scholarly journals Whey Proteins as Source of Bioactive Peptides Against Hypertension

10.5772/52680 ◽  
2013 ◽  
Author(s):  
Tania G. ◽  
F. Xavier
Keyword(s):  
Bioactive Peptides ◽  
Whey Proteins

Bioactive Peptides from Whey Proteins

Whey Proteins ◽  
2019 ◽  
pp. 519-547 ◽  
Author(s):  
Bimlesh Mann ◽  
Syamala Athira ◽  
Rajan Sharma ◽  
Rajesh Kumar ◽  
Prabin Sarkar
Keyword(s):  
Bioactive Peptides ◽  
Whey Proteins

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.

Using in silico methods to obtain bioactive peptides of whey

2021 ◽  
pp. 32-35
Author(s):  
Ксения Александровна Рязанцева ◽  
Евгения Юрьевна Агаркова
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Whey Proteins ◽  
Food Protein ◽  
Enzyme Preparations ◽  
Dpp Iv ◽  
Activity Modeling ◽  
In Silico Modeling ◽  
Ic50 Values ◽  
Beta Lactoglobulin

Целью данного исследования являлся скрининг биопептидов, высвобождаемых из белков молочной сыворотки с использованием базы данных BIOPEP. В задачи работы входили оценка сывороточных белков как потенциальных предшественников биоактивных пептидов с последующей оценкой их потенциальной биологической активности, моделирование ферментативного гидролиза и оценка полученного пептидного профиля. Объектами исследований являлись белки молочной сыворотки и ферментные препараты трипсин EC (3.4.21.4), химотрипсин EC (3.4.21.1) и алкалаза (EC 3.4.21.62). Методы исследований включали in silico анализ с использованием базы данных BIOPEP-UWM™. В результате исследований в бета-лактоглобулине была определена наибольшая частота встречаемости гипотензивных пептидов, ингибирующих ангиотензин-I-превращающий фермент (АПФ) (A=0,5528), и противодиабетических, ингибирующих дипептидилпептидазу IV (ДПП-IV) (A=0,6584), суммарная доля которых составила более 65 % среди всех потенциальных биопептидов. Наилучший результат при дальнейшем моделировании in silico гидролиза бета-лактоглобулина был получен с использованием трипсина, химотрипсина и алкалазы. Показано, что данные ферменты способствуют выделению пептидов с высокими значениями IC50: гипотензивные (VY [41-42] (IC50 = 7,1 мкМ), VF [80-81] (IC50 = 9,2 мкМ), VY [41-42] (IC50 = 7,1 мкМ), IIAEK [70-74] (IC50 = 63,7 мкМ), VR [122-123] (IC50 = 141мкМ) и противодиабетические (VL [91-92] (IC50 = 74 мкМ), IPAVF (IC50 = 44,7 мкМ), VR [122-123] (IC50 = 52,8 мкМ). Данные проведенного биоинформационного подхода определили условия для последующего воспроизведения на реальных пищевых белковых системах. The aim of this study was to screen for biopeptides released from whey proteins using the BIOPEP database. The tasks of the work included: assessment of whey proteins as potential precursors of bioactive peptides with subsequent assessment of their potential biological activity, modeling of enzymatic hydrolysis and assessment of the obtained peptide profile.The objects of the study were whey proteins and enzyme preparations trypsin EC (3.4.21.4), chymotrypsin EC (3.4.21.1) and Alcalase (EC 3.4.21.62). Research methods are included in silicoanalysis using the BIOPEP-UWM ™ database. As a result of studies on beta-lactoglobulin, the highest frequency of occurrence of antihypertensive peptides that inhibit angiotensin-I-converting enzyme (ACE) (A = 0.5528) and antidiabetic peptides that inhibit dipeptidyl peptidase IV (DPP-IV) (A = 0.6584) was obtained, the total share of which was more than 65 % among all potential biopeptides. The best result in further in silico modeling of beta-lactoglobulin hydrolysis was obtained using trypsin, chymotrypsin, and alkalase. These enzymes were shown to promote the release of peptides with high IC50 values: hypotensive (VY [41-42] (IC50 = 7.1 μM), VF [80-81] (IC50 = 9.2 μM), VY [41-42] (IC50 = 7.1 μM), IIAEK [70-74] (IC50 = 63.7 μM), VR [122-123] (IC50 = 141 μM) and antidiabetic (VL [91-92] (IC50 = 74 μM), IPAVF (IC50 = 44.7 μM), VR [122-123] (IC50 = 52.8 μM). The data of the bioinformatic approach carried out determined the conditions for subsequent reproduction on real food protein systems.

EFFECT OF STRAIN ENTEROCOCCUS FAECALIS AN1 ON RELEASE OF BIOACTIVE PEPTIDES FROM WHEY PROTEINS IN IN VITRO SIMULATED GASTROINTESTINAL CONDITIONS

2020 ◽  
Vol 03 (04) ◽  
pp. 64-68
Author(s):  
Rugiya Sabir Mustafayeva ◽  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Enterococcus Faecalis ◽  
Dairy Products ◽  
Bioactive Peptides ◽  
Whey Proteins ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Gastrointestinal Conditions ◽  
Casein Hydrolyzate

The aim of the study was to study the potential of the proteolytic strain Enterococcus faecalis AN1 to generate inhibition of angiotensin converting enzyme (ACE), as well as to determine the effect of subsequent hydrolysis with pepsin and pancreatin in vitro simulated gastrointestinal system on this activity. Analysis of substrate hydrolysis and peptide formation was performed using SDS-PAGE and electrophoresis by RP-HPLC. Casein hydrolyzate with proteases of the strain showed the ability to produce peptides with ACE inhibition activity, which shows the use of these strains in the development of functional dairy products with antihypertensive properties. The studied strain has the potential to produce functional dairy products. Key words: lactic acid bacteria, proteases, caseins, bioactive peptides, angiotensin converting enzyme

scholarly journals Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates

Biotecnia ◽  
2021 ◽  
Vol 23 (1) ◽  
pp. 161-169
Author(s):  
XOCHITL TOVAR JIMÉNEZ
Keyword(s):  
Whey Protein ◽  
Bioactive Peptides ◽  
Whey Proteins ◽  
Whey Protein Concentrate ◽  
Antihypertensive Activity ◽  
Activity Levels ◽  
Protein Concentrate ◽  
Commercial Enzymes ◽  
Sporisorium Reilianum ◽  
Hydrolysis Of

Whey is a highly polluting by-product of cheese processing. However, it has valuable nutritional properties since it is a rich and balanced source of proteins and amino acids. Therefore, it has a broad range of functional properties that can be exploited for diverse applications. Research has shown how the enzymatic hydrolysis of whey proteins releases bioactive peptides. In the present study, the hydrolysis of whey protein concentrate (WCP) was performed using purified Sporisorium reilianum aspartyl protease (Eap1), commercial enzymes chymotrypsin (C) and trypsin (T), as well as different enzymatic combinations in order to determine which enzyme or combination allowed for the release of peptides presenting the highest antioxidant and antihypertensive activity levels; our results indicated that hydrolysis with Eap1 releases the best-performing peptides in comparison with individual enzymes and their combinations.

scholarly journals OBTAINING OF Β-LACTOGLOBULIN BY GEL FILTRATION OF COW MILK WHEY

2019 ◽  
Vol 2 ◽  
pp. 33-39 ◽  
Author(s):  
Volodymyr Yukalo ◽  
Kateryna Datsyshyn ◽  
Liudmyla Storozh
Keyword(s):  
Bioactive Peptides ◽  
Whey Proteins ◽  
Gel Filtration ◽  
Biologically Active ◽  
Milk Whey ◽  
Active Peptides ◽  
Molecular Weights ◽  
Significant Difference ◽  
Biologically Active Peptides ◽  
Β Lactoglobulin

Milk whey proteins carry out a number of important biological functions and also they are precursors of many biologically active peptides (antihypertensive peptides, antagonists of opioid receptors, regulators of intestinal motility, immunomodulatory, anti-microbial and anti-cancer peptides, appetite regulators and so on.). An important stage in natural bioactive peptides obtaining from milk whey proteins is the isolation of homogeneous proteins-precursors. Considering the significant difference in the molecular masses of whey proteins, a promising method for their selection is gel filtration. The purpose of the research was the fractionation of bioactive peptides precursors from milk whey using gel filtration on Sephadex G-150. The whey was obtained from fresh skimmed milk after isoelectric precipitation of casein. Gel filtration was carried out on the columns from a liquid chromatography kit by the “Reanal” company. The fractional composition and the degree of homogeneity of milk whey proteins were determined by disc-electrophoresis in the plates of a polyacrylamide gel. A repeated gel filtration of fractions from the chromatographic peaks, separated into sections, was performed to increase the fractionation efficiency. While choosing a dextran gel for gel filtration of precursors of biologically active peptides from milk whey proteins, we have taken into account the range of their molecular weights (from 10000 to 150000 Da), the ability to form supramolecular structures (β-LG), as well as the previously obtained results of gel filtration. As a result, it was shown that repeated gel filtration of milk whey on Sephadex G-150 allows efficiently fractionate the proteins-precursors of bioactive peptides. The range of peptides and proteins molecular weights that can be fractionated on this Sephadex is from 5000 to 300 000 Da. The usage of repeated gel filtration on Sephadex G-150 with the chromatogram separation into sectors allows to effectively fractionate proteins-precursors of bioactive peptides from milk whey. In particular, homogeneous β-lactoglobulin (degree of homogeneity > 95 %) and partially purified α-lactalbumin, as well as a group of immunoglobulins and a proteose-peptone fraction were obtained.

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