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Bioactives in bovine milk: chemistry, technology, and applications

Lin, Tiantian, Meletharayil, Gopinathan, Kapoor, Rohit, Abbaspourrad, Alireza·2021·Nutrition Reviews
DOI 10.1093/nutrit/nuab099
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Abstract

The significance of dairy in human health and nutrition is gaining significant momentum as consumers continue to desire wholesome, nutritious foods to fulfill their health and wellness needs. Bovine milk not only consists of all the essential nutrients required for growth and development, it also provides a broad range of bioactive components that play an important role in managing human homeostasis and immune function. In recent years, milk bioactives, including α-lactalbumin, lactoferrin, glycomacropeptide, milk fat globule membrane, and milk oligosaccharides, have been intensively studied because of their unique bioactivity and functionality. Challenges for the application of these bioactive components in food and pharmaceutical formulations are associated with their isolation and purification on an industrial scale and also with their physical and chemical instability during processing, storage, and digestion. These challenges can be overcome by advanced separation techniques and sophisticated nano- or micro-encapsulation technologies. Current knowledge about the chemistry, separation, and encapsulation technology of major bioactives derived from bovine milk and their application in the food industry is reviewed here.

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  1. Haug, 2007, Bovine milk in human nutrition – a review, Lipids Health Dis., 6, 25, 10.1186/1476-511X-6-25 · DOI · Paper page
  2. Ren, 2021, Understanding the role of milk in regulating human homeostasis in the context of the COVID-19 global pandemic, Trends Food Sci Technol., 107, 157, 10.1016/j.tifs.2020.09.027 · DOI
  3. Pouliot, 2008, Membrane processes in dairy technology—from a simple idea to worldwide panacea, Int Dairy J, 18, 735, 10.1016/j.idairyj.2008.03.005 · DOI
  4. Dallas, 2014, Food Oligosaccharides, 21, 10.1002/9781118817360.ch2 · DOI
  5. Layman, 2018, Applications for α-lactalbumin in human nutrition, Nutr Rev., 76, 444, 10.1093/nutrit/nuy004 · DOI · Paper page
  6. Kamau, 2010, Alpha-lactalbumin: its production technologies and bioactive peptides, Compr Rev Food Sci Food Saf, 9, 197, 10.1111/j.1541-4337.2009.00100.x · DOI
  7. Chatterton, 2006, Bioactivity of β-lactoglobulin and α-lactalbumin—technological implications for processing, Int Dairy J, 16, 1229, 10.1016/j.idairyj.2006.06.001 · DOI · Paper page
  8. Barbana, 2006, Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy, Int Dairy J, 16, 18, 10.1016/j.idairyj.2005.01.007 · DOI
  9. Wang, 2019, Lactoferrin: structure, function, denaturation and digestion, Crit Rev Food Sci Nutr., 59, 580, 10.1080/10408398.2017.1381583 · DOI · Paper page
  10. King, 2007, A double-blind, placebo-controlled, pilot study of bovine lactoferrin supplementation in bottle-fed infants, J Pediatr Gastroenterol Nutr, 44, 245, 10.1097/01.mpg.0000243435.54958.68 · DOI
  11. Wang, 2018, Effect of lactoferrin on taste and smell abnormalities induced by chemotherapy: a proteome analysis, Food Funct., 9, 4948, 10.1039/C8FO00813B · DOI
  12. Rastogi, 2016, Structure of iron saturated C-lobe of bovine lactoferrin at pH 6.8 indicates a weakening of iron coordination, Proteins Struct Funct Bioinforma, 84, 591, 10.1002/prot.25004 · DOI
  13. Córdova-Dávalos, 2019, Glycomacropeptide bioactivity and health: a review highlighting action mechanisms and signaling pathways, Nutrients, 11, 598, 10.3390/nu11030598 · DOI
  14. Thomä-Worringer, 2006, Health effects and technological features of caseinomacropeptide, Int Dairy J, 16, 1324, 10.1016/j.idairyj.2006.06.012 · DOI
  15. Neelima Sharma, 2013, Chemical and functional properties of glycomacropeptide (GMP) and its role in the detection of cheese whey adulteration in milk: a review, Dairy Sci Technol, 93, 21, 10.1007/s13594-012-0095-0 · DOI
  16. Dewettinck, 2008, Nutritional and technological aspects of milk fat globule membrane material, Int Dairy J, 18, 436, 10.1016/j.idairyj.2007.10.014 · DOI · Paper page
  17. Fontecha, 2020, Sources, production, and clinical treatments of milk fat globule membrane for infant nutrition and well-being, Nutrients, 12, 1607, 10.3390/nu12061607 · DOI
  18. Timby, 2017, Supplementation of infant formula with bovine milk fat globule membranes, Adv Nutr., 8, 351, 10.3945/an.116.014142 · DOI
  19. Robinson, 2019, Structures and metabolic properties of bovine milk oligosaccharides and their potential in the development of novel therapeutics, Front Nutr., 6, 50, 10.3389/fnut.2019.00050 · DOI
  20. Zivkovic, 2011, Bovine milk as a source of functional oligosaccharides for improving human health, Adv Nutr., 2, 284, 10.3945/an.111.000455 · DOI
  21. Barile, 2009, Permeate from cheese whey ultrafiltration is a source of milk oligosaccharides, Int Dairy J., 19, 524, 10.1016/j.idairyj.2009.03.008 · DOI
  22. Argenta, 2019, Membrane separation processes applied to whey: a review, Food Rev Int, 36, 1
  23. Carter, 2021, Invited review: microfiltration-derived casein and whey proteins from milk, J Dairy Sci., 104, 2465, 10.3168/jds.2020-18811 · DOI
  24. Qiu, 2015, The effect of microfiltration on color, flavor, and functionality of 80% whey protein concentrate, J Dairy Sci., 98, 5862, 10.3168/jds.2014-9174 · DOI
  25. Mercier-Bouchard, 2017, Process efficiency of casein separation from milk using polymeric spiral-wound microfiltration membranes, J Dairy Sci., 100, 8838, 10.3168/jds.2017-13015 · DOI
  26. Hernández, 2009, Isolation of caseins from whey proteins by microfiltration modifying the mineral balance in skim milk, J Dairy Sci., 92, 5357, 10.3168/jds.2009-2335 · DOI
  27. Cheryan, 1998, Ultrafiltration and Microfiltration Handbook, 10.1201/9781482278743 · DOI · Paper page
  28. Baldasso, 2011, Concentration and purification of whey proteins by ultrafiltration, Desalination, 278, 381, 10.1016/j.desal.2011.05.055 · DOI · Paper page
  29. Andrés, 1995, Skimmed milk demineralization by electrodialysis: conventional versus selective membranes, J Food Eng, 26, 57, 10.1016/0260-8774(94)00042-8 · DOI
  30. Chen, 2016, Removal of lactic acid from acid whey using electrodialysis, Sep Purif Technol, 158, 230, 10.1016/j.seppur.2015.12.016 · DOI
  31. Xu, 2011, Protein purification by polyelectrolyte coacervation: influence of protein charge anisotropy on selectivity, Biomacromolecules, 12, 1512, 10.1021/bm101465y · DOI
  32. Ganju, 2017, A review on approaches for efficient recovery of whey proteins from dairy industry effluents, J Food Eng, 215, 84, 10.1016/j.jfoodeng.2017.07.021 · DOI
  33. Bramaud, 1997, Optimisation of a whey protein fractionation process based on the selective precipitation of α-lactalbumin, Lait., 77, 411, 10.1051/lait:1997328 · DOI
  34. Tolkach, 2006, Optimization of thermal pretreatment conditions for the separation of native α-lactalbumin from whey protein concentrates by means of selective denaturation of β-lactoglobulin, J Food Sci, 70, E557, 10.1111/j.1365-2621.2005.tb08319.x · DOI
  35. Toro-Sierra, 2013, Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale, Food Bioprocess Technol., 6, 1032, 10.1007/s11947-011-0732-2 · DOI
  36. Haller, 2020, Continuous centrifugal separation of selectively precipitated α-lactalbumin, Int Dairy J, 101, 104566, 10.1016/j.idairyj.2019.104566 · DOI
  37. Cheang, 2003, Separation of alpha-lactalbumin and beta-lactoglobulin using membrane ultrafiltration, Biotechnol Bioeng, 83, 201, 10.1002/bit.10659 · DOI
  38. Muller, 1999, Ultrafiltration modes of operation for the separation of α-lactalbumin from acid casein whey, J Membr Sci, 153, 9, 10.1016/S0376-7388(98)00218-X · DOI
  39. Cheison, 2011, Influence of hydrolysis temperature and pH on the selective hydrolysis of whey proteins by trypsin and potential recovery of native alpha-lactalbumin, Int Dairy J, 21, 166, 10.1016/j.idairyj.2010.09.008 · DOI
  40. Konrad, 2008, A new method for isolation of native α-lactalbumin from sweet whey, Int Dairy J, 18, 47, 10.1016/j.idairyj.2007.06.004 · DOI
  41. Lisak, 2013, Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native α-lactalbumin purification, J Dairy Res., 80, 14, 10.1017/S0022029912000416 · DOI
  42. Geng, 2015, Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration, Dairy Sci & Technol., 95, 353, 10.1007/s13594-015-0215-8 · DOI
  43. Neyestani, 2003, Isolation of α-lactalbumin, β-lactoglobulin, and bovine serum albumin from cow’s milk using gel filtration and anion-exchange chromatography including evaluation of their antigenicity, Protein Expr Purif., 29, 202, 10.1016/S1046-5928(03)00015-9 · DOI
  44. Ye, 2000, Isolation of lactoperoxidase, lactoferrin, α-lactalbumin, β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography, Int J Biochem Cell Biol., 32, 1143, 10.1016/S1357-2725(00)00063-7 · DOI
  45. Mao, 2017, One-step method for the isolation of α-lactalbumin and β-lactoglobulin from cow’s milk while preserving their antigenicity, Int J Food Prop, 20, 792, 10.1080/10942912.2016.1181649 · DOI
  46. Conrado, 2005, Concentration of alpha-lactalbumin from cow milk whey through expanded bed adsorption using a hydrophobic resin, Braz J Chem Eng., 22, 501, 10.1590/S0104-66322005000400002 · DOI
  47. Touhami, 2021, Coupling high hydrostatic pressure and ultrafiltration for fractionation of alpha-lactalbumin from skim milk, Sep Sci Technol, 56, 1102, 10.1080/01496395.2020.1749079 · DOI
  48. Liang, 2011, Simultaneous isolation of lactoferrin and lactoperoxidase from bovine colostrum by SPEC 70 SLS cation exchange resin, Int J Environ Res Public Health., 8, 3764, 10.3390/ijerph8093764 · DOI
  49. Lu, 2007, Isolation of lactoferrin from bovine colostrum by ultrafiltration coupled with strong cation exchange chromatography on a production scale, J Membr Sci, 297, 152, 10.1016/j.memsci.2007.03.039 · DOI
  50. Hirsch, 2020, Lactoferrin purification and whey protein isolate recovery from cheese whey using chitosan mini-spheres, Int Dairy J, 109, 104764, 10.1016/j.idairyj.2020.104764 · DOI
  51. Matijašić, 2020, Characterisation of lactoferrin isolated from acid whey using pilot-scale monolithic ion-exchange chromatography, Processes, 8, 804, 10.3390/pr8070804 · DOI
  52. Teepakorn, 2015, Optimization of lactoferrin and bovine serum albumin separation using ion-exchange membrane chromatography, Sep Purif Technol, 151, 292, 10.1016/j.seppur.2015.07.046 · DOI
  53. Brisson, 2007, Electrically-enhanced crossflow microfiltration for separation of lactoferrin from whey protein mixtures, J Membr Sci, 297, 206, 10.1016/j.memsci.2007.03.046 · DOI
  54. Ndiaye, 2010, Electroseparation of bovine lactoferrin from model and whey solutions, Sep Purif Technol, 74, 93, 10.1016/j.seppur.2010.05.011 · DOI
  55. Wang, 2020, Isolation of lactoferrin and immunoglobulins from dairy whey by an electrodialysis with filtration membrane process, Sep Purif Technol, 233, 115987, 10.1016/j.seppur.2019.115987 · DOI
  56. Baieli, 2014, Isolation of lactoferrin from whey by dye-affinity chromatography with yellow HE-4R attached to chitosan mini-spheres, Int Dairy J, 39, 53, 10.1016/j.idairyj.2014.03.014 · DOI
  57. Chen, 2007, Isolation of lactoferrin from acid whey by magnetic affinity separation, Sep Purif Technol, 56, 168, 10.1016/j.seppur.2007.01.019 · DOI
  58. Lönnerdal, 1977, Isolation of lactoferrin from human milk by metal-chelate affinity chromatography, FEBS Lett., 75, 89, 10.1016/0014-5793(77)80059-8 · DOI
  59. Santos, 2011, Fractionation and recovery of whey proteins by hydrophobic interaction chromatography, J Chromatogr B Analyt Technol Biomed Life Sci., 879, 475, 10.1016/j.jchromb.2011.01.003 · DOI
  60. Maciel, 2020, Purification of lactoferrin from sweet whey using ultrafiltration followed by expanded bed chromatography, Sep Purif Technol, 251, 117324, 10.1016/j.seppur.2020.117324 · DOI
  61. Nakano, 2018, Separation of bovine κ-casein glycomacropeptide from sweet whey protein products with undetectable level of phenylalanine by protein precipitation followed by anion exchange chromatography, J Dairy Res., 85, 110, 10.1017/S0022029917000838 · DOI
  62. Nakano, 2020, Isolation of κ-casein glycomacropeptide from bovine whey fraction using food grade anion exchange resin and chitin as an adsorbent, J Dairy Res, 87, 127, 10.1017/S0022029919000918 · DOI
  63. Nakano, 2002, Purification of κ-casien glycomacropeptide from sweet whey with undetectable level of phenylalanine, Biotechnol Prog., 18, 409, 10.1021/bp010195u · DOI
  64. Baieli, 2017, Affinity chromatography matrices for depletion and purification of casein glycomacropeptide from bovine whey, Biotechnol Prog., 33, 171, 10.1002/btpr.2404 · DOI
  65. Silva-Hernandez, 2002, Isolation and analysis of κ-casein glycomacropeptide from goat sweet whey, J Agric Food Chem., 50, 2034, 10.1021/jf010732q · DOI
  66. Rojas, 2013, Isolation and recovery of glycomacropeptide from milk whey by means of thermal treatment, Food Sci Technol., 33, 14, 10.1590/S0101-20612013005000027 · DOI
  67. Nakano, 2009, Cellulose acetate electrophoresis of whey proteins and glycomacropeptide, Milchwissenschaft, 64, 291
  68. Hansen, 2020, Microfiltration of raw milk for production of high-purity milk fat globule membrane material, J Food Eng, 276, 109887, 10.1016/j.jfoodeng.2019.109887 · DOI
  69. Le, 2009, Effect of washing conditions on the recovery of milk fat globule membrane proteins during the isolation of milk fat globule membrane from milk, J Dairy Sci., 92, 3592, 10.3168/jds.2008-2009 · DOI
  70. Ye, 2004, Interactions of whey proteins with milk fat globule membrane proteins during heat treatment of whole milk, Lait., 84, 269, 10.1051/lait:2004004 · DOI
  71. Fuller, 2013, Milk fat globule membrane isolated from buttermilk or whey cream and their lipid components inhibit infectivity of rotavirus in vitro, J Dairy Sci., 96, 3488, 10.3168/jds.2012-6122 · DOI
  72. Morin, 2007, Microfiltration of buttermilk and washed cream buttermilk for concentration of milk fat globule membrane components, J Dairy Sci., 90, 2132, 10.3168/jds.2006-832 · DOI
  73. Rombaut, 2006, Microfiltration of butter serum upon casein micelle destabilization, J Dairy Sci., 89, 1915, 10.3168/jds.S0022-0302(06)72259-7 · DOI
  74. Rombaut, 2007, Filtration of milk fat globule membrane fragments from acid buttermilk cheese whey, J Dairy Sci., 90, 1662, 10.3168/jds.2006-587 · DOI
  75. Holzmüller, 2016, Casein precipitation by acid and rennet coagulation of buttermilk: impact of pH and temperature on the isolation of milk fat globule membrane proteins, Int Dairy J, 63, 115, 10.1016/j.idairyj.2016.08.006 · DOI
  76. Robinson, 2018, An improved method for the purification of milk oligosaccharides by graphitised carbon-solid phase extraction, Int Dairy J., 80, 62, 10.1016/j.idairyj.2017.12.009 · DOI
  77. Ward, 2009, Isolation of milk oligosaccharides using solid-phase extraction, Open Glycosci., 2, 9, 10.2174/1875398100902010009 · DOI
  78. Altmann, 2015, Comparison of the efficiency of different NF membranes for the enrichment of milk oligosaccharides from bovine milk, Eur Food Res Technol., 241, 803, 10.1007/s00217-015-2505-z · DOI
  79. Cohen, 2017, Role of pH in the recovery of bovine milk oligosaccharides from colostrum whey permeate by nanofiltration, Int Dairy J., 66, 68, 10.1016/j.idairyj.2016.10.016 · DOI
  80. de Moura Bell, 2018, An integrated bioprocess to recover bovine milk oligosaccharides from colostrum whey permeate, J Food Eng., 216, 27, 10.1016/j.jfoodeng.2017.07.022 · DOI
  81. Lin, 2019, Manipulation of the dry bean (Phaseolus vulgaris L.) matrix by hydrothermal and high-pressure treatments: impact on in vitro bile salt-binding ability, Food Chem, 310, 125699, 10.1016/j.foodchem.2019.125699 · DOI
  82. Zou, 2016, Comparison of high hydrostatic pressure, high-pressure carbon dioxide and high-temperature short-time processing on quality of mulberry juice, Food Bioprocess Technol., 9, 217, 10.1007/s11947-015-1606-9 · DOI
  83. Lin, 2020, Retention of primary bile salts by dry beans (Phaseolus vulgaris L.) during in vitro digestion: role of bean components and effect of food processing, Food Res Int., 137, 109337, 10.1016/j.foodres.2020.109337 · DOI
  84. Lin, 2020, Effect of thermal and high-pressure processing on the thermo-rheological and functional properties of common bean (Phaseolus vulgaris L.) flours, LWT, 127, 109325, 10.1016/j.lwt.2020.109325 · DOI
  85. Xu, 2015, Quality assurance in pepper and orange juice blend treated by high pressure processing and high temperature short time, Innov Food Sci Emerg Technol, 31, 28, 10.1016/j.ifset.2015.08.001 · DOI
  86. Wang, 2014, Effects of anti-browning combinations of ascorbic acid, citric acid, nitrogen and carbon dioxide on the quality of banana smoothies, Food Bioprocess Technol., 7, 161, 10.1007/s11947-013-1107-7 · DOI
  87. Tomita, 2002, Bovine lactoferrin and lactoferricin derived from milk: production and applications, Biochem Cell Biol., 10.1139/o01-230 · DOI
  88. Almécija, 2006, Influence of pH in the recovery of lactoferrin from whey with ceramic membranes, Desalination, 200, 475, 10.1016/j.desal.2006.03.401 · DOI
  89. Nyström, 1998, Fractionation of model proteins using their physiochemical properties, Colloids Surf Physicochem Eng Asp, 138, 185, 10.1016/S0927-7757(96)03892-7 · DOI
  90. Tanimoto, 1992, Large-scale preparation of κ-casein glycomacropeptide from rennet casein whey, Biosci Biotechnol Biochem, 56, 140, 10.1271/bbb.56.140 · DOI
  91. Morin, 2007, Effect of processing on the composition and microstructure of buttermilk and its milk fat globule membranes, Int Dairy J, 17, 1179, 10.1016/j.idairyj.2007.03.010 · DOI
  92. Corredig, 2003, Production of a novel ingredient from buttermilk, J Dairy Sci., 86, 2744, 10.3168/jds.S0022-0302(03)73870-3 · DOI
  93. Holzmüller, 2016, Technical difficulties and future challenges in isolating membrane material from milk fat globules in industrial settings – a critical review, Int Dairy J, 61, 51, 10.1016/j.idairyj.2016.03.013 · DOI
  94. Verardo, 2017, Recent advances in phospholipids from colostrum, milk and dairy by-products, Int J Mol Sci., 18, 173, 10.3390/ijms18010173 · DOI
  95. Boyd, 1999, Isolation and characterization of whey phospholipids, J Dairy Sci., 82, 2550, 10.3168/jds.S0022-0302(99)75509-8 · DOI
  96. Costa, 2010, Use of ultrafiltration and supercritical fluid extraction to obtain a whey buttermilk powder enriched in milk fat globule membrane phospholipids, Int Dairy J, 20, 598, 10.1016/j.idairyj.2010.03.006 · DOI
  97. Catchpole, 2008, Extraction of lipids from a specialist dairy stream, J Supercrit Fluids, 45, 314, 10.1016/j.supflu.2008.01.004 · DOI
  98. Sarney, 2000, A novel approach to the recovery of biologically active oligosaccharides from milk using a combination of enzymatic treatment and nanofiltration, Biotechnol Bioeng., 69, 461, 10.1002/1097-0290(20000820)69:4<461::AID-BIT13>3.0.CO;2-L · DOI
  99. Nongonierma, 2015, Milk proteins as a source of tryptophan-containing bioactive peptides, Food Funct., 6, 2115, 10.1039/C5FO00407A · DOI · Paper page
  100. Atehli, 2020, Effects of mono- and diglycerides of fatty acids on the milk fat globule membrane after heat treatment, Int J Dairy Technol., 73, 667, 10.1111/1471-0307.12712 · DOI
  101. Hayashi, 1980, Racemization of amino acid residues during alkali-treatment of protein and its adverse effect on pepsin digestibility, Agric Biol Chem, 44, 891
  102. Wang, 2020, Interaction effect of LED color temperatures and light-protective additive packaging on photo-oxidation in milk displayed in retail dairy case, Food Chem., 323, 126699, 10.1016/j.foodchem.2020.126699 · DOI
  103. Bouzas, 1985, Storage stability of milkfat globule membrane, J Food Processing Preservation., 9, 11, 10.1111/j.1745-4549.1985.tb00704.x · DOI
  104. Wijayanti, 2014, Stability of whey proteins during thermal processing: a review, Comprehen Rev Food Sci Food Saf., 13, 1235, 10.1111/1541-4337.12105 · DOI · Paper page
  105. Bokkhim, 2016, In-vitro digestion of different forms of bovine lactoferrin encapsulated in alginate micro-gel particles, Food Hydrocoll, 52, 231, 10.1016/j.foodhyd.2015.07.007 · DOI
  106. Gong, 2020, Ultrasonic encapsulation of cinnamon flavor to impart heat stability for baking applications, Food Hydrocoll, 99, 105316, 10.1016/j.foodhyd.2019.105316 · DOI
  107. Zhang, 2021, Improvement of the storage stability of C-phycocyanin in beverages by high-pressure processing, Food Hydrocoll, 110, 106055, 10.1016/j.foodhyd.2020.106055 · DOI
  108. Tan, 2019, A simple route to renewable high internal phase emulsions (HIPEs) strengthened by successive cross-linking and electrostatics of polysaccharides, Chem Commun (Camb)., 55, 1225, 10.1039/C8CC09683J · DOI
  109. Yan, 2021, Improvement of vitamin C stability in vitamin gummies by encapsulation in casein gel, Food Hydrocoll, 113, 106414, 10.1016/j.foodhyd.2020.106414 · DOI
  110. Lee, 2019, Combination of internal structuring and external coating in an oleogel-based delivery system for fish oil stabilization, Food Chem., 277, 213, 10.1016/j.foodchem.2018.10.112 · DOI
  111. Jannasari, 2019, Microencapsulation of vitamin D using gelatin and cress seed mucilage: production, characterization and in vivo study, Int J Biol Macromol, 129, 972, 10.1016/j.ijbiomac.2019.02.096 · DOI
  112. Nazzaro, 2012, Microencapsulation in food science and biotechnology, Curr Opin Biotechnol., 23, 182, 10.1016/j.copbio.2011.10.001 · DOI · Paper page
  113. Tolve, 2016, Encapsulation of health-promoting ingredients: applications in foodstuffs, Int J Food Sci Nutr., 67, 888, 10.1080/09637486.2016.1205552 · DOI
  114. Ezhilarasi, 2013, Nanoencapsulation techniques for food bioactive components: a review, Food Bioprocess Technol., 6, 628, 10.1007/s11947-012-0944-0 · DOI · Paper page
  115. Ye, 2018, Microencapsulation of active ingredients in functional foods: from research stage to commercial food products, Trends Food Sci Technol, 78, 167, 10.1016/j.tifs.2018.05.025 · DOI · Paper page
  116. Wang, 2017, Preparation and study of digestion behavior of lactoferrin-sodium alginate complex coacervates, J Funct Foods, 37, 97, 10.1016/j.jff.2017.07.044 · DOI
  117. Zhang, 2010, Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by thermal pretreatment, Food Chem, 119, 1318, 10.1016/j.foodchem.2009.08.043 · DOI
  118. Balcão, 2013, Nanoencapsulation of bovine lactoferrin for food and biopharmaceutical applications, Food Hydrocoll, 32, 425, 10.1016/j.foodhyd.2013.02.004 · DOI
  119. Bastos, 2018, Formation and characterization of the complex coacervates obtained between lactoferrin and sodium alginate, Int J Biol Macromol., 120, 332, 10.1016/j.ijbiomac.2018.08.050 · DOI
  120. da S. Gulão, 2014, Complex coacervates obtained from lactoferrin and gum arabic: formation and characterization, Food Res Int, 65, 367, 10.1016/j.foodres.2014.08.024 · DOI
  121. Bengoechea, 2011, Formation and characterization of lactoferrin/pectin electrostatic complexes: impact of composition, pH and thermal treatment, Food Hydrocoll, 25, 1227, 10.1016/j.foodhyd.2010.11.010 · DOI
  122. Mendanha, 2009, Microencapsulation of casein hydrolysate by complex coacervation with SPI/pectin, Food Res Int, 42, 1099, 10.1016/j.foodres.2009.05.007 · DOI
  123. Liu, 2013, Stability during in vitro digestion of lactoferrin-loaded liposomes prepared from milk fat globule membrane-derived phospholipids, J Dairy Sci., 96, 2061, 10.3168/jds.2012-6072 · DOI
  124. Vergara, 2019, Encapsulation of lactoferrin into rapeseed phospholipids based liposomes: optimization and physicochemical characterization, J Food Eng, 262, 29, 10.1016/j.jfoodeng.2019.05.012 · DOI
  125. Mohan, 2016, Encapsulation of bioactive whey peptides in soy lecithin-derived nanoliposomes: influence of peptide molecular weight, Food Chem., 213, 143, 10.1016/j.foodchem.2016.06.075 · DOI
  126. Poshadri, 2010, Microencapsulation technology: a review, J Res Angrau, 38, 86
  127. Okuro, 2013, Technological challenges for spray chilling encapsulation of functional food ingredients, Food Technol Biotechnol, 51, 171
  128. Gouin, 2004, Microencapsulation: industrial appraisal of existing technologies and trends, Trends Food Sci Technol, 15, 330, 10.1016/j.tifs.2003.10.005 · DOI · Paper page
  129. Guignon, 2002, Fluid bed encapsulation of particles: principles and practice, Dry Technol, 20, 419, 10.1081/DRT-120002550 · DOI
  130. Ai, 2019, Preparation and characterization of hydroxyapatite macrobeads based on pneumatic extrusion dripping, Ceram Int, 45, 16399, 10.1016/j.ceramint.2019.05.168 · DOI
  131. Zasypkin, 2004, Glass encapsulation of flavours with chemically modified starch blends, J Microencapsul., 21, 385, 10.1080/02652040410001695924 · DOI
  132. Xiao, 2019, Encapsulation and sustained release properties of watermelon flavor and its characteristic aroma compounds from γ-cyclodextrin inclusion complexes, Food Hydrocoll, 97, 105202, 10.1016/j.foodhyd.2019.105202 · DOI
  133. Hong, 2002, Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment, Int Dairy J, 12, 345, 10.1016/S0958-6946(02)00030-4 · DOI
  134. McGuffey, 2005, Denaturation and aggregation of three α-lactalbumin preparations at neutral pH, J Agric Food Chem., 53, 3182, 10.1021/jf048863p · DOI
  135. Kilic, 2017, Formulation for oral delivery of lactoferrin based on bovine serum albumin and tannic acid multilayer microcapsules, Sci Rep., 7, 44159, 10.1038/srep44159 · DOI
  136. Anema, 2016, Phase separation and composition of coacervates of lactoferrin and caseins, Food Hydrocoll, 52, 670, 10.1016/j.foodhyd.2015.08.011 · DOI
  137. Niu, 2019, Protection of native lactoferrin under gastric conditions through complexation with pectin and chitosan, Food Hydrocoll, 93, 120, 10.1016/j.foodhyd.2019.02.020 · DOI
  138. Korhonen, 2007, Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum, Curr Pharm Des., 13, 829, 10.2174/138161207780363112 · DOI
  139. Graveland-Bikker, 2006, Unique milk protein based nanotubes: food and nanotechnology meet, Trends Food Sci Technol, 17, 196, 10.1016/j.tifs.2005.12.009 · DOI · Paper page
  140. Liu, 2021, α-Lactalbumin self-assembled nanoparticles with various morphologies, stiffnesses, and sizes as pickering stabilizers for oil-in-water emulsions and delivery of curcumin, J Agric Food Chem., 69, 2485, 10.1021/acs.jafc.0c06263 · DOI
  141. Geng, 2016, Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin, Int Dairy J, 52, 72, 10.1016/j.idairyj.2015.08.005 · DOI
  142. Sozer, 2009, Nanotechnology and its applications in the food sector, Trends Biotechnol., 27, 82, 10.1016/j.tibtech.2008.10.010 · DOI · Paper page
  143. Legrand, 2016, Overview of lactoferrin as a natural immune modulator, J Pediatr, 173, S10, 10.1016/j.jpeds.2016.02.071 · DOI · Paper page
  144. Tomita, 2009, Twenty-five years of research on bovine lactoferrin applications, Biochimie, 91, 52, 10.1016/j.biochi.2008.05.021 · DOI · Paper page
  145. Shin, 2011, Effects of a composition containing lactoferrin and lactoperoxidase on oral malodor and salivary bacteria: a randomized, double-blind, crossover, placebo-controlled clinical trial, Clin Oral Investig., 15, 485, 10.1007/s00784-010-0422-x · DOI
  146. Kaito, 2007, Effect of lactoferrin in patients with chronic hepatitis C: combination therapy with interferon and ribavirin, J Gastroenterol Hepatol., 22, 1894, 10.1111/j.1440-1746.2007.04858.x · DOI
  147. Wang, 2016, Bovine lactoferrampin, human lactoferricin, and lactoferrin 1-11 inhibit nuclear translocation of HIV integrase, Appl Biochem Biotechnol., 179, 1202, 10.1007/s12010-016-2059-y · DOI
  148. Serrano, 2020, Liposomal lactoferrin as potential preventative and cure for COVID-19, Int J Res Health Sci., 8, 08
  149. Song, 2018, Casein glycomacropeptide hydrolysates ameliorate hepatic insulin resistance of C57BL/6J mice challenged with high-fat diet, J Funct Foods, 45, 190, 10.1016/j.jff.2018.03.044 · DOI
  150. Zaki, 2016, The use of glycomacropeptide in dietary management of phenylketonuria, J Nutr Metab., 2016, 2453027, 10.1155/2016/2453027 · DOI
  151. Bergia, 2018, Effect of whey protein supplementation on body composition changes in women: a systematic review and meta-analysis, Nutr Rev., 76, 539, 10.1093/nutrit/nuy017 · DOI
  152. Morales, 2017, Synergistic effect of casein glycomacropeptide on sodium caseinate foaming properties, Colloids Surf B Biointerfaces., 159, 501, 10.1016/j.colsurfb.2017.08.017 · DOI
  153. Morales, 2016, Dynamics of gelation, textural and microstructural properties of gelatin gels in the presence of casein glycomacropeptide, Food Res Int, 84, 102, 10.1016/j.foodres.2016.03.024 · DOI
  154. Rosqvist, 2015, Potential role of milk fat globule membrane in modulating plasma lipoproteins, gene expression, and cholesterol metabolism in humans: a randomized study, Am J Clin Nutr., 102, 20, 10.3945/ajcn.115.107045 · DOI
  155. Bode, 2016, Overcoming the limited availability of human milk oligosaccharides: challenges and opportunities for research and application, Nutr Rev., 74, 635, 10.1093/nutrit/nuw025 · DOI
  156. Weinborn, 2020, Production of functional mimics of human milk oligosaccharides by enzymatic glycosylation of bovine milk oligosaccharides, Int Dairy J, 102, 104583, 10.1016/j.idairyj.2019.104583 · DOI
  157. 2005, Opinion of the Scientific Panel on dietetic products, nutrition and allergies [NDA] related to the safety and suitability for particular nutritional use by infants of formula based on whey protein partial hydrolysates with a protein content of at least 1.9 g protein/100 kcal, EFSA J, 3, 280, 10.2903/j.efsa.2005.280 · DOI
  158. 2012, Scientific Opinion on bovine lactoferrin, EFSA J, 10, 2811
  159. Taylor, 2004, Safety determination for the use of bovine milk-derived lactoferrin as a component of an antimicrobial beef carcass spray, Regul Toxicol Pharmacol., 39, 12, 10.1016/j.yrtph.2003.10.001 · DOI
  160. Koletzko, 2006, Standards for infant formula milk, BMJ., 332, 621, 10.1136/bmj.332.7542.621 · DOI
  161. Rudloff, 1997, Protein and nonprotein nitrogen components in human milk, bovine milk, and infant formula: quantitative and qualitative aspects in infant nutrition, J Pediatr Gastroenterol Nutr., 24, 328, 10.1097/00005176-199703000-00017 · DOI
  162. Räihä, 1995, Protein nutrition during infancy. An update, Pediatr Clin North Am., 42, 745, 10.1016/S0031-3955(16)39015-0 · DOI
  163. Koletzko, 2009, Lower protein in infant formula is associated with lower weight up to age 2 y: a randomized clinical trial, Am J Clin Nutr., 89, 1836, 10.3945/ajcn.2008.27091 · DOI · Paper page
  164. Chang, 2020, Lactoferrin as potential preventative and adjunct treatment for COVID-19, Int J Antimicrob Agents, 56, 106118, 10.1016/j.ijantimicag.2020.106118 · DOI

Cited by

Metadata

Authors
Lin, T., Meletharayil, G., Kapoor, R., & Abbaspourrad, A.
Affiliations
  • Department of Food Science, College of Agriculture and Life Sciences, Cornell University, Ithaca, New York, USA
  • Gopinathan Meletharayil and Rohit Kapoor are with the National Dairy Council, Rosemont, Illinois, USA
ORCID
Venue
Nutrition Reviews
Publisher
Oxford University Press (OUP)
Published
2021-12-01
Volume
79
Issue
Supplement_2
Pages
48-69
ISSN
  • 0029-6643
  • 1753-4887
DOI
10.1093/nutrit/nuab099
Cited by
114
References
1
Language
en
Licence
creativecommons.org/licenses/by-nc-nd/4.0/ (vor, 7 d)
Funders
National Dairy Council

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