scholarly journals Anti-Diabetic Activity of Whey Proteins

2020 ◽  
Vol 50 (2) ◽  
pp. 306-318
Author(s):  
E. Agarkova ◽  
Ksenia A Ryazantseva ◽  
A. Kruchinin
Keyword(s):  
Inhibitory Activity ◽  
Whey Proteins ◽  
Biologically Active ◽  
Cottage Cheese ◽  
Processing Technologies ◽  
Dpp Iv ◽  
Ic50 Value ◽  
Inhibitory Potential ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

Absract. Introduction. With the advent of membrane filtration technologies, milk whey stopped being a “by-product” of cheese, cottage cheese, and casein production. The combination of various whey-processing technologies, e.g. enzymatic hydrolysis and membrane fractionation, made it possible to obtain concentrates, isolates, and hydrolysates of whey proteins with various biologically active effects. Study objects and methods. The article features research results of Russian and foreign scientific teams in the development of functional antidiabetic ingredients from hydrolyzed proteins of milk and whey. Results and discussion. According to foreign studies, Ile-Pro-Ile (diprotin A) with an IC50 value of 4.7 μM is one of the most effective low molecular mass peptides with an inhibitory potential against DPP-IV. Various studies of trypsin hydrolysis of β-lactoglobulin described the production of IPAVF peptide fragment with the most potent inhibitory activity of DPP-IV (IC50 = 44.7 μM). Other studies featured pepsin-treated lactoglobulin production of fragments LKPTPEGDL and LKPTPEGDLEIL with inhibitory activity DPP-IV IC50 = 45 and 57 μM, respectively. A number of studies described similar fragments obtained by the sequential action of the enzyme preparation Neutrase 0.8 LTM on β-lactoglobulin, followed by pepsin hydrolysis. As for the hydrolysis of α-lactalbumin with pepsin, scientists identified peptides WLAHKALCSEKLDQ, LAHKALCSEKL, and TKCEVFRE. They revealed a high inhibitory potential against DPP-IV (IC50 = 141, 165, and 166 μM, respectively). Tryptic hydrolysates of bovine β-lactoglobulin proved to be able to inhibit DPP-IV in vitro (IC50 of 210 μM). Peptide VAGTWY was the major compound responsible for this effect, displaying an IC50 of 174 μM. In other research, tryptic hydrolysate inhibited DPP-IV with an IC50 value of 1.6 mg/mL, also demonstrating antioxidant and ACE-inhibitory activities. This hydrolysate became source of VAGTWY, the most potent DPP-IV inhibitor (IC50 of 74.9 μM). Conclusion. An analysis of Russian and foreign studies proved that milk protein hydrolysis has a great potential for antidiabetic additives used in the treatment of type II diabetes. This are requires further research in order to define the safety of biologically active peptides.

scholarly journals β-lactoglobulin peptides obtained by chymotrypsin hydrolysis

2021 ◽  
Author(s):  
Brayan Aguilar-Ovando ◽  
Georgina Calderón-Domínguez ◽  
Mariano García-Garibay ◽  
Judith Jiménez-Guzmán ◽  
Eduardo Jardón-Valadez ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Biological Activity ◽  
Inhibitory Activity ◽  
Whey Proteins ◽  
In Vitro Hydrolysis ◽  
Different Types ◽  
Β Lactoglobulin ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis

Objective: Whey proteins, as β-lactoglobulin, have biological activity. Controlled hydrolysis of this protein could generate peptides with some biological function. The aim of this work was to analyze the peptides resulting from the in vitro hydrolysis with chymotrypsin in order to evaluate the presence of bioactive peptides. Design/methodology/approach: Chymotrypsin was used in the hydrolysis of β-lactoglobulin, and its peptides were evaluated by ultrafiltration, electrophoresis, and mass spectrometry. Findings/conclusion: Results showed that 2 h of chymotrypsin hydrolysis (T1) released peptides with molecular weight values of 8 and 9 KDa, while 4 h of hydrolysis (T2) produced peptides with molecular mass weight values of 7 and 5 KDa. The mass spectrometry (MALDI-TOF) showed six peaks and five of them were comparable with those obtained by in silico hydrolysis results (done previously by Fonseca Ayala, 2018). The identified peptides (DTDYK, DAQSAPL and LKPTPEGDL) in the fraction <1 kDa showed inhibitory activity of angiotensin converting enzyme and inhibitory activity of enzyme dipeptidyl peptidase IV according BIOPEP database. These results showed that β-lactoglobulin peptides obtained by chymotrypsin hydrolysis could have biological activity that can be used in different types of industries as pharmaceutical and food. Limitations on study/implications: The in vitro evaluation of the biological activity of the characterized peptides is necessary.

Study on Milk Protein Hydrolysis of Infant Formula

2014 ◽  
Vol 898 ◽  
pp. 326-329
Author(s):  
Li Fu ◽  
Xi Qing Yue ◽  
Jian Xin Song
Keyword(s):  
Infant Formula ◽  
Milk Protein ◽  
Whey Proteins ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Hydrolysis ◽  
Step Process ◽  
Hydrolysis Process ◽  
One Step ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

First of all, whey protein concentrat was added to milk adjusting the proportion of casein and whey proteins to 40:60. And then milk was hydrolyzed by trypsin and flavourzyme (TF) single respectively in one-step process or staged in two-step process. The Antigen contents of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG) during the hydrolysis process were determined by indirect competitive enzyme-linked immunosorbent assay (ELISA) methods. The result showed that the most significant antigen reduction was observed in two-step hydrolysis process compared with one-step hydrolysis process

Peptides released from acid goat whey by a yeast-lactobacillus association isolated from cheese microflora

2006 ◽  
Vol 73 (2) ◽  
pp. 163-170 ◽  
Author(s):  
Sandrine Didelot ◽  
Stephanie Bordenave-Juchereau ◽  
Eric Rosenfeld ◽  
Jean-Marie Piot ◽  
Frederic Sannier
Keyword(s):  
Candida Parapsilosis ◽  
Whey Proteins ◽  
Raw Milk ◽  
Microbiological Analysis ◽  
Aerobic Growth ◽  
Protease Activation ◽  
Proteolytic Activities ◽  
Ph Decrease ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

Seven lactobacilli and a variety of microflora extracted from twenty five commercial cheeses were grown on unsupplemented acid goat whey and screened for their capacity to hydrolyse whey proteins [α-lactalbumin (α-la) and β-lactoglobulin (β-lg)] and to generate peptides. Fermentations were performed aerobically or anaerobically at 37 °C using crude or pre-heated whey (10 min at 65, 75 or 85 °C). Under aerobic conditions, growth of lactobacilli was poor and protein hydrolysis did not occur. Anaerobic conditions slightly increased lactobacilli growth but neither β-lg hydrolysis nor peptide generation were observed. More than 50% of α-la was digested into a truncated form of α-la (±12 kDa) in crude whey and whey pre-heated at 65 °C. Twenty-five microflora extracted from raw milk cheeses were screened for their proteolytic activities on acid goat whey under the conditions previously described. Eight of them were able to hydrolyse up to 50% of α-la mainly during aerobic growth on crude or pre-heated whey. The corresponding hydrolysates were enriched in peptides. The hydrolysate involving microflora extracted from Comté cheese after or at 18 months ripening was the only one to exhibit hydrolysis of both α-la and β-lg. Microbiological analysis showed that microorganisms originating from Comté cheese and capable of growth on unsupplemented whey consisted of Candida parapsilosis and Lactobacillus paracasei. Fermentation kinetic profiles suggested that peptides were released from α-la hydrolysis. The co-culture of both microorganisms was required for α-la hydrolysis that occurred concomitantly with the pH decrease. During whey fermentation, Cand. parapsilosis excrete at least one protease responsible for α-la hydrolysis, and Lb. paracasei is responsible for medium acidification that is required for protease activation.

Highly Potent and Selective Ectonucleoside Triphosphate Diphosphohydrolase (ENTPDase1, 2, 3 and 8) Inhibitors Having 2-substituted-7- trifluoromethyl-thiadiazolopyrimidones Scaffold

2020 ◽  
Vol 16 (5) ◽  
pp. 689-702 ◽  
Author(s):  
Saira Afzal ◽  
Sumera Zaib ◽  
Behzad Jafari ◽  
Peter Langer ◽  
Joanna Lecka ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Binding Pocket ◽  
Docking Studies ◽  
Extracellular Nucleotides ◽  
Nucleoside Triphosphate ◽  
Selective Inhibitors ◽  
Docking Analysis ◽  
Inhibitory Potential ◽  
Malachite Green Assay ◽  
Hydrolysis Of

Background: The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) terminate nucleotide signaling via the hydrolysis of extracellular nucleoside-5'-triphosphate and nucleoside- 5'-diphosphate, to nucleoside-5'-monophosphate and composed of eight Ca2+/Mg2+ dependent ectonucleotidases (NTPDase1-8). Extracellular nucleotides are involved in a variety of physiological mechanisms. However, they are rapidly inactivated by ectonucleotidases that are involved in the sequential removal of phosphate group from nucleotides with the release of inorganic phosphate and their respective nucleoside. Ectonucleoside triphosphate diphosphohydrolases (NTPDases) represent the key enzymes responsible for nucleotides hydrolysis and their overexpression has been related to certain pathological conditions. Therefore, the inhibitors of NTPDases are of particular importance in order to investigate their potential to treat various diseases e.g., cancer, ischemia and other disorders of the cardiovascular and immune system. Methods: Keeping in view the importance of NTPDase inhibitors, a series of thiadiazolopyrimidones were evaluated for their potential inhibitory activity towards NTPDases by the malachite green assay. Results: The results suggested that some of the compounds were found as non-selective inhibitors of isozyme of NTPDases, however, most of the compounds act as potent and selective inhibitors. In case of substituted amino derivatives (4c-m), the compounds 4m (IC50 = 1.13 ± 0.09 μM) and 4g (IC50 = 1.72 ± 0.08 μM) were found to be the most potent inhibitors of h-NTPDase1 and 2, respectively. Whereas, compound 4d showed the best inhibitory potential for both h-NTPDase3 (IC50 = 1.25 ± 0.06 μM) and h-NTPDase8 (0.21 ± 0.02 μM). Among 5a-t derivatives, compounds 5e (IC50 = 2.52 ± 0.15 μM), 5p (IC50 = 3.17 ± 0.05 μM), 5n (IC50 = 1.22 ± 0.06 μM) and 5b (IC50 = 0.35 ± 0.001 μM) were found to be the most potent inhibitors of h-NTPDase1, 2, 3 and 8, respectively. Interestingly, the inhibitory concentration values of above-mentioned inhibitors were several folds greater than suramin, a reference control. In order to determine the binding interactions, molecular docking studies of the most potent inhibitors were conducted into the homology models of NTPDases and the putative binding analysis further confirmed that selective and potent compounds bind deep inside the active pocket of the respective enzymes. Conclusions: The docking analysis proposed that the inhibitory activity correlates with the hydrogen bonds inside the binding pocket. Thus, these derivatives are of interest and may further be investigated for their importance in medicinal chemistry.

Comparison of selective hydrolysis of α-lactalbumin by acid Protease A and Protease M as alternative to pepsin: potential for β-lactoglobulin purification in whey proteins

2019 ◽  
Vol 86 (1) ◽  
pp. 114-119
Author(s):  
Katarina Lisak Jakopović ◽  
Seronei Chelulei Cheison ◽  
Ulrich Kulozik ◽  
Rajka Božanić
Keyword(s):  
High Performance ◽  
Whey Proteins ◽  
Reversed Phase ◽  
Protein Isolate ◽  
Acid Protease ◽  
Selective Hydrolysis ◽  
Hydrolysis Conditions ◽  
Β Lactoglobulin ◽  
Hydrolysis Of ◽  
Enzyme Selectivity

AbstractThe experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes were compared with pepsin hydrolysis since its selectivity to different whey proteins is known. Analysis of the hydrolysis environment showed that the pH and temperature play a significant role in determining the best conditions for achievement of hydrolysis, irrespective of which enzyme was used. Whey protein isolate (WPI) was hydrolysed using pepsin, Acid Protease A and Protease M by randomized hydrolysis conditions. Reversed-phase high performance liquid chromatography was used to analyse residual proteins. Regarding enzyme selectivity under various milieu conditions, all three enzymes showed similarities in the reaction progress and their potential for β-Lg isolation.

scholarly journals Phycobiliproteins from Arthrospira Platensis (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 794 ◽  
Author(s):  
Yuchen Li ◽  
Gilda Aiello ◽  
Carlotta Bollati ◽  
Martina Bartolomei ◽  
Anna Arnoldi ◽  
...  
Keyword(s):  
Dose Response ◽  
Inhibitory Activity ◽  
Arthrospira Platensis ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Esi Ms ◽  
Dpp Iv ◽  
Ic50 Value ◽  
Metabolic Degradation

Arthrospira platensis (spirulina) is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), i.e., C-phycocyanin (C-PC) and allophycocyanin (APC). In this study, PBP were hydrolyzed using trypsin, and the composition of the hydrolysate was characterized by HPLC-ESI-MS/MS. Furthermore, the potential anti-diabetic activity was assessed by using either biochemical or cellular techniques. Findings suggest that PBP peptides inhibit DPP-IV activity in vitro with a dose-response trend and an IC50 value falling in the range between 0.5 and 1.0 mg/mL. A lower inhibition of the DPP-IV activity expressed by Caco-2 cells was observed, which was explained by a secondary metabolic degradation exerted by the same cells.

Selective hydrolysis of α-lactalbumin by Acid Protease A offers potential for β-lactoglobulin purification in whey proteins

LWT ◽  
2012 ◽  
Vol 49 (1) ◽  
pp. 117-122 ◽  
Author(s):  
Seronei Chelulei Cheison ◽  
Elias Kiprono Bor ◽  
Abdul Kipruto Faraj ◽  
Ulrich Kulozik
Keyword(s):  
Whey Proteins ◽  
Acid Protease ◽  
Selective Hydrolysis ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

scholarly journals Antilipase and antioxidant activity of Orthosiphon stamineus methanolic extract

2016 ◽  
Vol 15 (1) ◽  
Author(s):  
Norsyuhada Alias ◽  
Adam Leow Thean Chor ◽  
Mohd. Shukuri Mohamad Ali ◽  
Abu Bakar Salleh ◽  
Asilah Ahmad Tajudin ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Inhibitory Activity ◽  
Methanolic Extract ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Orthosiphon Stamineus ◽  
Ic50 Value ◽  
High Antioxidant Activity ◽  
Treatment Of Obesity ◽  
Hydrolysis Of

Introduction: Antilipase from natural resources are a potential tool for the treatment of obesity while antioxidant-rich plants are essential in combating degenerative diseases. The aim of this study is to determine the antilipase and antioxidant activity of Orthosiphon stamineus methanolic extract. Methods: The inhibitory activity against pancreatic lipase was determined by measuring the hydrolysis of p-nitrophenyl butyrate to p-nitrophenol at 405 nm. Antioxidant activity of O. stamineus extract was measured by 2, 2, diphenyl-1-picrylhydrazyl (DPPH) free radical scavenging activity assay. Results: The O. stamineus crude extract exhibited strong lipase inhibitory activity with an IC50 value of 34.7 µg/ml. The inhibition mode study disclosed that O. stamineus could act as uncompetitive inhibitor. O. stamineus showed high antioxidant activity with an EC50 value of 26.3 µg/ml. Conclusions: The results suggest that O. stamineus has shown potential as a source of natural antilipase and antioxidant.

Exploration of the mechanism of heavy coagulum formation in lactic casein manufacture: role of starter and an unidentified co-factor

1997 ◽  
Vol 64 (1) ◽  
pp. 69-75 ◽  
Author(s):  
MICHAEL G. WEEKS ◽  
EILEEN J. GOSLING ◽  
PETER A. MUNRO
Keyword(s):  
Whey Proteins ◽  
Skim Milk ◽  
Low Ph ◽  
Cottage Cheese ◽  
Heat Inactivation ◽  
Isoelectric Precipitation ◽  
Heat Stable ◽  
Slow Coagulation ◽  
Β Lactoglobulin

Heavy coagulum formation in lactic casein manufacture results in high casein concentration, high starter bacteria concentration and low pH on the base of the coagulation vessel. No heavy coagulum was formed during slow coagulation of skim milk with glucono-δ-lactone, indicating that starter bacteria were necessary. Skim milk preheat treatments severe enough to cause denaturation of the more heat- stable whey proteins, α-lactalbumin and β-lactoglobulin, also caused a reduction in heavy coagulum formation, suggesting the heat inactivation of a co-factor involved in the process. These results suggest a mechanism for heavy coagulum formation similar to that for minor sludge formation in cottage cheese manufacture. Starter bacteria would clump together, probably assisted by a co-factor. These starter clumps would generate a region of low pH causing isoelectric precipitation of casein in and around the clumps. The clumps would then settle forming a layer on the base of the coagulation vessel which might become further compressed by gravity.

Synthesis, In vitro α-Glucosidase Inhibitory Potential and Molecular Docking Studies of 2-Amino-1,3,4-Oxadiazole Derivatives

2020 ◽  
Vol 16 (6) ◽  
pp. 724-734 ◽  
Author(s):  
Hayat Ullah ◽  
Fazal Rahim ◽  
Muhammad Taha ◽  
Raffaqat Hussain ◽  
Abdul Wadood ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
Docking Studies ◽  
Spectroscopic Techniques ◽  
Ongoing Research ◽  
Molecular Docking Studies ◽  
Ic50 Value ◽  
Oxadiazole Derivatives ◽  
Inhibitory Potential ◽  
Synthetic Derivatives

Background: In the recent past, we have synthesized and reported different derivatives of oxadiazoles as potential α-glucosidase inhibitors, keeping in mind, the pharmacological aspects of oxadiazole moiety and in continuation of our ongoing research on the chemistry and bioactivity of new heterocyclic compounds. Methods: 1,3,4-Oxadiazole derivatives (1-14) have been synthesized and characterized by different spectroscopic techniques such as 1H-, 13C-NMR and HREI-MS. Result: The synthetic derivatives were screened for α-glucosidase inhibitory potential. All compounds exhibited good inhibitory activity with IC50 values ranging between 0.80 ± 0.1 to 45.1 ± 1.7 μM in comparison with the standard acarbose having IC50 value 38.45 ± 0.80 μM. Conclusion: Thirteen compounds 1-6 and 8-14 showed potential inhibitory activity as compared to the standard acarbose having IC50 value 38.45 ± 0.80 μM, however, only one compound 7 (IC50 = 45.1 ± 1.7 μM) was found to be less active. Compound 14 (IC50 = 0.80 ± 0.1 μM) showed promising inhibitory activity among all synthetic derivatives. Molecular docking studies were also conducted for the active compounds to understand the ligand-enzyme binding interactions.

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