Goat milk Kefir with ACE inhibitory activity: Preparation and storage stability evaluation

2020 ◽  
Vol 44 (5) ◽  
Author(s):  
Guowei Shu ◽  
Lin Ma ◽  
Li Chen ◽  
Meng Guo ◽  
Yuliang Guo ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Storage Stability ◽  
Goat Milk ◽  
Stability Evaluation ◽  
Ace Inhibitory Activity ◽  
And Storage ◽  
Ace Inhibitory

scholarly journals Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 101 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Chunju Bao ◽  
Jiangpeng Meng ◽  
He Chen ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Goat Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

Optimisation of the hydrolysis of goat milk protein for the production of ACE-inhibitory peptides

2013 ◽  
Vol 80 (2) ◽  
pp. 214-222 ◽  
Author(s):  
Francisco Javier Espejo-Carpio ◽  
Raúl Pérez-Gálvez ◽  
Emilia M Guadix ◽  
Antonio Guadix
Keyword(s):  
Inhibitory Activity ◽  
Milk Protein ◽  
Goat Milk ◽  
Degree Of Hydrolysis ◽  
Ace Inhibitory Activity ◽  
Enzyme Substrate ◽  
Substrate Ratio ◽  
Input Variables ◽  
The Individual ◽  
Ace Inhibitory

Goat milk protein was hydrolysed with subtilisin and trypsin. As input variables, temperature was assayed in the interval 45–70 °C for subtilisin and 30–55 °C for trypsin, while the enzyme-substrate ratio varied from 1 to 5%. The effect of the input variables on the degree of hydrolysis and ACE-inhibitory activity (output variables) was modelled by second order polynomials, which were able to fit the experimental data with deviations below 10%. The individual maximum values of the degree of hydrolysis and the ACE-inhibitory activity were found at conflicting conditions of temperature and enzyme-substrate ratio. Since such maximum values could not be reached simultaneously, a bi-objective optimisation procedure was undertaken, producing a set of non-inferior solutions that weighted both objectives.

Effect of Probiotic lactobacillus Strains on Angiotensin I Converting Enzyme Inhibitory Activity from Fermented Goat Milk

2012 ◽  
Vol 531 ◽  
pp. 442-445 ◽  
Author(s):  
He Chen ◽  
Zhe Ji ◽  
Guo Wei Shu ◽  
Hong Ni Xing
Keyword(s):  
Inhibitory Activity ◽  
Lactobacillus Reuteri ◽  
Goat Milk ◽  
Lactobacillus Bulgaricus ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Probiotic Lactobacillus ◽  
Different Strains ◽  
Ace Inhibitory

Goat milk was fermented by different strains of lactic acid bacterias in anaerobic tube, strains with high angiotensin converting enzyme (ACE) inhibitory activity were screened from 28 probiotic Lactobacillus strains by the criteria of ACE inhibitory activity and pH. The results showed that 20 strains had ACE inhibitory activity and among them the activity of 4 strains were extremely high, they were Lactobacillus reuteri, Lactobacillus bulgaricus, Lactobacillus rhamnosu and Lactobacillus helveticu. In vitro experiments, the ACE inhibitory activity of goat milk fermented by these 4 strains reached 95.92%, 84.61%, 82.79% and 78.57%, respectively. After incubation, pH of them were 6.17, 3.88, 5.24 and 3.71, respectively.

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.

scholarly journals Peptide profiling of goat milk fermented by Lactobacillus delbrueckii ssp. delbrueckii BD7: Identification of potential biological activity

2021 ◽  
Vol 22 (8) ◽  
Author(s):  
Yuliana Tandi Rubak ◽  
Lilis Nuraida ◽  
Dyah Iswantini ◽  
Endang Prangdimurti ◽  
Maxs Urias Ebenhaizar Sanam
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Starter Culture ◽  
Goat Milk ◽  
Lactobacillus Delbrueckii ◽  
Amino Acid Residues ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

Abstract. Rubak YT, Nuraida L, Iswantini D, Prangdimurti E, Sanam MUE. 2021. Peptide profiling of goat milk fermented by Lactobacillus delbrueckii ssp. delbrueckii BD7: Identification of potential biological activity. Biodiversitas 22: 3136-3145. This study investigated the angiotensin-converting enzyme (ACE) inhibitory activity in fermented goat milk by Lactobacillus delbrueckii ssp. delbrueckii BD7, characterizing the peptide and its potential as a bioactive peptide. The starter culture (2%) was inoculated into pasteurized goat skim milk (11%), then incubated at 37 °C until it reached pH 4.6. Centrifugation at 6000 g x 10 minutes at 4 °C was applied. The supernatant obtained was then ultrafiltrated using a membrane cut-off with a molecular weight of 3 kDa, and the fraction obtained was analyzed to determine the inhibitory activity of ACE. Peptides were characterized using Nano LC / MS / MS, and identification as bioactive peptides was carried out based on a literature review. ACE inhibitory activity of fermented goat milk of Lb. delbrueckii ssp. delbrueckii BD7 was 55.98 ± 3.53%. A total of 157 peptides were released with molecular weights ranging from 770.78 - 2081.12 Da and having 7-19 amino acid residues. The main peptide was hydrolyzed from casein (72.6%), cleavage in the parent protein, specific for aliphatic and aromatic amino acids. Identification of bioactive peptides based on the similarity of amino acid residues at C-terminal obtained 28 ACE inhibitor peptides, 19 antioxidant peptides, and ten antimicrobial peptides. Some of these peptides have homologous sequences with previously reported peptides. Lb. delbrueckii ssp. delbrueckii BD7 has the potential as a starter culture to produce fermented milk, which is rich in biological activity.

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.

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

2005 ◽  
Vol 10 (3) ◽  
pp. 239-243 ◽  
Author(s):  
Rohan Karawita ◽  
Pyo-Jam park ◽  
Nalin Siriwardhana ◽  
Byong-Tae Jeon ◽  
Sang-Ho Moon ◽  
...  
Keyword(s):  
Cervus Elaphus ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Velvet Antler ◽  
Ace Inhibitory
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