CPR) and enzyme to substrate ratio (E/S) were optimized by Response surface methodology (RSM). The optimized conditions were: pH 8.4, CPR 1:1, and E/S 8.5%. In these conditions, the ACE-inhibitory activity of the obtained hydrolysates reached 91.99%. The response model was qualified to predict the reaction optimization. Hydrolysate fragments were purified consecutively. A fraction G2-2a exhibited highest ACE-inhibitory activity 93.50% with IC50 value of 72.14 μg/mL.

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.

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