Journal articles: 'Milk peptides'

1

Ganzorig, Khuukhenbaatar, Tadasu Urashima, and Kenji Fukuda. "Exploring Potential Bioactive Peptides in Fermented Bactrian Camel’s Milk and Mare’s Milk Made by Mongolian Nomads." Foods 9, no. 12 (December 7, 2020): 1817. http://dx.doi.org/10.3390/foods9121817.

Full text

Abstract:

To date, bioactive proteins and peptides from minor livestock milks and their fermented products have been scarcely reported. In Mongolia, nomads are commonly rearing five livestock animal species (i.e., cow, camel, goat, horse, and sheep) for milking and other purposes. In this study, we analyzed the peptide composition in fermented milks of Bactrian camels (Camelus bactrianus) and horses, produced by Mongolian nomads for self-consumption. Peptides from skimmed fermented milks were separated by ultrafiltration and reverse-phase high-performance liquid chromatography. Then, their amino acid sequences were determined by matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. Consequently, eleven peptides were identified in the fermented camel’s milk including four from β-casein (β-CN), three from αs1-CN, and two from both κ-CN and lactophorin. On the other hand, twenty-four peptides were identified in the fermented mare’s milk including nineteen from β-CN, three from αs1-CN, and one from both κ-CN and αs2-CN. According to previous reports on the bioactivities of milk-derived peptides, antibacterial and antihypertensive activities were promising in both the fermented camel’s milk and mare’s milk. In addition, potential antioxidant activity was conjectured in the fermented camel’s milk. Further investigations are currently needed to clarify the potential role of immunomodulatory peptides in the two fermented milks.

APA, Harvard, Vancouver, ISO, and other styles

2

Beverly, Robert L., Robert K. Huston, Andi M. Markell, Elizabeth A. McCulley, Rachel L. Martin, and David C. Dallas. "Milk Peptides Survive In Vivo Gastrointestinal Digestion and Are Excreted in the Stool of Infants." Journal of Nutrition 150, no. 4 (December 28, 2019): 712–21. http://dx.doi.org/10.1093/jn/nxz326.

Full text

Abstract:

ABSTRACT Background Human milk peptides released by gastrointestinal proteases have been identified with bioactivities that can benefit the infant but must first reach their respective sites of activity. Peptides in the stool either survived to or were released inside the intestinal tract, and thus had the opportunity to exert bioactivity there. However, it is unknown whether any milk peptides, bioactive or not, can survive in the stool of infants. Objective The aim of this study was primarily to identify milk peptides in infant stool samples and secondarily test the hypotheses that the milk peptide profiles of stools are different between preterm infants at different days of life and between preterm and term infants. Methods Infant stool samples were collected from 16 preterm infants (<34 weeks gestational age) at 8 or 9 and 21 or 22 days of life (DOL), and from 10 term infants (>34 weeks gestational age) at 8 or 9 DOL. Milk peptides were isolated from the stool samples and identified using tandem MS. The peptide counts and abundances were compared between infant groups. Results In total, 118 exclusively milk-derived peptides from the caseins and α-lactalbumin were present in the stool samples, including some peptides with known or potential bioactivity. The remaining 8014 identified peptides could be derived either from milk or endogenous proteins. Although many individual milk peptides were significantly different between preterm infants at 8/9 and 21/22 DOL and between preterm and term infants, total peptide abundance and count were similar for all 3 groups. Conclusions This is the first study to confirm the survival of milk peptides in the stool of infants. Some of the peptides had potential bioactivities that could influence infant gut development. These results are important to understand the physiological relevance of human milk peptides to the infant.

APA, Harvard, Vancouver, ISO, and other styles

3

Cirrincione, Simona, Anna Luganini, Cristina Lamberti, Marcello Manfredi, Laura Cavallarin, Maria Gabriella Giuffrida, and Enrica Pessione. "Donkey Milk Fermentation by Lactococcus lactis subsp. cremoris and Lactobacillus rhamnosus Affects the Antiviral and Antibacterial Milk Properties." Molecules 26, no. 16 (August 23, 2021): 5100. http://dx.doi.org/10.3390/molecules26165100.

Full text

Abstract:

Background: Milk is considered an important source of bioactive peptides, which can be produced by endogenous or starter bacteria, such as lactic acid bacteria, that are considered effective and safe producers of food-grade bioactive peptides. Among the various types of milk, donkey milk has been gaining more and more attention for its nutraceutical properties. Methods: Lactobacillus rhamnosus 17D10 and Lactococcus lactis subsp. cremoris 40FEL3 were selected for their ability to produce peptides from donkey milk. The endogenous peptides and those obtained after bacterial fermentation were assayed for their antioxidant, antibacterial, and antiviral activities. The peptide mixtures were characterized by means of LC-MS/MS and then analyzed in silico using the Milk Bioactive Peptide DataBase. Results: The peptides produced by the two selected bacteria enhanced the antioxidant activity and reduced E. coli growth. Only the peptides produced by L. rhamnosus 17D10 were able to reduce S. aureus growth. All the peptide mixtures were able to inhibit the replication of HSV-1 by more than 50%. Seventeen peptides were found to have 60% sequence similarity with already known bioactive peptides. Conclusions: A lactic acid bacterium fermentation process is able to enhance the value of donkey milk through bioactivities that are important for human health.

APA, Harvard, Vancouver, ISO, and other styles

4

Liang, Ningjian, Robert L. Beverly, Brian P. Scottoline, and David C. Dallas. "Peptides Derived from In Vitro and In Vivo Digestion of Human Milk Are Immunomodulatory in THP-1 Human Macrophages." Journal of Nutrition 152, no. 1 (November 9, 2021): 331–42. http://dx.doi.org/10.1093/jn/nxab350.

Full text

Abstract:

ABSTRACT Background Milk proteins contain many encrypted bioactive peptides. Whether these bioactive peptides are released in the infant intestine and exert immunomodulatory activity remains unknown. Objective This study examined in vitro immunomodulatory activities of peptides from in vitro– and in vivo–digested human milk. Methods Peptides were extracted from in vitro–digested human milk and pooled intestinal samples from 8 infants fed human milk. Peptides extracted from in vitro–digested samples were fractionated. The in vitro effects of these peptides and fractions on the secretion of TNF-α and IL-8 in LPS-treated human immune THP-1 macrophages were evaluated. The significance of differences between in vitro peptide fraction treatment and control on cytokine production was analyzed by t test. LC-MS/MS–based peptidomics was conducted to identify the peptides. The peptides were screened for potential bioactivity using a sequence homology search using the Milk Bioactive Peptide Database (MBPDB). Results Six fractions of the peptide mixture extracted from the in vitro–digested human milk significantly inhibited TNF-α production by LPS-challenged THP-1 macrophages. Fractions F4, F8, F11, F14, and F17 attenuated IL-8 secretion, and F6/7 and F18 increased IL-8 secretion. Peptides extracted from the pooled in vivo intestinal samples attenuated both TNF-α and IL-8 secretion. There were 266 and 418 peptides identified in the in vitro and in vivo samples, respectively. Among the peptides, 34 and 50 in the in vitro and in vivo samples, respectively, had >80% sequence similarity to bioactive peptides in the MBPDB. Conclusions Peptides released by in vitro and in vivo infant digestion of human milk were immunomodulatory in human immune cells; fractions F4, F8, and F11 were anti-inflammatory; and F6/7 and F18 were proinflammatory. Thirteen peptides were present in all fractions with anti-inflammatory activity, and 38 peptides were present in all fractions with proinflammatory activity. These peptides potentially contributed to the observed immunomodulatory activity of the peptide mixtures.

APA, Harvard, Vancouver, ISO, and other styles

5

Gill, Harsharnjit S., F. Doull, K. J. Rutherfurd, and M. L. Cross. "Immunoregulatory peptides in bovine milk." British Journal of Nutrition 84, S1 (November 2000): 111–17. http://dx.doi.org/10.1017/s0007114500002336.

Full text

Abstract:

Bovine milk is known to contain a number of peptide fractions that can affect immune function. The vast majority of immunoregulatory peptides that have been characterised are hydrolysate derivatives of major milk proteins. Recent research has also indicated that the metabolic activity of probiotic lactic acid bacteria can generate de novo immunoregulatory peptides from milk, via enzymatic degradation of parent milk protein molecules. In contrast, relatively little is known of endogenous, preformed immunoregulatory peptides in milk that may be relevant to modulating human health. The natural in vivo role of preformed and enzymatically derived peptides is likely to be one of regulation of the neonatal (bovine) gastrointestinal tract immune system, in order to modulate immune function with respect to the development of immunocompetence and avoidance of undesirable immunological responses (e.g. tolerance, and hypersensitivity to nutrients). There is scope for the further characterisation of both the origin and function of milk-derived immunoregulatory peptides, so that their potential to influence human health can be fully appraised. This review highlights our current knowledge of milk-derived immunoregulatory peptides, and outlines areas that are of relevance for further research.

APA, Harvard, Vancouver, ISO, and other styles

6

Christensen, Brian, Andrea E. Toth, Simone S. E. Nielsen, Carsten Scavenius, Steen V. Petersen, Jan J. Enghild, Jan T. Rasmussen, Morten S. Nielsen, and Esben S. Sørensen. "Transport of a Peptide from Bovine αs1-Casein across Models of the Intestinal and Blood–Brain Barriers." Nutrients 12, no. 10 (October 16, 2020): 3157. http://dx.doi.org/10.3390/nu12103157.

Full text

Abstract:

The effect of food components on brain growth and development has attracted increasing attention. Milk has been shown to contain peptides that deliver important signals to the brains of neonates and infants. In order to reach the brain, milk peptides have to resist proteolytic degradation in the gastrointestinal tract, cross the gastrointestinal barrier and later cross the highly selective blood–brain barrier (BBB). To investigate this, we purified and characterized endogenous peptides from bovine milk and investigated their apical to basal transport by using human intestinal Caco-2 cells and primary porcine brain endothelial cell monolayer models. Among 192 characterized milk peptides, only the αS1-casein peptide 185PIGSENSEKTTMPLW199, and especially fragments of this peptide processed during the transport, could cross both the intestinal barrier and the BBB cell monolayer models. This peptide was also shown to resist simulated gastrointestinal digestion. This study demonstrates that a milk derived peptide can cross the major biological barriers in vitro and potentially reach the brain, where it may deliver physiological signals.

APA, Harvard, Vancouver, ISO, and other styles

7

Wölk, Michele, Sanja Milkovska-Stamenova, and Ralf Hoffmann. "Comprehensive Profiling of the Native and Modified Peptidomes of Raw Bovine Milk and Processed Milk Products." Foods 9, no. 12 (December 10, 2020): 1841. http://dx.doi.org/10.3390/foods9121841.

Full text

Abstract:

Bovine milk contains a variety of endogenous peptides, partially formed by milk proteases that may exert diverse bioactive functions. Milk storage allows further protease activities altering the milk peptidome, while processing, e.g., heat treatment can trigger diverse chemical reactions, such as Maillard reactions and oxidations, leading to different posttranslational modifications (PTMs). The influence of processing on the native and modified peptidome was studied by analyzing peptides extracted from raw milk (RM), ultra-high temperature (UHT) milk, and powdered infant formula (IF) by nano reversed-phase liquid chromatography coupled online to electrospray ionization (ESI) tandem mass spectrometry. Only unmodified peptides proposed by two independent software tools were considered as identified. Thus, 801 identified peptides mainly originated from αS- and β-caseins, but also from milk fat globular membrane proteins, such as glycosylation-dependent cell adhesion molecule 1. RM and UHT milk showed comparable unmodified peptide profiles, whereas IF differed mainly due to a higher number of β-casein peptides. When 26 non-enzymatic posttranslational modifications (PTMs) were targeted in the milk peptidomes, 175 modified peptides were identified, i.e., mostly lactosylated and a few hexosylated or oxidized peptides. Most modified peptides originated from αS-caseins. The numbers of lactosylated peptides increased with harsher processing.

APA, Harvard, Vancouver, ISO, and other styles

8

Beverly, Robert L., Prajna Woonnimani, Brian P. Scottoline, Jiraporn Lueangsakulthai, and David C. Dallas. "Peptides from the Intestinal Tract of Breast Milk-Fed Infants Have Antimicrobial and Bifidogenic Activity." International Journal of Molecular Sciences 22, no. 5 (February 27, 2021): 2377. http://dx.doi.org/10.3390/ijms22052377.

Full text

Abstract:

For bioactive milk peptides to be relevant to infant health, they must be released by gastrointestinal proteolysis and resist further proteolysis until they reach their site of activity. The intestinal tract is the likeliest site for most bioactivities, but it is currently unknown whether bioactive milk peptides are present therein. The purpose of the present study was to identify antimicrobial and bifidogenic peptides in the infant intestinal tract. Milk peptides were extracted from infant intestinal samples, and the activities of the bulk peptide extracts were determined by measuring growth of Escherichia coli, Staphylococcus aureus, and Bifidobacterium longum spp. infantis after incubation with serial dilutions. The peptide profiles of active and inactive samples were determined by peptidomics analysis and compared to identify candidate peptides for bioactivity testing. We extracted peptides from 29 intestinal samples collected from 16 infants. Five samples had antimicrobial activity against S. aureus and six samples had bifidogenic activity for B. infantis. We narrowed down a list of 6645 milk peptides to 11 candidate peptides for synthesis, of which 6 fully inhibited E. coli and S. aureus growth at concentrations of 2500 and 3000 µg/mL. This study provides evidence for the potential bioactivity of milk peptides in the infant intestinal tract.

APA, Harvard, Vancouver, ISO, and other styles

9

Kahala, Minna, Eero Pahkala, and Anne Pihlanto-Leppälä. "Peptides in fermented Finnish milk products." Agricultural and Food Science 2, no. 5 (September 1, 1993): 379–86. http://dx.doi.org/10.23986/afsci.72663.

Full text

Abstract:

This study was conducted to investigate the rate of proteolysis and peptide profiles of different Finnish fermented milk products. The highest rate of proteolysis was observed in Biokefir, while the greatest change in the rate of proteolysis was observed in Gefilus®. Differences in starters and manufacturing processes reflected on the peptide profiles of the products. Most of the identified peptides originated from either the N- or C-terminal region of β-casein or from the N-terminal region of αs1-casein.

APA, Harvard, Vancouver, ISO, and other styles

10

Juillard, Vincent, Alain Guillot, Dominique Le Bars, and Jean-Claude Gripon. "Specificity of Milk Peptide Utilization byLactococcus lactis." Applied and Environmental Microbiology 64, no. 4 (April 1, 1998): 1230–36. http://dx.doi.org/10.1128/aem.64.4.1230-1236.1998.

Full text

Abstract:

ABSTRACT To study the substrate specificity of the oligopeptide transport system of Lactococcus lactis for its natural substrates, the growth of L. lactis MG1363 was studied in a chemically defined medium containing milk peptides or a tryptic digest of αs2-casein as the source of amino acids. Peptides were separated into acidic, neutral, and basic pools by solid-phase extraction or by cation-exchange liquid chromatography. Their ability to sustain growth and the time course of their utilization demonstrated the preferential use of hydrophobic basic peptides with molecular masses ranging between 600 and 1,100 Da by L. lactis MG1363 and the inability to use large, acidic peptides. These peptide utilization preferences reflect the substrate specificity of the oligopeptide transport system of the strain, since no significant cell lysis was inferred. Considering the free amino acid content of milk and these findings on peptide utilization, it was demonstrated that the cessation of growth of L. lactis MG1363 in milk was due to deprivation of leucine and methionine.

APA, Harvard, Vancouver, ISO, and other styles

11

Lamarque, Mauld, Dominique Aubel, Jean-Christophe Piard, Christophe Gilbert, Vincent Juillard, and Danièle Atlan. "The peptide transport system Opt is involved in both nutrition and environmental sensing during growth of Lactococcus lactis in milk." Microbiology 157, no. 6 (June 1, 2011): 1612–19. http://dx.doi.org/10.1099/mic.0.048173-0.

Full text

Abstract:

Lactococcus lactis is known to take up extracellular peptides via at least three distinct peptide transporters. The well-described oligopeptide transporter Opp alone is able to ensure the growth of L. lactis in milk, while the di- and tripeptide transporter DtpT is involved in a peptide-dependent signalling mechanism. The oligopeptide Opt transporter displays two peptide-binding proteins, OptA and OptS. We previously demonstrated that OptA-dependent transport is dedicated to nutritional peptides, as an optABCDF mutant (of a strain devoid of Opp) has an impaired capacity to grow in milk. Using isogenic peptide transport mutants, this study shows that biosynthesis of the Opt transporter is much less sensitive to downregulation that is dependent on extracellular peptides taken up by DtpT than is Opp biosynthesis; this peptide-dependent regulation relies on the transcriptional repressor CodY. We demonstrate the dual function of the Opt system; while OptA contributes to the bacterial nutrition during growth in milk, OptS is involved in the transport of signalling peptides derived from milk and controlling opp expression. So, these results shed new light on the peptide-dependent regulation relying on two peptide transporters with different specificities: DtpT and Opt (via OptS).

APA, Harvard, Vancouver, ISO, and other styles

12

Rubak, Yuliana Tandi, Lilis Nuraida, Dyah Iswantini, and Endang Prangdimurti. "Angiotensin-I-converting enzyme inhibitory peptides in milk fermented by indigenous lactic acid bacteria." February-2020 13, no. 2 (2020): 345–53. http://dx.doi.org/10.14202/vetworld.2020.345-353.

Full text

Abstract:

Background and Aim: Fermented milk can be used to produce antihypertensive peptides. Lactic acid bacteria (LAB) with its proteolytic system hydrolyze milk protein during fermentation to produce several peptides, which include antihypertensive bioactive peptides. This study aimed to investigate the ability of indigenous LAB for the production of angiotensin-I-converting enzyme inhibitory (ACE-I) peptides in fermented milk and to characterize the ACEI peptides. Materials and Methods: Reconstituted milk (11%) inoculated with ten LAB isolates, and then incubated at 37°C until it reaches pH 4.6. The evaluation was carried out for LAB count, lactic acid concentration, peptide content, and ACE-I activity. The low molecular weight (MW) peptides (<3 kDa) were identified using Nano LC Ultimate 3000 series system Tandem Q Exactive Plus Orbitrap high-resolution mass spectrometry. Results: The result showed that the ten LAB isolates were able to produce ACE-I in fermented milk with the activities in the range of 22.78±2.55-57.36±5.40%. The activity of ACE-I above 50% produced by Lactobacillus delbrueckii BD7, Lactococcus lactis ssp. lactis BD17, and Lactobacillus kefiri YK4 and JK17, with the highest activity of ACE-I produced by L. kefiri YK4 (IC50 0.261 mg/mL) and L. kefiri JK17 (IC50 0.308 mg/mL). Results of peptide identification showed that L. kefiri YK 4 could release as many as 1329, while L. kefiri JK 17 could release 174 peptides. The peptides produced were 95% derived from casein. The other peptides were from α-lactalbumin, β-lactoglobulin, and serum amyloid A. The peptides produced consisted of 6-19 amino acid residues, with MWs of 634-2079 Dalton and detected at 317-1093 m/z. A total of 30 peptides have been recognized based on literature searches as ACE-I peptides (sequence similarity: 100%). Conclusion: L. kefiri YK4 and JK17 are the potential to be used as starter cultures to produce the bioactive peptide as ACE-I in fermented milk.

APA, Harvard, Vancouver, ISO, and other styles

13

Rutherfurd, Kay J., and H. S. Gill. "Peptides affecting coagulation." British Journal of Nutrition 84, S1 (November 2000): 99–102. http://dx.doi.org/10.1017/s0007114500002312.

Full text

Abstract:

Based on amino acid sequence similarities that exist between the fibrinogen γ-chain and κ-casein, and also functional similarities between milk and blood coagulation, considerable effort has been made to investigate the effects of milk proteins and peptides on platelet function and thrombosis. In particular, a number of peptides derived from the glycomacropeptide segment of κ-casein, have been shown to inhibit platelet aggregation and thrombosis. KRDS, a peptide from lactoferrin has also been shown to inhibit platelet aggregation but to a lesser extent than its fibrinogen analogue RGDS. Despite their functional and structural similarities they do not act in the same way on platelet function and are thought to affect thrombus formation differently. Further investigation is needed to determine if these milk-derived bioactive peptides are released naturally following ingestion and might therefore be useful as the basis for milk-based products with anti-thrombotic properties.

APA, Harvard, Vancouver, ISO, and other styles

14

Kusumaningtyas, Eni, R. Widiastuti, H. D. Kusumaningrum, and M. T. Suhartono. "Bioactivities and analysis of peptides from Sumbawa horse milk generated by Bacillus thuringiensis protease." Jurnal Ilmu Ternak dan Veteriner 21, no. 4 (January 11, 2018): 244. http://dx.doi.org/10.14334/jitv.v21i4.1627.

Full text

Abstract:

Sumbawa horse milk is claimed to cure some diseases such as asthma, hypertension, diabetes and gastrointestinal disorder but its potential bioactive peptide has not been explored. The aims of this study are to evaluate bioactivities peptides from Sumbawa horse milk protein hydrolysate and to analyzethe physio-chemical properties of selected peptides. The milk protein was hydrolyzed by Bacillus thuringiensis protease, the peptide produced were sequential fractionated and then analyzed for antibacterial and antioxidant activities. The peptide fraction <3 kDa was then sequenced using LCMS-MS and the physio-chemical properties of the peptides were analyzed. The result showed that peptides fraction <3 kDa from the 30 min hydrolysis was the most active as antibacterial and more active to Gram negative bacteria. For antioxidant, scavenging activity of the fraction per µg protein/mL were 83% to ABTS and 31% to DPPH radicals. The values were similar with vitamin C 12.5 µg/mL for ABTS and 14.5 µg/mL for DPPH. Peptide <tt>HPYFYAPELLYYANK with molecular weight prediction </tt>1887.92 Da and isoelectric point 7.47 has high therapeutic index prediction (64.75). The result showed that peptides from Sumbawa horse milk hydrolyzed by Bacillus thuringiensis protease was active as antibacterial and antioxidant. Peptide <tt>HPYFYAPELLYYANK from fraction <3 kDa was potential as antibacterial.</tt>Key Words: Bacillus thuringiensis, Bioactive Peptide, Horse Milk

APA, Harvard, Vancouver, ISO, and other styles

15

Power, Orla, A. B. Nongonierma, P. Jakeman, and R. J. FitzGerald. "Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes." Proceedings of the Nutrition Society 73, no. 1 (October 17, 2013): 34–46. http://dx.doi.org/10.1017/s0029665113003601.

Full text

Abstract:

The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure–activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM.

APA, Harvard, Vancouver, ISO, and other styles

16

Schanbacher, F. L., R. S. Talhouk, F. A. Murray, L. I. Gherman, and L. B. Willett. "Milk-Borne Bioactive Peptides." International Dairy Journal 8, no. 5-6 (May 1998): 393–403. http://dx.doi.org/10.1016/s0958-6946(98)00062-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Hazum, Eli. "Neuroendocrine peptides in milk." Trends in Endocrinology & Metabolism 2, no. 1 (January 1991): 25–28. http://dx.doi.org/10.1016/1043-2760(91)90057-t.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Zenker, Hannah E., Harry J. Wichers, Monic M. M. Tomassen, Sjef Boeren, Nicolette W. De Jong, and Kasper A. Hettinga. "Peptide Release after Simulated Infant In Vitro Digestion of Dry Heated Cow’s Milk Protein and Transport of Potentially Immunoreactive Peptides across the Caco-2 Cell Monolayer." Nutrients 12, no. 8 (August 18, 2020): 2483. http://dx.doi.org/10.3390/nu12082483.

Full text

Abstract:

Dry heating of cow’s milk protein, as applied in the production of “baked milk”, facilitates the resolution of cow’s milk allergy symptoms upon digestion. The heating and glycation-induced changes of the protein structure can affect both digestibility and immunoreactivity. The immunological consequences may be due to changes in the peptide profile of the digested dry heated milk protein. Therefore, cow’s milk protein powder was heated at low temperature (60 °C) and high temperature (130 °C) and applied to simulated infant in vitro digestion. Digestion-derived peptides after 10 min and 60 min in the intestinal phase were measured using LC-MS/MS. Moreover, digests after 10 min intestinal digestion were applied to a Caco-2 cell monolayer. T-cell epitopes were analysed using prediction software, while specific immunoglobin E (sIgE) binding epitopes were identified based on the existing literature. The largest number of sIgE binding epitopes was found in unheated samples, while T-cell epitopes were equally represented in all samples. Transport of glycated peptide indicated a preference for glucosyl lysine and lactosyl-lysine-modified peptides, while transport of peptides containing epitope structures was limited. This showed that the release of immunoreactive peptides can be affected by the applied heating conditions; however, availability of peptides containing epitopes might be limited.

APA, Harvard, Vancouver, ISO, and other styles

19

Gobbetti, M., P. Ferranti, E. Smacchi, F. Goffredi, and F. Addeo. "Production of Angiotensin-I-Converting-Enzyme-Inhibitory Peptides in Fermented Milks Started by Lactobacillus delbrueckiisubsp. bulgaricus SS1 and Lactococcus lactissubsp. cremoris FT4." Applied and Environmental Microbiology 66, no. 9 (September 1, 2000): 3898–904. http://dx.doi.org/10.1128/aem.66.9.3898-3904.2000.

Full text

Abstract:

ABSTRACT Two fermented milks containing angiotensin-I-converting-enzyme (ACE)-inhibitory peptides were produced by using selectedLactobacillus delbrueckii subsp. bulgaricus SS1 and L. lactis subsp. cremoris FT4. The pH 4.6-soluble nitrogen fraction of the two fermented milks was fractionated by reversed-phase fast-protein liquid chromatography. The fractions which showed the highest ACE-inhibitory indexes were further purified, and the related peptides were sequenced by tandem fast atom bombardment-mass spectrometry. The most inhibitory fractions of the milk fermented by L. delbrueckii subsp.bulgaricus SS1 contained the sequences of β-casein (β-CN) fragment 6-14 (f6-14), f7-14, f73-82, f74-82, and f75-82. Those from the milk fermented by L. lactis subsp.cremoris FT4 contained the sequences of β-CN f7-14, f47-52, and f169-175 and κ-CN f155-160 and f152-160. Most of these sequences had features in common with other ACE-inhibitory peptides reported in the literature. In particular, the β-CN f47-52 sequence had high homology with that of angiotensin-II. Some of these peptides were chemically synthesized. The 50% inhibitory concentrations (IC50s) of the crude purified fractions containing the peptide mixture were very low (8.0 to 11.2 mg/liter). When the synthesized peptides were used individually, the ACE-inhibitory activity was confirmed but the IC50s increased considerably. A strengthened inhibitory effect of the peptide mixtures with respect to the activity of individual peptides was presumed. Once generated, the inhibitory peptides were resistant to further proteolysis either during dairy processing or by trypsin and chymotrypsin.

APA, Harvard, Vancouver, ISO, and other styles

20

Wölk, Michele, Corinna Gebauer, Ralf Hoffmann, and Sanja Milkovska-Stamenova. "Analysis of the Endogenous Peptidomes of Different Infant Formula Types and Human Milk." Foods 10, no. 11 (October 26, 2021): 2579. http://dx.doi.org/10.3390/foods10112579.

Full text

Abstract:

Infant formula (IF) is a commonly used replacement whenever mother’s own milk is not available. Most IFs are based on cow milk (powders, liquids). Alternatives, based on other sources such as goat milk or plants, exist. Independent of the source, IF production and composition are strictly regulated. Besides proteins, minerals, and lipids, milk contains a variety of endogenous peptides. Whereas the human milk peptidome has been studied intensively, the peptidomes of IFs have been mostly neglected. This study investigated the peptidomes of different types of first stage IF, including cow milk-based powders and liquids, and powdered goat milk-based IF, highlighting major similarities and differences to human milk. Extracted native peptidomes were analyzed by nanoRPC-ESI-MS/MS using two different fragmentation techniques allowing the confident identification of 1587 peptides. β-Casein peptides dominated in all samples. Interestingly, powdered and liquid cow milk-based IFs differed in the numbers of β- and αS1-casein peptides, indicating processing-derived variations. However, the peptidomes of cow and goat milk-based IF appeared to be more comparable to each other than to human milk. Despite an overlap in the major source proteins, many peptide sequences were different, i.e., species-specific. Remarkably, the data indicate that the human milk peptidome might be donor-specific as well.

APA, Harvard, Vancouver, ISO, and other styles

21

AGRAWAL, R. P., R. AGRAWAL, M. N. RANGA, and M. RIZWAN. "Insulin like protein from camel milk and similarity with human insulin." Indian Journal of Animal Sciences 92, no. 1 (February 1, 2022): 101–4. http://dx.doi.org/10.56093/ijans.v92i1.120933.

Full text

Abstract:

From experimental studies, clinical studies and epidemiological studies it is proved beyond doubt that camel milk has potential role in prevention and treatment of diabetes. The main purpose of the study to isolate camel milk protein and compare its similarity with human insulin so that camel milk can be used as an adjunct therapy for diabetes. Raw camel milk (30 ml) was used for isolation of protein and peptides. The complete process included trypsin digestion, peptide fractionation and LC-MS technique. Digested and fractionized peptide sample was processed further for liquid chromatography and mass spectra/ tandem mass spectra were recorded in positive-ion and high sensitivity mode. MS/MS spectra were automatically calibrated during dynamic LC-MS. Raw data files were converted to Mascot Generic Format (MGF) and these MGF files were searched against UniPort, NCBI and common MS contaminant database. In our study 13 proteins and 22 peptide sequences were found similar to insulin/ insulin like growth factor and isoform. In our study some very large peptide sequence were identified which were seen similar to NUAK family SNF1-like kinase and this peptide sequence gives evidence of role of camel milk in cancer treatment. Observing so many similar peptides in camel milk sample with human insulin, isoform of insulin, receptors and others give strong evidence that camel milk have proteins/ peptides of such proteins similar to human insulin and give support to finding that camel milk contains insulin like molecule that mimics insulin interaction with its receptors.

APA, Harvard, Vancouver, ISO, and other styles

22

Begunova, Anna V., Olga S. Savinova, Olga A. Glazunova, Konstantin V. Moiseenko, Irina V. Rozhkova, and Tatyana V. Fedorova. "Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow’s Milk: Fermentation and Peptidomics Study." Foods 10, no. 1 (December 23, 2020): 17. http://dx.doi.org/10.3390/foods10010017.

Full text

Abstract:

Bioactive peptides derived from milk proteins are an active research area. Exhibiting numerous positive physiological effects on digestive, cardiovascular, immune and nervous systems, these peptides thought to be one of the most promising ingredients for functional food. Generally, these peptides are inactive within the parent proteins and can be liberated during milk fermentation by the specific proteolytic systems of various Lactobacillus spp. Here we present the study of milk fermentation by Lactobacillus helveticus NK1, Lactobacillus rhamnosus F and Lactobacillus reuteri LR1 strains. It was demonstrated that the antioxidant activity of the milk fermented by these strains concomitantly increased with the strains’ proteolytic activity. For the angiotensin I-converting enzyme (ACE) inhibitory activity, the same tendency was not observed. Although the proteolytic activity of L. helveticus NK1 was two times higher than that of L. rhamnosus F, the milk fermented by these strains showed comparable ACE inhibition. The analysis of the peptide profiles of the fermented milk samples allowed us to hypothesize that some previously unreported peptides can be produced by L. rhamnosus F. In addition, it was demonstrated that these potential ACE-inhibiting peptides originated from the C-terminus of αS2-casein.

APA, Harvard, Vancouver, ISO, and other styles

23

Scanff, P., M. Yvon, S. Thirouin, and J. P. Pelissffir. "Characterization and kinetics of gastric emptying of peptides derived from milk proteins in the preruminant calf." Journal of Dairy Research 59, no. 4 (November 1992): 437–47. http://dx.doi.org/10.1017/s0022029900027102.

Full text

Abstract:

SummaryThe gastric emptying kinetics of peptides derived from milk protein were studied in vivo in preruminant calves by collecting and characterizing the whole effluent leaving the stomach for 12 h after ingestion of crude skim milk. Peptides were isolated by reversed-phase HPLC and identified. Particular attention was paid to biologically active peptides and to peptides that could be precursors of biologically active sequences. A gastrin inhibitor, the caseinomacropeptide, was emptied from the stomach only during the first 0·5 h of digestion and rapidly hydrolysed. Precursors of immunostimulatory peptides from αs1 - and β-caseins were emptied throughout digestion in the gastric effluent. A precursor of β-casomorphins (peptide 58–93 of β-casein) was emptied from the stomach 3·5 h after the meal when it was taken on an empty stomach. From this precursor, peptides that may be resistant to hydrolysis by intestinal peptidase were obtained after in vitro hydrolysis by pancreatic enzymes. A phosphopeptide (fragment 110–142 of αs1-casein) was also found in digesta after a few hours of digestion. When the meal was not taken on an empty stomach, these peptides were emptied in the first digesta at a low concentration. The potential activity of these peptides is discussed. The results support the hypothesis that active sequences could still be present in the gut after the action of pancreatic enzymes.

APA, Harvard, Vancouver, ISO, and other styles

24

Cao, Yan, Jinyang Cai, Xin Li, and Chenbo Ji. "A novel human milk protein-derived peptide BCCY-1 exerts immunomodulatory effects on monocytes through NF-κB and MAPK signaling pathways." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 73.16. http://dx.doi.org/10.4049/jimmunol.204.supp.73.16.

Full text

Abstract:

Abstract Protective effects of breastfeeding in reducing childhood infection have been reported. Human breast milk contains diverse bioactive compounds with direct and indirect antimicrobial activities as well as molecules that modulate the immune system. Although some of the molecules involved in human milk’s beneficial effects on development of immune function have been studied, the role of specific milk component in immunomodulation is not yet clear. Milk protein-derived bioactive peptides have been identified with various health-promoting functions icluding immunoregulation. In the present study, we found that a peptide derived from human milk protein β-casein (BCCY-1) enhance the migration of monocytes without affecting cell proliferation and apoptosis. In addition, BCCY-1 induced the chemokine production via activition of NF-κB and MAPK signaling pathways, which could be blocked by specific inhibitors of NF-κB and MAPK. Moreover, the relative intensity of peptide BCCY-1 as well as a cluster of β-casein derived peptides comprising a fragment of BCCY-1 were decreased in the preterm breast milk compared with the term breast milk, indicating a potential role of BCCY-1 and the similar sequences under physiological condition. Identification of those peptides and their physiological functions are necessary to transfer their potent functional properties into food or potential applications in health-care. This study highlight the important role of β-casein derived peptides in the immunomodulatory effects of human breast milk and suggest a promising way to develop novel dietary supplements, foods and even pharmaceutical agents.

APA, Harvard, Vancouver, ISO, and other styles

25

Zhizhin, N. A. "Investigation of the effect of b-galactosidase enzyme on the storage capacity of low-lactose milk." Agrarian science, no. 9 (November 2, 2021): 42–45. http://dx.doi.org/10.32634/0869-8155-2021-352-9-48-51.

Full text

Abstract:

The article discusses the effect of the b-galactosidase enzyme on the storage capacity of milk with hydrolyzed lactose. For this purpose, parallel studies of a sample of sterilized milk and low-lactose milk, produced on its basis, were carried out. The peptide profile was used as a criterion for assessing the storage capacity of milk that underwent enzymatic decomposition of lactose. Assessment of the state of the peptide profile during storage was recorded at three control points — 30, 60 and 90 days. Studies have shown that at the second checkpoint, peptides were identified that characterize the proteolytic activity in the product. The third checkpoint study revealed the presence of low molecular weight peptides responsible for the bitter taste in milk. Parallel studies of sterilized milk without the addition of the enzyme did not reveal any changes in the peptide profile. The studies carried out indicate that the b-galactosidase enzyme has a residual proteolytic activity, which negatively affects the storage capacity of low-lactose milk and, as a consequence, the products, produced on its basis.

APA, Harvard, Vancouver, ISO, and other styles

26

Nielsen, Søren D., Robert L. Beverly, Mark A. Underwood, and David C. Dallas. "Differences and Similarities in the Peptide Profile of Preterm and Term Mother’s Milk, and Preterm and Term Infant Gastric Samples." Nutrients 12, no. 9 (September 15, 2020): 2825. http://dx.doi.org/10.3390/nu12092825.

Full text

Abstract:

Our previous studies revealed that milk proteases begin to hydrolyze proteins in the mammary gland and that proteolytic digestion continues within the infant stomach. No research has measured how the release of milk peptides differs between the gastric aspirates of term and premature infants. This study examined the presence of milk peptides in milk and gastric samples from term and preterm infants using an Orbitrap Fusion Lumos mass spectrometer. Samples were collected from nine preterm-delivering and four term-delivering mother–infant pairs. Our study reveals an increased count and ion abundance of peptides and decreased peptide length from mother’s milk to the infant stomach, confirming that additional break-down of the milk proteins occurred in both preterm and term infants’ stomachs. Protein digestion occurred at a higher level in the gastric contents of term infants than in gastric contents of preterm infants. An amino acid cleavage site-based enzyme analysis suggested that the observed higher proteolysis in the term infants was due to higher pepsin/cathepsin D activity in the stomach. Additionally, there was a higher quantity of antimicrobial peptides in term infant gastric contents than in those of preterm infants, which could indicate that preterm infants benefit less from bioactive peptides in the gut.

APA, Harvard, Vancouver, ISO, and other styles

27

Baranyi, Maria, Ursula Thomas, and Antonio Pellegrini. "Antibacterial activity of casein-derived peptides isolated from rabbit (Oryctolagus cuniculus) milk." Journal of Dairy Research 70, no. 2 (May 2003): 189–97. http://dx.doi.org/10.1017/s0022029903006150.

Full text

Abstract:

Acid-precipitated rabbit ‘whole casein’ was digested by trypsin, chymotrypsin, pepsin, and clostripain to screen for possible peptides with antibacterial properties. The peptide fragments were separated by reversed-phase chromatography. The collected fractions were pooled and their antibacterial properties tested against Escherichia coli, Bacillus subtilis and Staphylococcus lentus. Three antibacterial peptide fragments derived from tryptic digestion of rabbit casein were isolated and identified. Their sequences were found as follows: HVEQLLR (residues 50–56 of β-casein), ILPFIQSLFPFAER (residues 64–77 of β-casein), and FHLGHLK (residues 19–25 of αs1-casein). The three peptides were synthesized and found to exert antibacterial effect against Gram positive bacteria only. Proteolytic digestion of rabbit casein by chymotrypsin, pepsin and clostripain yielded several peptide fragments with antibacterial activity. Since antibiotic peptides can be released from casein during the digestion of milk proteins, our results suggest a possible antibacterial function of rabbit caseins. It is conceivable that antibacterial peptides can be generated by endopeptidases of the mammalian gastrointestinal tract possibly providing protection for new-born rabbits against aggression of micro-organisms.

APA, Harvard, Vancouver, ISO, and other styles

28

Lestari, Diana, and Eddyson Giordan. "Peptida Bioaktif Kasein Susu Kambing sebagai Agen Antibakteri terhadap Staphylococcus aureus." JURNAL AGROINDUSTRI HALAL 6, no. 1 (April 7, 2020): 028. http://dx.doi.org/10.30997/jah.v6i1.2025.

Full text

Abstract:

Goat milk is widely consumed as a functional food. Milk’s derived bioactive peptides are the specific peptides which are produced by the degradation of milk protein by proteases enzyme and posseses a different positive properties such as antihypertensive, antioxidant, antibacterial, antiiflamatory and many more. The purpose of this research is to explore the antibacterial activity of fractionated bioactive peptides derived from the hydrolysis of goat milk casein and identify the peptide profiles using SDS-PAGE electrophoresis. Casein was isolated from fresh goat milk and then hydrolyzed by crude bromelain enzyme with an activity of 0.420 U/mL for 0, 1, 2, and 3 minutes at a temperature of 50oC. Profile analysis from bromelain hydrolyzates showed some protein bands with molecular weights from about 6.63 kDa to 7.32 kDa on SDS PAGE gel. The fractionation process was carried out on selected bromelain hydrolyzates using a 30 kDa and 10 kDa membrane Cut-Off. The antibacterial test results showed that the hydrolysates from B0 and B1 peptides showed inhibitory activity on Staphylococcus aureus. The fractionation process increased the antibacterial activity of hydrolysates from peptides B0 and B1. Small molecular weight peptides have better inhibitory activity.

APA, Harvard, Vancouver, ISO, and other styles

29

Wedholm, Anna, Hanne S. Møller, Helena Lindmark-Månsson, Morten D. Rasmussen, Anders Andrén, and Lotte B. Larsen. "Identification of peptides in milk as a result of proteolysis at different levels of somatic cell counts using LC MALDI MS/MS detection." Journal of Dairy Research 75, no. 1 (January 29, 2008): 76–83. http://dx.doi.org/10.1017/s0022029907002968.

Full text

Abstract:

The somatic cell count (SCC) in milk is associated with increasing proteolytic degradation of caseins and it has been suggested that enzymes derived from somatic cells contribute to a lower yield and poorer quality of cheese. It is essential to increase the knowledge on naturally occurring milk proteinase activities to better understand how to improve the technological quality of milk. The aim of this work was to identify peptides actually present in milk as a result of proteolysis at different levels of SCC and to assign these peptides to potential responsible proteases where possible. Peptide fractions were prepared from acid whey by ultrafiltration at a molecular cut-off value of 10 000 Da. The peptides were separated using capillary reversed phase high performance liquid chromatography (RP-HPLC) and identified by matrix-assisted laser desorption/ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS). Peptides identified ranged in mass from 1023 to 2000 Da, and originated from αS1-, αS2- or β-casein. Possible responsible proteases that could be suggested when examining the peptide cleavage sites included plasmin, cathepsin B, D and leukocyte elastase. The results indicated that plasmin was primarily responsible for the observed proteolysis in milk at low cell count, whereas the cathepsins and elastase became implicated at elevated cell count. Specificity and activity of cathepsins and elastase has earlier mainly been studied in model systems, whereas less is known about their activities in milk itself. This is also the first indication of involvement of elastase in milk proteolysis through the unequivocal determination of cleavage sites.

APA, Harvard, Vancouver, ISO, and other styles

30

Radosavljević, Jelena, Danijela Apostolović, Jelena Mihailović, Marina Atanasković-Marković, Lidija Burazer, Marianne van Hage, and Tanja Ćirković Veličković. "Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation." Foods 9, no. 11 (October 30, 2020): 1576. http://dx.doi.org/10.3390/foods9111576.

Full text

Abstract:

The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow’s milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow’s milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 ± 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.

APA, Harvard, Vancouver, ISO, and other styles

31

León-López, Arely, Xóchitl Alejandra Pérez-Marroquín, Ana Guadalupe Estrada-Fernández, Gieraldin Campos-Lozada, Alejandro Morales-Peñaloza, Rafael G. Campos-Montiel, and Gabriel Aguirre-Álvarez. "Milk Whey Hydrolysates as High Value-Added Natural Polymers: Functional Properties and Applications." Polymers 14, no. 6 (March 21, 2022): 1258. http://dx.doi.org/10.3390/polym14061258.

Full text

Abstract:

There are two types of milk whey obtained from cheese manufacture: sweet and acid. It retains around 55% of the nutrients of the milk. Milk whey is considered as a waste, creating a critical pollution problem, because 9 L of whey are produced from every 10 L of milk. Some treatments such as hydrolysis by chemical, fermentation process, enzymatic action, and green technologies (ultrasound and thermal treatment) are successful in obtaining peptides from protein whey. Milk whey peptides possess excellent functional properties such as antihypertensive, antiviral, anticancer, immunity, and antioxidant, with benefits in the cardiovascular, digestive, endocrine, immune, and nervous system. This review presents an update of the applications of milk whey hydrolysates as a high value-added peptide based on their functional properties.

APA, Harvard, Vancouver, ISO, and other styles

32

Howland, Vanessa, Maik Klaedtke, Johanna Ruhnau, Vishnu M. Dhople, Hans J. Grabe, Uwe Völker, Matthias Heckmann, and Elke Hammer. "Impact of Storage Conditions on the Breast Milk Peptidome." Nutrients 12, no. 9 (September 8, 2020): 2733. http://dx.doi.org/10.3390/nu12092733.

Full text

Abstract:

Human donor milk (HDM) provides appropriate nutrition and offers protective functions in preterm infants. The aim of the study is to examine the impact of different storage conditions on the stability of the human breast milk peptidome. HDM was directly frozen at −80 °C or stored at −20 °C (120 h), 4 °C (6 h), or room temperature (RT for 6 or 24 h). The milk peptidome was profiled by mass spectrometry after peptide collection by ultrafiltration. Profiling of the peptidome covered 3587 peptides corresponding to 212 proteins. The variance of the peptidome increased with storage temperature and time and varied for different peptides. The highest impact was observed when samples were stored at RT. Smaller but significant effects were still observed in samples stored at 4 °C, while samples showed highest similarity to those immediately frozen at −80 °C when stored at −20 °C. Peptide structures after storage at RT for 24 h point to the increased activity of thrombin and other proteases cleaving proteins at lysine/arginine. The results point to an ongoing protein degradation/peptide production by milk-derived proteases. They underline the need for immediate freezing of HDM at −20 °C or −80 °C to prevent degradation of peptides and enable reproducible investigation of prospectively collected samples.

APA, Harvard, Vancouver, ISO, and other styles

33

Backwell, F. R. C., B. J. Bequette, L. A. Crompton, C. K. Reynolds, D. E. Beever, and J. C. MacRae. "Effect of intravenous histidine or histidine peptide infusion on milk protein yield in lactating goats with an induced histidine deficiency." Proceedings of the British Society of Animal Science 1996 (March 1996): 180. http://dx.doi.org/10.1017/s1752756200593752.

Full text

Abstract:

Studies involving infusion of stable isotope labelled peptides have shown that the mammary gland has the ability to utilise peptide-derived AA for milk protein synthesis (Backwell et al., 1994a) and that peptides may be involved in the supply of phenylalanine to the mammary gland in vivo (Backwell et al., 1994b). The aim of the present experiment was to compare milk production responses to systemic (jugular vein) provision of histidine as free AA or as a peptide (glycyl-histidine) in lactating dairy goats with an induced histidine deficiency.

APA, Harvard, Vancouver, ISO, and other styles

34

Backwell, F. R. C., B. J. Bequette, L. A. Crompton, C. K. Reynolds, D. E. Beever, and J. C. MacRae. "Effect of intravenous histidine or histidine peptide infusion on milk protein yield in lactating goats with an induced histidine deficiency." Proceedings of the British Society of Animal Science 1996 (March 1996): 180. http://dx.doi.org/10.1017/s0308229600031469.

Full text

Abstract:

Studies involving infusion of stable isotope labelled peptides have shown that the mammary gland has the ability to utilise peptide-derived AA for milk protein synthesis (Backwell et al., 1994a) and that peptides may be involved in the supply of phenylalanine to the mammary gland in vivo (Backwell et al., 1994b). The aim of the present experiment was to compare milk production responses to systemic (jugular vein) provision of histidine as free AA or as a peptide (glycyl-histidine) in lactating dairy goats with an induced histidine deficiency.

APA, Harvard, Vancouver, ISO, and other styles

35

Clare, D. A., and H. E. Swaisgood. "Bioactive Milk Peptides: A Prospectus." Journal of Dairy Science 83, no. 6 (June 2000): 1187–95. http://dx.doi.org/10.3168/jds.s0022-0302(00)74983-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Jäkälä, Pauliina, and Heikki Vapaatalo. "Antihypertensive Peptides from Milk Proteins." Pharmaceuticals 3, no. 1 (January 19, 2010): 251–72. http://dx.doi.org/10.3390/ph3010251.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

YOSHKAWA, Masaaki, Fumito TANI, Takashi YOSHIMURA, and Hideo CHIBA. "Opioid peptides from milk proteins." Agricultural and Biological Chemistry 50, no. 9 (1986): 2419–21. http://dx.doi.org/10.1271/bbb1961.50.2419.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Yoshikawa, Masaaki, Fumito Tani, Takashi Yoshimura, and Hideo Chiba. "Opioid Peptides from Milk Proteins." Agricultural and Biological Chemistry 50, no. 9 (September 1986): 2419–21. http://dx.doi.org/10.1080/00021369.1986.10867763.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

FitzGerald, Richard J., Brian A. Murray, and Daniel J. Walsh. "Hypotensive Peptides from Milk Proteins." Journal of Nutrition 134, no. 4 (April 2004): 980S—988S. http://dx.doi.org/10.1093/jn/134.4.980s.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Jauhiainen, Tiina, and Riitta Korpela. "Milk Peptides and Blood Pressure." Journal of Nutrition 137, no. 3 (March 1, 2007): 825S—829S. http://dx.doi.org/10.1093/jn/137.3.825s.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Coste, M., and D. Tome. "Milk peptides with physiological activities. II. Opioid and immunostimulating peptides derived from milk proteins." Le Lait 71, no. 2 (1991): 241–47. http://dx.doi.org/10.1051/lait:1991218.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Ning, Jianting, Mohan Li, Weiyan Chen, Huiwen Zhao, Jiali Chen, Mei Yang, Xueyan Cao, and Xiqing Yue. "Peptidomics as a tool to analyze endogenous peptides in milk and milk-related peptides." Food Bioscience 50 (December 2022): 102199. http://dx.doi.org/10.1016/j.fbio.2022.102199.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Gao, Shuman, Yang Jiang, Xinyi Zhang, Shumao Cui, Xiaoming Liu, Jianxin Zhao, Hao Zhang, and Wei Chen. "Comparative Peptidomics Analysis of Milk Fermented by Lactobacillus helveticus." Foods 11, no. 23 (December 1, 2022): 3885. http://dx.doi.org/10.3390/foods11233885.

Full text

Abstract:

Lactobacillus helveticus is one of the commonly used starter cultures for manufacturing various fermented dairy products. However, only a few studies have explored the cleavage region preference of L. helveticus with different cell envelope proteinase (CEP) genes. In the present study, we profiled the peptide composition of milk samples fermented by three different L. helveticus strains by means of peptidomics to illustrate their different proteolysis patterns. The result revealed that the differences in peptide profiles of milk samples fermented by different L. helveticus strains were mainly a result of variations in the peptide patterns of the casein fractions, which were correlated with CEP genotypes. This was mainly reflected in the extensiveness of the hydrolysis region of αS1-casein and the degree of β-casein hydrolysis. Bioactive peptides were mostly derived from the hydrolysis region common to the three L. helveticus strains, and DQHXN-Q32M42 fermentation resulted in the highest diversity and abundance of bioactive peptides and a significant antihypertensive effect in spontaneous hypertension rats.

APA, Harvard, Vancouver, ISO, and other styles

44

Xing, P. X., J. J. Tjandra, K. Reynolds, P. J. McLaughlin, D. F. Purcell, and I. F. McKenzie. "Reactivity of anti-human milk fat globule antibodies with synthetic peptides." Journal of Immunology 142, no. 10 (May 15, 1989): 3503–9. http://dx.doi.org/10.4049/jimmunol.142.10.3503.

Full text

Abstract:

Abstract The nucleotide sequence of partial cDNA clones coding for the core protein of a human polymorphic epithelial mucin has recently been obtained, this mucin consists of a highly conserved 60 bp tandem repeat and the amino acids commonly found are PDTRPAPGSTAPPAHGVTSA. We synthesized three peptides, 1) P1.24 containing the 20 amino acids and four amino acids (PDTR) of the adjoining repeat; 2) P1.15 consisting of the first fifteen (PDTRPAPGSTAPPAH) and P1.09 the second nine amino acids (GVTSAPDTR) of peptide P1.24. The reactivities of the synthetic peptides with mAb known to react with breast cancer (BC1, BC2, BC3, HMFG-1, 3E1.2, and RCC-1) were studied. The synthetic peptide, P1.24, corresponding to the antigenic sequence predicted from the tandem repeat reacted with antibodies BC1, BC2, and BC3 (known to react with human milk mucin and mucin expressed in breast cancer) and the antibody HMFG-1 which was used to select the cDNA clones. In addition, the epitopes recognized by BC1, BC2, and BC3 appear to be in the same region of the molecule represented by their reactions with the nine amino acids in peptide P1.09 (GVTSAPDTR). By contrast, other antibodies such as 3E1.2 which reacts only weakly with components of human milk, and RCC-1 that detects a low Mr component (95 kDa) in breast cancer, had no specific reaction with the synthetic peptides, indicating that their epitopes are distinct from those of BC1, BC2, BC3, and HMFG-1. Inasmuch as the antibodies HMFG-1, BC1, BC2, and BC3 react with the fully processed milk mucin, it is likely that some of the peptide is exposed, even in the fully glycosylated molecule. Identification of the different epitopes could lead to the development of "second generation" mAb with enhanced specificity for breast carcinoma using the appropriate synthetic peptides as immunogens.

APA, Harvard, Vancouver, ISO, and other styles

45

Ma, Xin, Fan Yang, Xuanyi Meng, Yong Wu, Ping Tong, Jinyan Gao, Hongbing Chen, and Xin Li. "Immunomodulatory Role of BLG-Derived Peptides Based on Simulated Gastrointestinal Digestion and DC-T Cell from Mice Allergic to Cow’s Milk." Foods 11, no. 10 (May 17, 2022): 1450. http://dx.doi.org/10.3390/foods11101450.

Full text

Abstract:

Peptides, but not whole protein, elicit an allergic reaction since food allergens should be consumed by digestion. In this study, we explored the remaining peptides after simulated digestion of cow’s milk in order to search for β-lactoglobulin (BLG)-derived peptides that could play an immunomodulatory role. As a major allergen in milk, BLG-derived peptides, 109 in total, were identified both from simulated infant and adult digestion in vitro. These peptides were mainly located in four regions, and they were synthesized as five peptides, namely, BLG1–14, BLG24–35, BLG40–60, BLG82–101, and BLG123–139. Then, the effect of peptides on the Caco-2 cell’s transport absorption, the co-stimulatory molecules of DC, and the T-cell phenotype was explored. The results suggested all peptides showed better transport absorption capacity with the apparent permeability coefficient higher than 2 × 10−6 cm·s−1. The ability of BLG40–60 for promoting lamina propria-derived DC cell (LPDC) maturation was observed by the increase in MHC II. Moreover, BLG1–14 and BLG40–60 directed activation of T lymphocytes towards a Th1 phenotype. This is the first report of the immunomodulatory potential of peptides in the sensitization of allergic reaction, and one peptide, BLG40–60, was regarded as an immunomodulatory peptide, one that should be further explored in an animal model in depth.

APA, Harvard, Vancouver, ISO, and other styles

46

Dingess, Kelly A., Marita de Waard, Sjef Boeren, Jacques Vervoort, Tim T. Lambers, Johannes B. van Goudoever, and Kasper Hettinga. "Human milk peptides differentiate between the preterm and term infant and across varying lactational stages." Food Funct. 8, no. 10 (2017): 3769–82. http://dx.doi.org/10.1039/c7fo00539c.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Lacroix, Isabelle M. E., Xiu-Min Chen, David D. Kitts, and Eunice C. Y. Li-Chan. "Investigation into the bioavailability of milk protein-derived peptides with dipeptidyl-peptidase IV inhibitory activity using Caco-2 cell monolayers." Food & Function 8, no. 2 (2017): 701–9. http://dx.doi.org/10.1039/c6fo01411a.

Full text

Abstract:

The present study used Caco-2 cell monolayers to investigate the bioavailability of milk protein-derived peptides with DPP-IV inhibitory activity and showed that the susceptibility of the peptides to brush border membrane peptidases impacts their biological activity.

APA, Harvard, Vancouver, ISO, and other styles

48

Aalaei, Kataneh, Bekzod Khakimov, Cristian De Gobba, and Lilia Ahrné. "Gastric Digestion of Milk Proteins in Adult and Elderly: Effect of High-Pressure Processing." Foods 10, no. 4 (April 6, 2021): 786. http://dx.doi.org/10.3390/foods10040786.

Full text

Abstract:

Reduced physiological capability of the human gastrointestinal tract with increasing age has recently attracted considerable attention to the potential of novel technologies to modify food digestion. Thus, the aim of this study was to investigate gastric digestion of milk proteins after application of high-pressure processing (HPP) at 400 MPa 15 min, 600 MPa 5 min and 600 MPa 15 min using two static in vitro models of adults (INFOGEST) and the elderly in comparison to a fresh untreated raw milk. Peptides distribution classified based on the number of amino acids (AA) (<10, 11–15, 16–20, 21–30, >30 AA) were investigated after 0, 5, 10 and 30 min of digestion using LC–MS and multivariate data analysis. Our results show significantly less efficient protein digestion of all investigated milks in the elderly model indicated by higher percentages of longer peptides during digestion, except for the HPP milk 400 MPa 15 min, which indicated an improved and comparable digestion in the elderly as in the adult model. Furthermore, increasing the pressurization time at 600 MPa did not have a significant effect on the peptides profile during the digestion. More efficient digestion of whey proteins in HPP milks, with the majority of peptides in the 16–20 AA range, compared to fresh milk was also noticed. According to the findings of this study, HPP at 400 MPa 15 min showed the most efficient digestion of major milk proteins and thus may be considered a suitable process to improve bioaccessibility of milk proteins, especially in products intended for the elderly.

APA, Harvard, Vancouver, ISO, and other styles

49

Kong, Saerom, Hye-Ryung Choi, Yoon-Jeong Kim, Yoon-Sik Lee, Kyoung-Chan Park, and Seon-Yeong Kwak. "Milk Protein-Derived Antioxidant Tetrapeptides as Potential Hypopigmenting Agents." Antioxidants 9, no. 11 (November 10, 2020): 1106. http://dx.doi.org/10.3390/antiox9111106.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

50

Sebastián-Nicolas, Jessica Lizbeth, Elizabeth Contreras-López, Juan Ramírez-Godínez, Alma Elizabeth Cruz-Guerrero, Gabriela Mariana Rodríguez-Serrano, Javier Añorve-Morga, Judith Jaimez-Ordaz, et al. "Milk Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102: Proteolytic Profile and ACE-Inhibitory Activity." Fermentation 7, no. 4 (October 2, 2021): 215. http://dx.doi.org/10.3390/fermentation7040215.

Full text

Abstract:

Health benefits of probiotics and production of inhibitors of angiotensin converting enzyme (ACE) released during milk fermentation are well known. That is why in this investigation the proteolytic profile and ACE inhibitory capacity of peptide fractions from protein hydrolysis of milk during fermentation processes was analyzed. Milk fermentation was carried out inoculating 106 CFU of L. rhamnosus GG, S. thermophilus SY-102 and with both bacteria. The proteolytic profile was determined using: TNBS, SDS-PAGE and SEC-HPLC techniques. In vitro ACE inhibition capacity was measured. The pH of 4.5 was reached at 56 h when the milk was fermented with L. rhamnosus, at 12 h with S. thermophillus and at 41 h in the co-culture. Production of free amino groups corresponded with the profile of low molecular weight peptides observed by SDS-PAGE and SEC-HPLC. Co-culture fermentation showed both the highest concentration of low molecular weight peptides and the ACE inhibitory activity (>80%). Results indicated that the combination of lactic cultures could be useful in manufacture of fermented milk with an added value that goes beyond basic nutrition, such as the production of ACE-inhibitory peptides.

APA, Harvard, Vancouver, ISO, and other styles

Journal articles on the topic 'Milk peptides'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles