scholarly journals Cheese Whey Fermentation by Its Native Microbiota: Proteolysis and Bioactive Peptides Release with ACE-Inhibitory Activity

Fermentation ◽  
2020 ◽  
Vol 6 (1) ◽  
pp. 19 ◽  
Author(s):  
Miguel A. Mazorra-Manzano ◽  
Glen R. Robles-Porchas ◽  
Daniel A. González-Velázquez ◽  
María J. Torres-Llanez ◽  
Marcel Martínez-Porchas ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Cheese Whey ◽  
Lactic Acid Production ◽  
Whey Proteins ◽  
Biological Properties ◽  
Effect Of Temperature ◽  
Ace Inhibitory Activity ◽  
Beneficial Effects ◽  
Ace Inhibitory

Cheese whey contains about 20% of the total milk protein and has high nutritional and technological value, as well as attractive biological properties. Whey protein represents an important source of bioactive peptides with beneficial effects on health (e.g., antioxidant, antidiabetic, antihypertensive, etc.). Microbiota in cheese whey can hydrolyze proteins and generate bioactive peptides through a fermentation process. The objective of this study was to evaluate the effect of temperature on the fermentation of cheese whey by its native microbiota, and the action of microbial proteolytic activity on whey proteins to release peptides with inhibitory activity of the angiotensin-converting enzyme (ACE). Whey proteins hydrolysis occurred at all incubation temperatures evaluated (32–50 °C), with the major proteolytic effect within the range of 35–42 °C. Minor whey proteins (i.e., Lf, bovine serum albumin (BSA), and IgG) were more susceptible to degradation, while β-lactoglobulin and α-lactalbumin showed major resistance to microbial proteolytic action. Alfa-amino groups increased from 36 to 360–456 µg Gly/mL after 120 h of fermentation. A higher lactic acid production (11.32–13.55 g/L) and lower pH (3.3–3.5) were also observed in the same temperature range (32–42 °C). In addition, ACE-inhibitory activity increased from 22% (unfermented whey) to 60–70% after 120 h of fermentation. These results suggest that the fermentation of cheese whey by its native microbiota represents an attractive process to give value to whey for the production of whey-based beverages or functional foods with potential antihypertensive properties.

scholarly journals Isolasi Penghambat Aktivitas Enzim Pengubah Angiotensin Dari Protein Susu

2016 ◽  
Vol 7 (2) ◽  
pp. 33-38
Author(s):  
Amhar Abubakar
Keyword(s):  
Whey Protein ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Cheese Whey ◽  
The Other ◽  
Ace Inhibitory Activity ◽  
Whey Powder ◽  
Other Hand ◽  
To Come ◽  
Ace Inhibitory

ABSTRACT. Three kinds of samles (whey protein containing casenoglycopeptide, whey protein removed casenoglycopeptide and cheese whey powder digested with 7 kinds of proteases at 37 0C for 24 hr (trypsin, protenase-K, actinase-E, thermolysin, and papain) or 25 0C (pepsin and chymotrypsin). Strong inhibotory activity against the angiotensin converting enzyime (ACE, EC 3.4.15.1) was generated in all samples by 5 proteases digestion (pepsin, chymotrypsin, protinase-K, thermolysin and papain). In whey protein removed caseinoglycopeptide digestion by thermolysin induced the highest activity (95,25%). In cheese whey powder, the highest activity was derived by thermolysin (98.25%). On the other hand, week ACE inhibitory activity were derived by trypsin and actinase-E digestion. As no remarkable differences in inhibitory activity were observed between whey protein containing casenoglycopeptide and whey protein removed casenoglycopeptide samples, the bioactive peptides are considered to come mainly not from casenoglycopeptide but from cheese whey powder components.

scholarly journals Partial Purification and Characterization of Bioactive Peptides from Cooked New Zealand Green-Lipped Mussel (Perna canaliculus) Protein Hydrolyzates

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 879
Author(s):  
Ramya Jayaprakash ◽  
Conrad O. Perera
Keyword(s):  
New Zealand ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Partial Purification ◽  
Ace Inhibitory Activity ◽  
Perna Canaliculus ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, named GPH, exhibited the highest antioxidant and ACE inhibitory activity, but no antimicrobial activity. Purification of the GPH using gel-filtration chromatography revealed that the protein fraction (GPH-IV*) containing peptides with a molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities. Further purification was done using reverse-phase HPLC (RP-HPLC) and the only major peak obtained (GPH-IV*-P2) had the highest antioxidant and ACE inhibitory activity. From this fraction, several bioactive peptides with an MW ≈ 5 kDa were identified using LC-MS and in silico analyses. This research highlights that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with potential therapeutic applications.

Insects as source of angiotensin converting enzyme inhibitory peptides

2017 ◽  
Vol 3 (4) ◽  
pp. 231-240 ◽  
Author(s):  
A. Cito ◽  
M. Botta ◽  
V. Francardi ◽  
E. Dreassi
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Hypertension Treatment ◽  
Converting Enzyme ◽  
Oecophylla Smaragdina ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Hypertension is well known as one of the major risk for cardiovascular diseases which annually affect millions of people. The angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation process. Indeed, hypertension treatment by synthetic ACE inhibitors (e.g. captopril, lisinopril and ramipril) is effective; however, their use can cause serious side effects, such as hypotension, cough, reduced renal function and angioedema. Thus, research was focused on natural ACE inhibitory peptides sources such as foodstuffs and also, more recently, edible insects. In the last decades, ACE inhibitory activity has been detected in protein hydrolysates from insect species belonging to the orders of Coleoptera, Diptera, Hymenoptera, Lepidoptera and also Orthoptera. Further investigations led to identify specific ACE inhibitory peptides from the silkworm Bombyx mori (Lepidoptera: Bombycidae), the yellow mealworm Tenebrio molitor (Coleoptera: Tenebrionidae), the cotton leafworm Spodoptera littoralis (Lepidoptera: Noctuidae) and also from the weaver ant Oecophylla smaragdina (Hymenoptera: Formicidae). Even if ACE inhibitory activity of these bioactive peptides has been in vitro assayed and is comparable to those of some bioactive peptides derived from other animal protein sources, the in vivo effectiveness of most of these bioactive peptides still needs to be confirmed. The aim of this review is to present an outline of the currently available data on the potential use of insects for hypertension treatment with a focus on the ACE inhibitory peptides identified in these invertebrates to date.

scholarly journals Angiotensin Converting Enzyme (ACE) Inhibitory Activity of Peptide Fraction of Germinated Pigeon Pea (Cajanus cajan (L.) Millsp.)

2019 ◽  
Vol 19 (4) ◽  
pp. 900
Author(s):  
Ketut Ratnayani ◽  
I Ketut Suter ◽  
Nyoman Semadi Antara ◽  
I Nengah Kencana Putra
Keyword(s):  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Storage Proteins ◽  
Pigeon Pea ◽  
Ace Inhibitory Activity ◽  
Germination Process ◽  
Peptide Fraction ◽  
Ic50 Value ◽  
Centrifugal Ultrafiltration ◽  
Ace Inhibitory

During the germination process, seeds can release various types of peptides due to the degradation of storage proteins. Some of these peptides can have biological activity (bioactive peptides). The objective of this study was to determine the ACE inhibitory activity of germinated pigeon pea peptide extract at various germination times and to carry out the fractionation to the extract to get the most active peptide fraction. The results showed that the highest activity of peptide extract was found on the 4th-day germination of pigeon pea with an IC50 value of 63.46 μg/mL. The peptide extract was further fractionated by centrifugal ultrafiltration method and it was found that the peptide fraction < 3 kDa had the highest ACE inhibitory activity with an IC50 value of 57.79 μg/mL. The result of identification with the LCMS method to the fraction was able to detect 4 types of the peptide with a molecular weight of 230.304, 294.303, 441.436, and 570.591 Da. These results suggested that the peptide fraction of germinated pigeon pea has the potency as an ACE inhibitory nutraceutical.

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 ACE inhibitory peptides in standard and fermented deer velvet: an in silico and in vitro investigation

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Stephen R. Haines ◽  
Mark J. McCann ◽  
Anita J. Grosvenor ◽  
Ancy Thomas ◽  
Alasdair Noble ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Bioactive Peptides ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
In Vitro Investigation ◽  
Vitro Analysis ◽  
Ace Inhibitory ◽  
In Vitro Analysis

Abstract Background The use of deer velvet antler (DVA) as a potent traditional medicine ingredient goes back for over 2000 years in Asia. Increasingly, though, DVA is being included as a high protein functional food ingredient in convenient, ready to consume products in Korea and China. As such, it is a potential source of endogenous bioactive peptides and of ‘cryptides’, i.e. bioactive peptides enzymatically released by endogenous proteases, by processing and/or by gastrointestinal digestion. Fermentation is an example of a processing step known to release bioactive peptides from food proteins. In this study, we aimed to identify in silico bioactive peptides and cryptides in DVA, before and after fermentation, and subsequently to validate the major predicted bioactivity by in vitro analysis. Methods Peptides that were either free or located within proteins were identified in the DVA samples by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by database searching. Bioactive peptides and cryptides were identified in silico by sequence matching against a database of known bioactive peptides. Angiotensin-converting enzyme (ACE) inhibitory activity was measured by a colorimetric method. Results Three free bioactive peptides (LVVYPW, LVVYPWTQ and VVYPWTQ) were solely found in fermented DVA, the latter two of which are known ACE inhibitors. However matches to multiple ACE inhibitor cryptides were obtained within protein and peptide sequences of both unfermented and fermented DVA. In vitro analysis showed that the ACE inhibitory activity of DVA was more pronounced in the fermented sample, but both unfermented and fermented DVA had similar activity following release of cryptides by simulated gastrointestinal digestion. Conclusions DVA contains multiple ACE inhibitory peptide sequences that may be released by fermentation or following oral consumption, and which may provide a health benefit through positive effects on the cardiovascular system. The study illustrates the power of in silico combined with in vitro methods for analysis of the effects of processing on bioactive peptides in complex functional ingredients like DVA.

scholarly journals Bioactivities and ACE-inhibitory peptides releasing potential of lactic acid bacteria in fermented soy milk

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
J. Undhad Trupti ◽  
Sujit Das ◽  
Divyang Solanki ◽  
Dhvany Kinariwala ◽  
Subrota Hati
Keyword(s):  
Proteolytic Activity ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Growth Behavior ◽  
Soy Milk ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Inhibitory Peptides ◽  
Glucosidase Activity ◽  
Ace Inhibitory

Abstract This study was designed to evaluate the bioactivities such as β-glucosidase activity, α-galactosidase activity, and the growth behavior of the Lactobacillus cultures in soy milk medium. Ten Lactobacillus cultures were considered in this study. L. fermentum (M2) and L. casei (NK9) were selected due to their better α-galactosidase, β-glucosidase activity and growth behavior in soy milk medium during fermentation. Further, soy milk fermented with M2 showed higher proteolytic activity (0.67 OD) and ACE-inhibitory (48.44%) than NK9 (proteolytic activity: 0.48 OD and ACE-inhibitory activity: 41.33%). Bioactive peptides produced during the fermentation of soy milk using the selected Lactobacillus cultures were also identified with potent ACE-inhibitory activity by MALDI-TOF spectrometry, and the identified ACE inhibitory peptide sequences from fermented soy milk were characterized using Biopep database. Graphical abstract

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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