scholarly journals Milk Protein-Derived Antioxidant Tetrapeptides as Potential Hypopigmenting Agents

Antioxidants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1106
Author(s):  
Saerom Kong ◽  
Hye-Ryung Choi ◽  
Yoon-Jeong Kim ◽  
Yoon-Sik Lee ◽  
Kyoung-Chan Park ◽  
...  
Keyword(s):  
Milk Protein ◽  
Antioxidant Activities ◽  
Biological Activities ◽  
Skin Pigmentation ◽  
Milk Proteins ◽  
Mushroom Tyrosinase ◽  
Antioxidant Peptides ◽  
Β Lactoglobulin ◽  
Pigmentation Disorders ◽  
Excessive Accumulation

Excessive accumulation of melanin can cause skin pigmentation disorders, which may be accompanied by significant psychological stress. Although many natural and synthetic products have been developed for the regulation of melanogenesis biochemistry, the management of unwanted skin pigmentation remains challenging. Herein, we investigated the potential hypopigmenting properties of peptide sequences that originated from milk proteins such as ĸ-casein and β-lactoglobulin. These proteins are known to inhibit melanogenesis and their hydrolysates are reported as antioxidant peptides. We synthesize tetrapeptide fragments of the milk protein hydrolysates and investigate the amino acids that are essential for designing peptides with tyrosinase inhibitory and antioxidant activities. We found that the peptide methionine-histidine-isoleucine-arginine amide sufficiently inhibits mushroom tyrosinase activity, shows potent antioxidant activity and effectively impedes melanogenesis in cultured melanocytes via cooperative biological activities. Our findings demonstrate the potential utility of the bioactive tetrapeptide from milk proteins as a chemical alternative to hypopigmenting agents.

Attachment of Listeria innocua to Polystyrene: Effects of Ionic Strength and Conditioning Films from Culture Media and Milk Proteins

2014 ◽  
Vol 77 (3) ◽  
pp. 427-434 ◽  
Author(s):  
GILLES ROBITAILLE ◽  
SÉBASTIEN CHOINIÈRE ◽  
TIMOTHY ELLS ◽  
LOUISE DESCHÈNES ◽  
AKIER ASSANTA MAFU
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bacterial Adhesion ◽  
Bovine Serum ◽  
Biofilm Formation ◽  
Milk Protein ◽  
Milk Proteins ◽  
Listeria Innocua ◽  
Conditioning Films ◽  
Β Lactoglobulin

It is recognized that bacterial adhesion usually occurs on conditioning films made of organic macromolecules absorbed to abiotic surfaces. The objectives of this study were to determine the extent to which milk protein–coated polystyrene (PS) pegs interfere with biofilm formation and the synergistic effect of this conditioning and hypertonic growth media on the bacterial adhesion and biofilm formation of Listeria innocua, used as a nonpathogenic surrogate for Listeria monocytogenes. PS pegs were uncoated (bare PS) or individually coated with whey proteins isolate (WPI), β-lactoglobulin, bovine serum albumin, or tryptic soy broth (TSB) and were incubated in bacterial suspensions in modified Welshimer's broth. After 4 h, the number of adherent cells was dependent on the coating, as follows: TSB (107 CFU/ml) > bare PS > β-lactoglobulin > bovine serum albumin ≈ WPI (104 CFU/ml). The sessile cell counts increased up to 24 h, reaching >107 CFU per peg for all surfaces (P > 0.1), except for WPI-coated PS; this indicates that the inhibitory effects of milk protein conditioning films are transient, slowing down the adhesion process. The 4-h bacterial adhesion on milk protein–coated PS in modified Welshimer's broth supplemented with salt (0 to 10% [wt/vol]) did not vary (P > 0.1), indicating that conditioning with milk proteins was the major determinant for inhibition of bacterial adhesion and that the synergetic effect of salt and milk proteins on adhesion was minimal. Moreover, the presence of 5 to 10% salt significantly inhibited 24-h biofilm formation on the TSB-coated and bare PS, with a decrease of >3 log at 10% (wt/vol) NaCl and almost completely depleted viable sessile bacteria on the milk protein–coated PS.

Biofunctional properties of milk protein derived bioactive peptides -A review

2015 ◽  
Vol 34 (4) ◽  
Author(s):  
Prasad Patil ◽  
Akanksha Wadehra ◽  
Varsha Garg ◽  
Kanchan Munjal ◽  
Sudhir Kumar Tomar ◽  
...  
Keyword(s):  
Milk Protein ◽  
Bioactive Peptides ◽  
Therapeutic Potential ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Milk Proteins ◽  
Physiological Effect ◽  
Amino Acid Sequences ◽  
The Body ◽  
Biologically Active

Milk has long been acknowledged as a source of macro- and micro nutrients. Presently, several identified biologically active substances from milk and their derivatives has attracted much attention from the scientific community. These bioactive compounds confer many health benefits that might support disease prevention. Worldwide, there is an increasing interest in the therapeutic potential of bioactive peptides which collectively present a cornucopia of bioactivities for utilization in humans. Bioactive peptides are hydrolysates with specific amino acid sequences that exert a positive physiological effect on the body. Most of the biological activities are encrypted within the primary sequence of the native protein and can be released during digestion by proteolytic enzymes in the gastrointestinal tract or during fermentation and food processing. Milk protein is an important source of bioactive peptides which may contribute to regulate the nervous, gastrointestinal, and cardiovascular systems as well as the immune system. Milk protein derived bioactive peptides are shown to have antihypertensive, antimicrobial, immunomodulatory, antioxidative and mineral-binding properties. Bioactive peptides derived from milk proteins are of particular interest to the food industry due to the potential functional and physiological roles that they exhibit.

Effect of polymorphisms in the leptin, leptin receptor and acyl-CoA:diacylglycerol acyltransferase 1 (DGAT1) genes and genetic polymorphism of milk proteins on bovine milk composition

2011 ◽  
Vol 79 (1) ◽  
pp. 110-118 ◽  
Author(s):  
Maria Glantz ◽  
Helena Lindmark Månsson ◽  
Hans Stålhammar ◽  
Marie Paulsson
Keyword(s):  
Genetic Polymorphism ◽  
Milk Protein ◽  
Leptin Receptor ◽  
Bovine Milk ◽  
Genetic Selection ◽  
Milk Proteins ◽  
Milk Composition ◽  
Milk Samples ◽  
The Past ◽  
Β Lactoglobulin

The relations between cow genetics and milk composition have gained a lot of attention during the past years, however, generally only a few compositional traits have been examined. The aim of this study was to determine if polymorphisms in the leptin (LEP), leptin receptor (LEPR) and acyl-CoA:diacylglycerol acyltransferase 1 (DGAT1) genes as well as genetic polymorphism of β-casein (β-CN), κ-CN and β-lactoglobulin (β-LG) impact several bovine milk composition traits. Individual milk samples from the Swedish Red and Swedish Holstein breeds were analyzed for components in the protein, lipid, carbohydrate and mineral profiles. Cow alleles were determined on the following SNP: A1457G, A252T, A59V and C963T on the LEP gene, T945M on the LEPR gene and Nt984+8(A-G) on the DGAT1 gene. Additionally, genetic variants of β-CN, κ-CN and β-LG were determined. For both the breeds, the same tendency of minor allele frequency was found for all SNPs and protein genes, except on LEPA1457G and LEPC963T. This study indicated significant (P<0·05) associations between the studied SNPs and several compositional parameters. Protein content was influenced by LEPA1457G (G>A) and LEPC963T (T>C), whereas total Ca, ionic Ca concentration and milk pH were affected by LEPA1457G, LEPA59V, LEPC963T and LEPRT945M. However, yields of milk, protein, CN, lactose, total Ca and P were mainly affected by β-CN (A2>A1) and κ-CN (A>B>E). β-LG was mainly associated with whey protein yield and ionic Ca concentration (A>B). Thus, this study shows possibilities of using these polymorphisms as markers within genetic selection programs to improve and adjust several compositional parameters.

Validation of the RIDASCREEN®FAST Milk Kit

2016 ◽  
Vol 99 (2) ◽  
pp. 495-503 ◽  
Author(s):  
Thomas Weiss ◽  
Markus Lacorn ◽  
Jonathan Flannery ◽  
M Joseph Benzinger ◽  
Patrick Bird ◽  
...  
Keyword(s):  
Milk Protein ◽  
Incubation Temperature ◽  
Sandwich Elisa ◽  
Milk Proteins ◽  
Cross Reactivity ◽  
Significant Loss ◽  
Extraction Temperature ◽  
Independent Laboratory ◽  
The Stability ◽  
Β Lactoglobulin

Abstract The RIDASCREEN®FAST Milk test is a sandwich ELISA for the rapid quantification of milk proteins in various foods. The specific antibodies target casein and β-lactoglobulin. Samples are extracted and can then be analyzed in less than 40 min. The calibration curve covers a range from 2.5 to 67.5 mg/kg milk protein. The assay was validated with cookies, infant formula, chocolate dessert, ice cream, and sausages. All negative samples were found well below the LOQ of 2.5 mg/kg. Recoveries of the spiked samples were mostly in the range of 80–120%. The LOD of the ELISA was found below 1 mg/kg. The analysis of 39 different substances of interest revealed that no cross-reactivity above the LOQ occurred. Ruggedness testing proved that variations in incubation temperature, reagent volume, incubation time, extraction temperature, and extraction time had no significant influence. The stability at 4–8°C of three independent lots was investigated and found to exceed 18 months. Very good lot-to-lot consistency and no significant loss of the analytical capacity over the shelf life were observed. Incurred cookies and chocolate dessert samples were prepared and analyzed by an independent laboratory; mean recoveries of 94.4 and 102.2% and mean SDs of 10.9 and 6.3%, respectively, were found. For the 0 mg/kg level for both materials, all samples tested returned values of &lt;2.5 mg/kg. Therefore, the analytical performance claims of the manufacturer were confirmed.

scholarly journals Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

2020 ◽  
Vol 58 (2) ◽  
pp. 147-158
Author(s):  
Olfa Oussaief ◽  
Zeineb Jrad ◽  
Isabelle Adt ◽  
Touhami Khorchani ◽  
Halima El-Hatmi
Keyword(s):  
Molecular Mass ◽  
Functional Properties ◽  
Milk Protein ◽  
Molecular Mass Distribution ◽  
Antioxidant Activities ◽  
Milk Proteins ◽  
Protein Hydrolysates ◽  
Rp Hplc ◽  
Dromedary Milk ◽  
Hydrolysis Of

Research background. Milk protein hydrolysates have received particular attention due to their health-promoting effects. Dromedary milk differs from the milk of other dairy animals in the composition and structure of its protein components, which give it unique properties. The bioactivity and functionality of whole dromedary milk proteins and their enzymatic hydrolysates have not received much attention, hence this study aims to investigate the effect of enzymatic hydrolysis of dromedary milk proteins on their antioxidant activities and functional properties. Experimental approach. Dromedary milk proteins were treated using four proteolytic enzymes (pepsin, trypsin, α-chymotrypsin and papain) and two mixtures of enzymes (pancreatin and pronase). The degree of hydrolysis was measured to verify the hydrolysis of the proteins. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography served to determine the molecular mass distribution of the hydrolysates while reversed phase-high performance liquid chromatography (RP-HPLC) was conducted to explore their hydrophobicity. The antioxidant activities were evaluated using various in vitro tests, including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical scavenging capacities, iron(III) reducing ability and chelating activity. Besides, functional properties such as solubility, foaming and emulsification were assessed. Results and conclusions. Dromedary milk protein hydrolysates exhibited different degrees of hydrolysis ranging from 17.69 to 41.86 %. Apart from that, the hydrolysates showed different electrophoretic patterns, molecular mass distribution and RP-HPLC profiles demonstrating the heterogeneity of the resulting peptides in terms of molecular mass and polarity. The hydrolysates displayed significantly higher antioxidant capacities than the undigested proteins at all the tested concentrations. Iron(II) chelating activity was the most improved assay after proteolysis and the hydrolysate generated with pancreatin had the highest chelating power. Dromedary milk protein hydrolysates possessed good solubility (&gt;89 %). Further, foaming and emulsifying properties of dromedary milk proteins were enhanced after their proteolysis. These interfacial properties were influenced by the enzymes employed during proteolysis. Novelty and scientific contribution. Enzymatic hydrolysis of dromedary milk proteins is an effective tool to obtain protein hydrolysates with great antioxidant and functional properties. These results suggest that dromedary milk protein hydrolysates could be used as a natural source of antioxidant peptides to formulate functional foods and nutraceuticals.

scholarly journals A Comprehensive Review on the Interaction of Milk Protein Concentrates with Plant-Based Polyphenolics

2021 ◽  
Vol 22 (24) ◽  
pp. 13548
Author(s):  
Mansuri M. Tosif ◽  
Agnieszka Najda ◽  
Aarti Bains ◽  
Thummalacharla Chaitanya Krishna ◽  
Prince Chawla ◽  
...  
Keyword(s):  
Functional Properties ◽  
Milk Protein ◽  
Structural Changes ◽  
Biological Activities ◽  
Structural Characteristics ◽  
Milk Proteins ◽  
Polyphenolic Compounds ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Structural And Functional Properties

Functional properties and biological activities of plant-derived polyphenolic compounds have gained great interest due to their epidemiologically proven health benefits and diverse industrial applications in the food and pharmaceutical industry. Moreover, the food processing conditions and certain chemical reactions such as pigmentation, acylation, hydroxylation, and glycosylation can also cause alteration in the stability, antioxidant activity, and structural characteristics of the polyphenolic compounds. Since the (poly)phenols are highly reactive, to overcome these problems, the formulation of a complex of polyphenolic compounds with natural biopolymers is an effective approach. Besides, to increase the bioavailability and bioaccessibility of polyphenolic compounds, milk proteins such as whey protein concentrate, sodium caseinate, and milk protein concentrate act as natural vehicles, due to their specific structural and functional properties with high nutritional value. Therefore, milk proteins are suitable for the delivery of polyphenols to parts of the gastrointestinal tract. Therefore, this review reports on types of (poly)phenols, methods for the analysis of binding interactions between (poly)phenols–milk proteins, and structural changes that occur during the interaction.

scholarly journals Study on milk composition and milk protein distribution in Romanian Holstein cattle

2020 ◽  
Vol 23 (1) ◽  
pp. 13-21
Author(s):  
Rodica Ştefania Pelmuş ◽  
Cristina Lazăr ◽  
M. L. Palade ◽  
Mariana Stancu ◽  
C. M. Rotar ◽  
...  
Keyword(s):  
Milk Protein ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Protein Composition ◽  
Holstein Cattle ◽  
Protein Distribution ◽  
Quality Indices ◽  
Milk Samples ◽  
Sds Page ◽  
Β Lactoglobulin

AbstractThe aim of this study was to determine milk quality indices as well as the milk protein composition in Romanian Holstein cattle raised under the conditions of experimental farm of INCDBNA-IBNA. The study was carried out on 22 milk samples. The types of different milk proteins were identified by SDS-PAGE technique. Sampling day and milk chemical composition were performed during the milking period of studied cattle. The quality indices were breed-specific for protein (3.38%) and higher for fat (4.39%).Milk proteins analysis of Romanian Holstein cattle separated by SDS-PAGE electrophoresis showed the presence of four major caseins (αs1-, αs2-, β- and k-casein) and two whey proteins (β-lactoglobulin, α-lactalbumin). The caseins accounted 77.28% of the total milk proteins, while the major proteins (β-lactoglobulin, α-lactalbumin) from the whey represented 22.72% of the total proteins. αs1-casein + αs2-casein had a higher expression (36.01%) followed by β-casein (31.45%), β-lactoglobulin (18.16%), k-casein (9.82%) and α-lactalbumin (4.56%). The most of milk samples was characterized by a medium expression level of both caseins and whey proteins

Effect of Heat Treatment and Enzymatic Hydrolysis on Reduction in Allergenicity of Milk Proteins

2018 ◽  
Vol 55 (2) ◽  
pp. 156
Author(s):  
B.P. Pushpa ◽  
G.S. Bhat ◽  
H.M. Jayaprakasha
Keyword(s):  
Heat Treatment ◽  
Enzymatic Hydrolysis ◽  
Milk Protein ◽  
Milk Proteins ◽  
Degree Of Hydrolysis ◽  
Inhibition Elisa ◽  
Protein Allergenicity ◽  
Potent Allergen ◽  
History Of ◽  
Β Lactoglobulin

The allergy due to different fractions of milk protein was estimated by the level of milk specific Ig E blood sera of children suspected for milk allergy with a history of symptoms such as wheezing, diarrhoea or dermatitis. It was observed that among the milk proteins β - lactoglobulin of whey protein is the most potent allergen. Effect of heat treatment and enzymatic hydrolysis on reduction in β - lactoglobulin allergenicity was investigated by inhibition ELISA while heat treatment could reduce the allergenicity only to the extent of 12.5%, enzymatic hydrolysis could reduce the allergenicity significantly. The extent of hydrolysis as well as the enzyme used had significant role in reduction of milk protein allergenicity. The degree of hydrolysis corresponded well with the reduction of milk protein allergenicity. Though chymotrypsin was effective in hydrolyzing β - lactoglobulin, neutrase was more effective in reducing the allergenicity by 52% even at lower degree of hydrolysis. The combination of chymotrypsin and neutrase was found to be more useful in hydrolysis as well as reduction in allergenicity of the protein.

scholarly journals Impact of Sow Milk Protein Polymorphism on Piglet Rearing

2012 ◽  
Vol 12 (3) ◽  
pp. 335-347 ◽  
Author(s):  
Ewa Skrzypczak ◽  
Marek Babicz ◽  
Karolina Szulc ◽  
Anna Walendowska ◽  
Anna Panek
Keyword(s):  
Body Weight ◽  
Milk Protein ◽  
Milk Proteins ◽  
Protein Polymorphism ◽  
Percentage Mortality ◽  
Electrophoretic Separations ◽  
Weight Gains ◽  
White Breed ◽  
Resources Conservation ◽  
Β Lactoglobulin

Impact of Sow Milk Protein Polymorphism on Piglet RearingThe aim of the investigations was to ascertain interrelationships between polymorphic fractions of milk proteins and rearing results of piglets from Złotnicka White sows. The experimental material comprised 20 sows of the native Złotnicka White breed. Pigs of this breed are included in the National Genetic Resources Conservation Programme. Investigations included two successive (2nd and 3rd) lactations of sows during which the following parameters were determined: number and weight of piglets on days 1, 7, 14, 21 and 28; weight gains of individual piglets during the period from day 1 to 7, from day 8 to 14, from day 15 to 21 and from day 22 to 28; as well as mortality for the entire period of rearing, i.e. from day 1 to day 28 of age. A total of 425 piglets born in 40 litters (20 sows x 2 lactations) were investigated. As a result of electrophoretic separations, the following four protein fractions were isolated from sow milk: αs1-casein (CSN1S1), genotypes AA, AB, BB and BC; β-casein (CSN2), genotypes AA, AB and BB; κ-casein (CSN3), genotypes AA, AB and BB; β-lactoglobulin (LGB), genotypes AA and BB. The present study showed that milk from sows of AA CSN1S1 and AA LGB genotypes appeared to be more valuable and nourishing, as indicated by the fact that these sows reared piglets which were characterized by the best production results, i.e. body weight, weight gains and the lowest percentage mortality. The least dynamic results were obtained by piglets originating from litters of sows of the AA-CSN3 genotype.

Improvement of cytoprotective and antioxidant activity of Rosa canina L. and Salix alba L. by controlled differential sieving process against H2O2-induced oxidative stress in mouse primary splenocytes

2017 ◽  
Vol 87 (3-4) ◽  
pp. 191-200 ◽  
Author(s):  
Nidhal Soualeh ◽  
Aliçia Stiévenard ◽  
Elie Baudelaire ◽  
Rachid Soulimani ◽  
Jaouad Bouayed
Keyword(s):  
Antioxidant Activity ◽  
Antioxidant Activities ◽  
Biological Activities ◽  
Good Alternative ◽  
Activity Levels ◽  
Salix Alba ◽  
Rosa Canina ◽  
Free Process ◽  
Plant Powders ◽  
Sieving Process

Abstract. In this study, cytoprotective and antioxidant activities of Rosa canina (RC) and Salix alba (SA), medicinal plants, were studied on mouse primary splenocytes by comparing Controlled Differential Sieving process (CDSp), which is a novel green solvent-free process, versus a conventional technique, employing hydroethanolic extraction (HEE). Thus, preventive antioxidant activity of three plant powders of homogeneous particle sizes, 50–100 µm, 100–180 µm and 180–315 µm, dissolved directly in the cellular buffer, were compared to those of hydroethanolic (HE) extract, at 2 concentrations (250 and 500 µg/mL) in H2O2-treated spleen cells. Overall, compared to HE extract, the superfine powders, i. e., fractions < 180 µm, at the lowest concentration, resulted in greater reactive oxygen species (ROS) elimination, increased glutathione peroxidase (GPx) activity and lower malondialdehyde (MDA) production. Better antioxidant and preventive effects in pre-treated cells were found with the superfine powders for SA (i. e., 50–100 µm and 100–180 µm, both p < 0.001), and with the intermediate powder for RC (i. e., 100–180 µm, p < 0.05) versus HE extract. The activity levels of catalase (CAT) and superoxide dismutase (SOD) in pretreated splenocytes exposed to H2O2, albeit reduced, were near to those in unexposed cells, suggesting that pretreatment with the fine powders has relatively restored the normal levels of antioxidant-related enzymes. These findings supported that CDSp improved the biological activities of plants, avoiding the use of organic solvents and thus it could be a good alternative to conventional extraction techniques.

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