Journal articles: 'Milk proteins'

1

CHANG, M. K., and H. ZHANG. "Carbonated Milk: Proteins." Journal of Food Science 57, no. 4 (July 1992): 880–82. http://dx.doi.org/10.1111/j.1365-2621.1992.tb14314.x.

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SETO, Yasuyuki. "Bovine Milk Proteins." Oleoscience 23, no. 8 (2023): 415–21. http://dx.doi.org/10.5650/oleoscience.23.415.

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3

Ye, Aiqian, Skelte G. Anema, and Harjinder Singh. "Changes in the surface protein of the fat globules during homogenization and heat treatment of concentrated milk." Journal of Dairy Research 75, no. 3 (July 14, 2008): 347–53. http://dx.doi.org/10.1017/s0022029908003464.

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The changes in milk fat globules and fat globule surface proteins of both low-preheated and high-preheated concentrated milks, which were homogenized at low or high pressure, were examined. The average fat globule size decreased with increasing homogenization pressure. The total surface protein (mg m−2) of concentrated milk increased after homogenization, the extent of the increase being dependent on the temperature and the pressure of homogenization, as well as on the preheat treatment. The concentrates obtained from high-preheated milks had higher surface protein concentration than the concentrates obtained from low-preheated milks after homogenization. Concentrated milks heat treated at 79°C either before or after homogenization had greater amounts of fat globule surface protein than concentrated milks heat treated at 50 or 65°C. This was attributed to the association of whey protein with the native MFGM (milk fat globule membrane) proteins and the adsorbed skim milk proteins. Also, at the same homogenization temperature and pressure, the amount of whey protein on the fat globule surface of the concentrated milk that was heated after homogenization was greater than that of the concentrated milk that was heated before homogenization. The amounts of the major native MFGM proteins did not change during homogenization, indicating that the skim milk proteins did not displace the native MFGM proteins but adsorbed on to the newly formed surface.

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Horne, David S., and Jeffrey Leaver. "Milk proteins on surfaces." Food Hydrocolloids 9, no. 2 (June 1995): 91–95. http://dx.doi.org/10.1016/s0268-005x(09)80270-1.

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Wal, Jean-Michel. "Cow's milk proteins/allergens." Annals of Allergy, Asthma & Immunology 89, no. 6 (December 2002): 3–10. http://dx.doi.org/10.1016/s1081-1206(10)62115-1.

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DONNELLY, WILLIAM J., and RAJ K. MEHRA. "Fractionation of milk proteins." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 238–40. http://dx.doi.org/10.1042/bst0180238.

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7

Ye, A., S. G. Anema, and H. Singh. "High-Pressure–Induced Interactions Between Milk Fat Globule Membrane Proteins and Skim Milk Proteins in Whole Milk." Journal of Dairy Science 87, no. 12 (December 2004): 4013–22. http://dx.doi.org/10.3168/jds.s0022-0302(04)73542-0.

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8

Turpeinen, Anu, Hanna Kautiainen, Marja-Leena Tikkanen, Timo Sibakov, Olli Tossavainen, and Eveliina Myllyluoma. "Mild protein hydrolysation of lactose-free milk further reduces milk-related gastrointestinal symptoms." Journal of Dairy Research 83, no. 2 (April 1, 2016): 256–60. http://dx.doi.org/10.1017/s0022029916000066.

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Gastrointestinal symptoms associated with milk are common. Besides lactose, milk proteins may cause symptoms in sensitive individuals. We have developed a method for mild enzymatic hydrolysation of milk proteins and studied the effects of hydrolysed milk on gastrointestinal symptoms in adults with a self-diagnosed sensitive stomach. In a double blind, randomised placebo-controlled study, 97 subjects consumed protein-hydrolysed lactose-free milk or commercially available lactose-free milk for 10 d. Frequency of gastrointestinal symptoms during the study period was reported and a symptom score was calculated. Rumbling and flatulence decreased significantly in the hydrolysed milk group (P < 0·05). Also, the total symptom score was lower in subjects who consumed hydrolysed milk (P < 0·05). No difference between groups was seen in abdominal pain (P = 0·47) or bloating (P = 0·076). The results suggest that mild enzymatic protein hydrolysation may decrease gastrointestinal symptoms in adults with a sensitive stomach.

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9

Montagne, Paul, Marie Louise Cuillière, Claire Molé, Marie Christine Béné, and Gilbert Faure. "Immunological and Nutritional Composition of Human Milk in Relation to Prematurity and Mothers' Parity During the First 2 Weeks of Lactation." Journal of Pediatric Gastroenterology and Nutrition 29, no. 1 (July 1999): 75–80. http://dx.doi.org/10.1002/j.1536-4801.1999.tb02365.x.

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ABSTRACTBackground:To investigate the effect of prematurity and parity on the dynamics of the major immunologic and nutritional proteins of human milk over the first 2 weeks of lactation.Methods:Microparticle‐enhanced nephelometric immunoassays were developed for the quantification of α‐lactalbumin, β‐casein, serum albumin, lactoferrin, and lysozyme in human milk. These components, immunoglobulin A, and total proteins were assayed in 368 individual samples collected from 74 mothers.Results:The dynamics of the major immunologic and nutritional proteins in early lactation presented similar patterns in preterm and term human milks. In comparison with term milk, preterm milk was globally characterized by higher concentrations of immune proteins and lower concentrations of nutritive proteins. These differences were increased by the degree of prematurity, which, however, influenced the absolute and relative protein concentrations differently, depending on the stage of lactation. The protein composition of term milk was similar, whatever the mother's parity. Conversely, the influence of prematurity on the levels of milk proteins during the first days of lactation was even greater in primiparous mothers.Conclusions:This precise description of the composition of preterm and term milk, regarding the main nutritional and immunologic proteins, confirms the influence of both prematurity and parity on milk components and demonstrates the combined effect of these two conditions.

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10

Kinsella, John E., Patrick F. Fox, and Louis B. Rockland. "Water sorption by proteins: Milk and whey proteins." C R C Critical Reviews in Food Science and Nutrition 24, no. 2 (January 1986): 91–139. http://dx.doi.org/10.1080/10408398609527434.

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11

Benjamin-van Aalst, Olga, Christophe Dupont, Lucie van der Zee, Johan Garssen, and Karen Knipping. "Goat Milk Allergy and a Potential Role for Goat Milk in Cow’s Milk Allergy." Nutrients 16, no. 15 (July 24, 2024): 2402. http://dx.doi.org/10.3390/nu16152402.

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In many parts of the world, goat milk has been part of the human diet for millennia. Allergy to goat’s milk, not associated with allergy to cow’s milk, is a rare disorder, although some cases have been described. Goat milk proteins have substantial homology with cow’s milk proteins and even show cross-reactivity; therefore, they are not advised as an alternative to cow’s milk for infants with IgE-mediated cow’s milk allergies. However, there are indications that, due to the composition of the goat milk proteins, goat milk proteins show lower allergenicity than cow’s milk due to a lower αS1-casein content. For this reason, goat milk might be a better choice over cow’s milk as a first source of protein when breastfeeding is not possible or after the breastfeeding period. Additionally, some studies show that goat milk could play a role in specific types of non-IgE-mediated cow milk allergy or even in the prevention of sensitization to cow’s milk proteins. This review discusses a possible role of goat milk in non-IgE mediated allergy and the prevention or oral tolerance induction of milk allergy.

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12

CHUMAKOVA, IRINA, GALINA DONSKAYA, EKATERINA DOBRIYAN, and VIKTOR DROZHZHIN. "ANTIOXIDANT ACTIVITY OF RAW MILK AND MILK PROTEIN FRACTIONS." Elektrotekhnologii i elektrooborudovanie v APK 4, no. 41 (December 2020): 111–18. http://dx.doi.org/10.22314/2658-4859-2020-67-4-111-118.

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Compounds with antioxidant properties act as stabilizers of biological membranes and prevent the development of free-radical chain processes that lead to the development of severe diseases. Cow’s milk shows antioxidant activity due to whey proteins. Heat treatment used in dairy production technology can inhibit the antioxidant properties of milk proteins. Preserving the natural properties of milk is an urgent task. (Research purpose) The research purpose is in studying the antioxidant activity of raw milk and protein fractions isolated from it with optimal preservation of the activity of whey proteins. (Materials and methods) Authors received raw milk from an individual farm in the Moscow region. The physicochemical parameters of milk and whey were assessed by standardized methods; the fractional composition of proteins was assessed by high-performance liquid chromatography; and the antioxidant activity (total content of water-soluble antioxidants) of milk and protein fractions isolated from it assessed by amperometric method. Milk proteins were coagulated using rennet and calcium chloride. Protein fractions were separated by centrifugation (15,000 revolutions per minute) for 90 minutes. (Results and discussion) The article presents the physical and chemical parameters of raw whole and skimmed milk. The fractional composition of native serum proteins with a predominance of beta-lactoglobulin was studied. The method of milk protein isolation by rennet-calcium method was worked out at a minimum temperature of 38-40 degrees Celsius. (Conclusions) The article presents the composition of raw milk. The article presents the developed optimal conditions for isolation of native proteins from raw skim milk. The antioxidant activity of raw milk, casein fraction and whey was assessed. To maximize the preservation of the antioxidant activity of biologically active whey proteins, it is necessary to reduce the generally accepted pasteurization temperatures of milk (75-95 degrees Celsius), while at the same time searching for new methods of decontamination of milk from foreign microflora.

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13

NASALEAN, Alina, Laurentiu OGNEAN, Sergiu MUNTEAN, Stefana BALICI, and Horea MATEI. "Comparative Analysis of Electrophoretic Profile of Major Proteins of Milk from Alpine and Carpathian Goats." Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca. Veterinary Medicine 74, no. 1 (May 18, 2017): 20. http://dx.doi.org/10.15835/buasvmcn-vm:12447.

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The milkâ€™s proteins provide nutritional and biologically active values, essential in human and animal nutrition. In the case of goat milk, the proteinsâ€™ concentration and quality represent basic indices for the evaluation of the nutritional and biologically active values. The proposal is to comparatively analyse the protein profile of milk. The milk was collected from two different breeds: French Alpine and Romanian Carpathian. During March and April 2016 there were collected samples of raw milk in hygienic and sanitation conditions. There were two lots: first lot has 10 Carpathian goats and the second lot has 10 Alpine goats. The protein composition of goat milk was established with SDS-PAGE, after the evaluation of the total proteinsâ€™ concentration with the Bradford method. The quantitative and percentage data obtained with electrophoresis revealed few differences between those 8 identified protein fractions. Between those two lots, regarding the levels of Î²-CN, k-CN and Î²-lactoglobulines there were significant differences. The other protein fractions have values almost identical. Statistical analysis of obtained data shaped the differences in the protein profile at those two breeds. Based on those differences it is to note the superior potential of the Alpine breed regarding the content in biologically active milk proteins. Regarding the obtained data, this study brings new contributions for the evaluation and analysis of protein profile as a nutritive and biologically active component of goat milk, confirming its character as a functional aliment.

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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.

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15

de Kruif, Kees G., Marion A. M. Hoffmann, Marieke E. van Marle, Peter J. J. M. van Mil, Sebastianus P. F. M. Roefs, Marleen Verheul, and Nel Zoon. "Gelation of proteins from milk." Faraday Discussions 101 (1995): 185. http://dx.doi.org/10.1039/fd9950100185.

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16

Albani, S., M. A. Avanzini, R. Maccario, A. Plebani, S. Perversi, G. Licardi, and M. S. Scotta. "Lymphoblastic Response to Milk Proteins." Journal of Pediatric Gastroenterology and Nutrition 7, no. 3 (May 1988): 471. http://dx.doi.org/10.1097/00005176-198805000-00030.

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17

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.

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18

Clark, A. J. "Genetic modification of milk proteins." American Journal of Clinical Nutrition 63, no. 4 (April 1, 1996): 633S—638S. http://dx.doi.org/10.1093/ajcn/63.4.633.

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19

Savilahti, Erkki, and Mikael Kuitunen. "Allergenicity of cow milk proteins." Journal of Pediatrics 121, no. 5 (November 1992): S12—S20. http://dx.doi.org/10.1016/s0022-3476(05)81401-5.

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20

Nunes, M. C., P. Batista, A. Raymundo, M. M. Alves, and I. Sousa. "Vegetable proteins and milk puddings." Colloids and Surfaces B: Biointerfaces 31, no. 1-4 (September 2003): 21–29. http://dx.doi.org/10.1016/s0927-7765(03)00040-7.

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21

Gallagher, Daniel P., Patrick F. Cotter, and Daniel M. Mulvihill. "Porcine milk proteins: A review." International Dairy Journal 7, no. 2-3 (February 1997): 99–118. http://dx.doi.org/10.1016/s0958-6946(96)00056-8.

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22

Fox, P. F. "Milk proteins as food ingredients." International Journal of Dairy Technology 54, no. 2 (May 2001): 41–55. http://dx.doi.org/10.1046/j.1471-0307.2001.00014.x.

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23

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.

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24

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.

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25

Lönnerdal, Bo. "Bioactive proteins in breast milk." Journal of Paediatrics and Child Health 49 (March 2013): 1–7. http://dx.doi.org/10.1111/jpc.12104.

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26

Albani, S., M. A. Avanzini, R. Maccario, A. Plebani, S. Perversi, G. Licardi, and M. S. Scotta. "Lymphoblastic Response to Milk Proteins." Journal of Pediatric Gastroenterology and Nutrition 7, no. 3 (May 1988): 471. http://dx.doi.org/10.1002/j.1536-4801.1988.tb09570.x.

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27

VINȚE, Cezara-Georgiana, and Aurelia COROIAN. "Whey proteins in donkey milk." Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca. Animal Science and Biotechnologies 80, no. 1 (May 30, 2023): 1–6. http://dx.doi.org/10.15835/buasvmcn-asb:2023.0001.

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In recent years, by-products obtained from farm animals are of increasing interest to farmers and once again to the population, which have properties that are not to be neglected by consumers. Milk is one of the main sources of essential compounds, and the by-products obtained from its processing are important elements in human nutrition, bringing an important contribution of elements to the body. Whey is a complex by-product with a high protein content, and in the case of donkey milk, important benefits have been highlighted, such as antimicrobial, antiviral and anti-allergenic properties. The cost of whey from donkey milk is currently low, which is of interest in terms of its capitalization. In the case of whey obtained from donkeys, the amount of protein is very high, thus, it can be successfully used as a substitute in people with allergies to milk of other species and can be harnessed in the form of protein supplements of interest to the population.

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Chrif, Marouane, Abderrahim El Hourch, and Abdellah El Abidi. "Optimized Chemical Analysis of Cow’s Milk Proteins: Evaluation of New Measuring Devices." Indonesian Journal of Chemistry 22, no. 4 (July 1, 2022): 1116. http://dx.doi.org/10.22146/ijc.63900.

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The demands of quality and choice in the dairy industry require analysis of extended performance. Ancient milk protein measuring devices take a long time and provide slow and inaccurate results. This work is part of the reliable analysis of cow’s milk proteins and defines the laws linking the two parameters, total nitrogen (NT) and protein nitrogen (NP). We are studying to prove a fast and effective method for measuring the non-protein nitrogen (NPN) composition of milk that allows the direct calculation of NP from the NT value, whose objective is to adapt the calibration of the Milko Scan FT2 cow’s milk protein analysis since NPN has a direct impact on protein analysis, payment of milk, and on the manufacture of milk products. The study showed that there is a compatibility between these two parameters and gave an idea of the percentage (5.9%) of NPN in milk. New analytical solutions such as the latest generation of the Kjeldahl K-375/376 and the new Milko Scan FT2 meet these needs. Data processing is done using XLSTAT, which is free statistical analysis software.

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Hernández-Caravaca, Iván, Andrés Cabañas, Rebeca López-Úbeda, Leopoldo González-Brusi, Ascensión Guillén-Martínez, Mª José Izquierdo-Rico, Mª Nieves Muñoz-Rodríguez, Manuel Avilés, and Mª Jesús Ruiz García. "Analysis of Minor Proteins Present in Breast Milk by Using WGA Lectin." Children 9, no. 7 (July 20, 2022): 1084. http://dx.doi.org/10.3390/children9071084.

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Breast milk is a complex and dynamic biological fluid and considered an essential source of nutrition in early life. In its composition, the proteins have a relevant biological activity and are related to the multiple benefits demonstrated when compared with artificial milks derived from cow’s milk. Understanding human milk composition provides an important tool for health care providers toward the management of infant feeding and the establishment of breastfeeding. In this work, a new technique was developed to increase the knowledge of human milk, because many of the components remain unknown. To isolate minor proteins present in breast milk by using WGA lectin, breast milk was centrifuged to remove cells and separate the fat phase from the serum phase. The serum obtained was separated into two groups: control (n = 3; whole serum sample from mature milk) and WGA lectin (n = 3; sample processed with WGA lectin to isolate glycosylated proteins). The samples were analyzed by high-performance liquid chromatography coupled to mass spectrometry (HPLC/MS). A total of 84 different proteins were identified from all of the samples. In the WGA lectin group, 55 different proteins were isolated, 77% of which had biological functions related to the immune response. Of these proteins, there were eight WGA lectin group exclusives, and two had not previously been described in breast milk (polyubiquitin-B and POTE ankyrin domain family member F). Isolation by WGA lectin is a useful technique to detect minor proteins in breast milk and to identify proteins that could not be observed in whole serum.

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Sodhi, Monika, RanjitS Kataria, BalwinderK Joshii, Manishi Mukesh, and BishnuP Mishra. "Milk proteins and human health: A1/A2 milk hypothesis." Indian Journal of Endocrinology and Metabolism 16, no. 5 (2012): 856. http://dx.doi.org/10.4103/2230-8210.100685.

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31

Hinz, Katharina, Paula M. O'Connor, Thom Huppertz, R. Paul Ross, and Alan L. Kelly. "Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk." Journal of Dairy Research 79, no. 2 (February 27, 2012): 185–91. http://dx.doi.org/10.1017/s0022029912000015.

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Proteomic analysis of bovine, caprine, buffalo, equine and camel milk highlighted significant interspecies differences. Camel milk was found to be devoid of β-lactoglobulin, whereas β-lactoglobulin was the major whey protein in bovine, buffalo, caprine, and equine milk. Five different isoforms of κ-casein were found in camel milk, analogous to the micro-heterogeneity observed for bovine κ-casein. Several spots observed in 2D-electrophoretograms of milk of all species could tentatively be identified as polypeptides arising from the enzymatic hydrolysis of caseins. The understanding gained from the proteomic comparison of these milks may be of relevance both in terms of identifying sources of hypoallergenic alternatives to bovine milk and detection of adulteration of milk samples and products.

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32

Warner, E. A., A. D. Kanekanian, and A. T. Andrews. "Bioactivity of milk proteins: 1. Anticariogenicity of whey proteins." International Journal of Dairy Technology 54, no. 4 (November 2001): 151–53. http://dx.doi.org/10.1046/j.1364-727x.2001.00029.x.

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33

Lajnaf, Roua, Laetitia Picart-Palmade, Hamadi Attia, Sylvie Marchesseau, and M. A. Ayadi. "Foaming and air-water interfacial properties of camel milk proteins compared to bovine milk proteins." Food Hydrocolloids 126 (May 2022): 107470. http://dx.doi.org/10.1016/j.foodhyd.2021.107470.

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34

Pelmuş, Rodica Ştefania, Cristina Lazăr, M. L. Palade, Mariana Stancu, C. M. Rotar, and M. A. Gras. "Study on milk composition and milk protein distribution in Romanian Holstein cattle." Archiva Zootechnica 23, no. 1 (June 1, 2020): 13–21. http://dx.doi.org/10.2478/azibna-2020-0002.

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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

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O'SULLIVAN, M. M., A. L. KELLY, and P. F. FOX. "Influence of transglutaminase treatment on some physico-chemical properties of milk." Journal of Dairy Research 69, no. 3 (August 2002): 433–42. http://dx.doi.org/10.1017/s0022029902005617.

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Transglutaminase (TGase) is an enzyme that cross-links many proteins, including milk proteins. In this study, the effects of TGase on some physico-chemical properties of milk were studied. TGase-treated milk was not coagulable by rennet, which was due to failure of the primary (enzymic) stage of rennet action rather than the non-enzymic secondary phase. Dissociation of TGase-treated casein micelles by urea or sodium citrate or removal of colloidal calcium phosphate by acidification and dialysis was reduced, presumably due to the formation of cross-links between the caseins. Casein micelles in TGase-treated milks were also resistant to high pressure treatment and to hydrolysis by plasmin. Results of the present study show that milk proteins are fundamentally modified by the action of TGase, which may have applications in the manufacture of functional proteins for use as novel food ingredients.

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Смирнова, Ирина, Irina Smirnova, Николай Гутов, Nikolay Gutov, Андрей Лукин, and Andrey Lukin. "Research of composition of milk protein concentrates." Food Processing: Techniques and Technology 48, no. 1 (January 10, 2019): 85–90. http://dx.doi.org/10.21603/2074-9414-2018-1-85-90.

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Emergence of the dairy products enriched with milky proteinaceous concentrates is connected with low level of consumption of protein the population. Results of a research of structure of two samples of milk protein concentrates – Promilk 852 FBI and Promilk Kappa Optimum for the purpose of their further application in production of dairy products are presented in article. Fractions of proteins of milk protein concentrates with use of size of molecular weight are defined. As a result of electrophoretic division of fractions of proteins the method of a free electrophoresis by means of a cell for an electrophoresis of MINI-PROTEAN has received an initial electrophoregram. In the studied samples the number of fractions of serumal proteins and casein is identified. Absolute values of fractions of serumal proteins and casein in samples of milk protein concentrates are calculated. On the basis of the received values of fractions of serumal proteins and casein their percentage in milk protein concentrates is determined. The received results allow to draw a conclusion that the studied samples of milk protein concentrates can be used in production of dairy products as an additional component for increase in nutrition value of a ready-made product.

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Kato, Yuri, Akihiro Sanda, Naoki Shimojo, and Kazuyuki Sogawa. "Allergenic proteins in cow’s milk and hypoallergenic cow’s milk products." Electrophoresis Letters 59, no. 2 (2015): 55–57. http://dx.doi.org/10.2198/electroph.59.55.

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38

Singh, Harjinder. "Interactions of milk proteins during the manufacture of milk powders." Le Lait 87, no. 4-5 (July 2007): 413–23. http://dx.doi.org/10.1051/lait:2007014.

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39

SCHMIDT, KAREN. "EFFECT OF MILK PROTEINS AND STABILIZER ON ICE MILK QUALITY." Journal of Food Quality 17, no. 1 (March 1994): 9–19. http://dx.doi.org/10.1111/j.1745-4557.1994.tb00127.x.

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40

Liu, Yaowei, Wenjin Zhang, Binsong Han, Lina Zhang, and Peng Zhou. "Changes in bioactive milk serum proteins during milk powder processing." Food Chemistry 314 (June 2020): 126177. http://dx.doi.org/10.1016/j.foodchem.2020.126177.

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41

Martínez-Padilla, L. P., V. García-Mena, N. B. Casas-Alencáster, and M. G. Sosa-Herrera. "Foaming properties of skim milk powder fortified with milk proteins." International Dairy Journal 36, no. 1 (May 2014): 21–28. http://dx.doi.org/10.1016/j.idairyj.2013.11.011.

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42

Kurchenko, Vladimir, Elena Simonenko, Natalia Sushynskaya, Tatsiana Halavach, Andrey Petrov, and Sergey Simonenko. "HPLC Identification of Mare’s Milk and Its Mix with Cow’s Milk." Food Processing: Techniques and Technology 51, no. 2 (June 15, 2021): 402–12. http://dx.doi.org/10.21603/2074-9414-2021-2-402-412.

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Introduction. Mare’s milk is a valuable food product with medicinal properties. In combination with cow’s milk, it is used to create new functional foods. Efficient identification of mare’s milk, cow’s milk, and their mixes prevent falsification. Study objects and methods. The protein composition of mare’s and cow’s milk whey and their mixes was analyzed by high performance liquid chromatography (HPLC) using an Agilent 1200 chromatograph with an Agilent G1315C diode array detector. Separation was performed using a column Machinery Nagel C 18 4.6×250, 5 μm. Results and discussion. The standard HPLC method was optimized to analyse whey proteins in the milk samples. The separation of whey proteins included the following optimal parameters: chromatography time = 60 min, linear gradient of acetonitrile concentration = 0–50%, and sample volume for injection = 20 μl. Alpha-lactoalbumin proved to be the protein of mare’s milk and cow’s milk. The retention time of mare’s α-lactoalbumin was 45.16 min, and that of cow’s milk – 40.09 min. The differences in the retention time of α-lactoalbumin were associated with the presence of 33 amino acid substitutions in the primary structure of both milks. The areas of α-lactoalbumin peaks were used to calculate the amount of cow’s milk added to mare’s milk and the related percentage. Conclusion. A HPLC analysis of whey proteins made it possible to determine up to 50 mL of added cow’s milk in 1 liter of mare’s milk.

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Chen, Fu-Tai A., and Ji-Hong Zang. "Determination of Milk Proteins by Capillary Electrophoresis." Journal of AOAC INTERNATIONAL 75, no. 5 (September 1, 1992): 905–9. http://dx.doi.org/10.1093/jaoac/75.5.905.

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Abstract The potential utility of capillary electrophoresis (CE) for routine determination of milk protein is established. Proteins in cow's milk can be determined by CE in 10 min with high separation efficiency. The major protein components of milk are well-separated and identified. Separations of milk proteins are achieved reliably and reproducibly in an untreated fused-silica column of 21 µm id x 23- 25 cm. Fresh homogenized, low-fat, and nonfat milk show almost identical contents of each protein species; dry milk has a substantially reduced amount of whey proteins, especially oc-lactalbumin. Extensive degradation of whey proteins is evident from a reconstituted dry milk, which may be used to differentiate dry from fresh milk. By using the ratio of β-casein to α-lactalbumin, the adulteration of fresh milk with 25% or more of dry milk could easily be detected.

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Smith, T. J., R. E. Campbell, Y. Jo, and M. A. Drake. "Flavor and stability of milk proteins." Journal of Dairy Science 99, no. 6 (June 2016): 4325–46. http://dx.doi.org/10.3168/jds.2016-10847.

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Rudakov, O. B., and L. V. Rudakova. "Amino acid analysis of milk proteins." Milk branch magazine, no. 12 (November 28, 2019): 32–35. http://dx.doi.org/10.33465/2222-5455-2019-12-32-35.

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Dalsgaard, T. K., C. W. Heegaard, and L. B. Larsen. "Plasmin Digestion of Photooxidized Milk Proteins." Journal of Dairy Science 91, no. 6 (June 2008): 2175–83. http://dx.doi.org/10.3168/jds.2007-0843.

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SZÉPFALUSI, Z., I. NENTWICH, M. GERSTMAYR, E. JOST, L. TODORAN, R. GRATZL, K. HERKNER, and R. URBANEK. "Prenatal allergen contact with milk proteins." Clinical & Experimental Allergy 27, no. 1 (January 1997): 28–35. http://dx.doi.org/10.1111/j.1365-2222.1997.tb00669.x.

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SZEPFALUSI, Z., I. NENTWICH, M. GERSTMAYR, E. JOST, L. TODORAN, R. GRATZL, K. HERKNER, and R. URBANEK. "Prenatal allergen contact with milk proteins." Clinical Experimental Allergy 27, no. 1 (January 1997): 28–35. http://dx.doi.org/10.1046/j.1365-2222.1997.d01-417.x.

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Craig, Oliver, Jacqui Mulville, Mike Parker Pearson, Robert Sokol, Keith Gelsthorpe, Rebecca Stacey, and Matthew Collins. "Detecting milk proteins in ancient pots." Nature 408, no. 6810 (November 2000): 312. http://dx.doi.org/10.1038/35042684.

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Swan, James S., Maryam Azadpur, Ashok J. Bharucha, and Michael A. Krafczyk. "Separation of Proteins in Human Milk." Journal of Liquid Chromatography 11, no. 16 (December 1988): 3385–92. http://dx.doi.org/10.1080/01483918808082261.

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Journal articles on the topic 'Milk proteins'

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