浓缩乳蛋白的离子交换脱钙及其对酪蛋白胶束的影响
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摘要
研究了浓缩乳蛋白的离子脱钙技术,以及部分脱钙对截留液中酪蛋白存在形式及酪蛋白胶束水合率的影响。研究确定了离子交换树脂的平衡脱钙时间为2 h,并通过改变树脂添加量得到了0、5%.5%、10.5%、19.6%、29.6%、38.7%、49.9%、63.8%和83.6%系列脱钙程度的截留液。随着脱钙程度的增加,截留液超离心上清中游离酪蛋白的含量逐渐增加,而超离心沉淀的胶束酪蛋白减少,说明酪蛋白逐渐从酪蛋白胶束中游离出来。当脱钙程度为0~29.6%时,酪蛋白胶束的水合率从2.6 g/g(干基)增加到4.1 g/g(干基),而脱钙程度从29.6%进一步增加到83.6%时,酪蛋白胶束水合率则变小至3.3 g/g(干基)。浓缩乳蛋白的钙离子含量以及酪蛋白的存在状态决定了其在应用时的功能特性,研究对开发新型的浓缩乳蛋白配料具有重要的指导意义。
This study investigated the technology of ion exchange decalcification of milk protein concentrate( MPC),and also the effects of partial decalcification on casein micelle and its hydration property. A series of decalcified MPC retentates( decalcification ratios of 0,5. 5%,10. 5%,19. 6%,29. 6%,38. 7%,49. 9%,63. 8%,83. 6%) were produced after 2 hours of ion exchange with adding corresponding amounts of resins. Casein components dissociated from casein micelles regarding the increase of decalcified MPC retentates; the contents of micellar casein decreased,while the concentrations of dissociated casein in the supernantants increased. The hydration properties of casein micelles increased from 2. 6 g / g dry basis to 4. 1 g / g dry basis( 0-29. 6% decalcification),and then decreased to 3. 3 g / g dry basis( 29. 6%-83. 6% decalcification). The content of calcium ions and the state of casein micelles in MPCs may affect the functionalities of MPCs in application. This study offered the potential of new MPCs with different functionalities and also will broaden the applications of new MPCs into food industry.
This study investigated the technology of ion exchange decalcification of milk protein concentrate( MPC),and also the effects of partial decalcification on casein micelle and its hydration property. A series of decalcified MPC retentates( decalcification ratios of 0,5. 5%,10. 5%,19. 6%,29. 6%,38. 7%,49. 9%,63. 8%,83. 6%) were produced after 2 hours of ion exchange with adding corresponding amounts of resins. Casein components dissociated from casein micelles regarding the increase of decalcified MPC retentates; the contents of micellar casein decreased,while the concentrations of dissociated casein in the supernantants increased. The hydration properties of casein micelles increased from 2. 6 g / g dry basis to 4. 1 g / g dry basis( 0-29. 6% decalcification),and then decreased to 3. 3 g / g dry basis( 29. 6%-83. 6% decalcification). The content of calcium ions and the state of casein micelles in MPCs may affect the functionalities of MPCs in application. This study offered the potential of new MPCs with different functionalities and also will broaden the applications of new MPCs into food industry.
引文
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[11]POST A E,ARNOLD B,WEISS J,et al.Effect of temperature and p H on the solubility of caseins:environmental influences on the dissociation ofαS-andβ-casein[J].Journal of Dairy Science,2012,95(4):1 603-1 616.
[12]BEHERA P,KUMAR R,SANDEEP I V R,et al.Casein hydrolysates enhance osteoblast proliferation and differentiation in mouse bone marrow culture[J].Food Bioscience,2013,2:24-30.
[13]PREMLAL RANJITH H M,LEWIS M J,MAW D.Production of calcium-reduced milks using an ion-exchange resin[J].Journal of Dairy Research,1999,66(1):139
[14]VAN KREVELD A,VAN MINNENG.Calcium and magnesium ion activity in raw milk and processed milk[J].Nederlandsch Melk-en Zuiveltijdschrift,1955,9:1-29.
[15]SILVA N N,PIOT M,DE CARVALHOA F,et al.p Hinduced demineralization of casein micelles modifies their physico-chemical and foaming properties[J].Food Hydrocolloids,2013,32(2):322-330.
[16]MCMAHON D J,DU H,MCMANUSW R,et al.Microstructural changes in casein supramolecules during acidification of skim milk[J].Journal of Dairy Science,2009,92(12):5 854-5 867.
[17]MARCHIN S,PUTAUX J L,PIGNON F,et al.Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle x-ray scattering/ultrasmall-angle x-ray scattering[J].The Journal of Chemical Physics,2007,126(4):045101.
[18]NG-KWAI-HANG K F,OTTER D E,LOWEE,et al.Influence of genetic variants ofβ-lactoglobulin on milk composition and size of casein micelles[J].Milchwissenschaft,2002,57(6):303-306.
[19]WALSTRA P.On the stability of casein micelles[J].Journal of Dairy Science,1990,73(8):1 965-1 979.
[2]HAVEA P.Protein interactions in milk protein concentrate powders[J].International Dairy Journal,2006,16(5):415-422.
[3]FRANCOLINO S,LOCCI F,GHIGLIETTI R,et al.Use of milk protein concentrate to standardize milk composition in Italian citric Mozzarella cheese making[J].LWT-Food Science and Technology,2010,43(2):310-314.
[4]FARKYE N Y,YIM B.Use of dry milk protein concentrate in pizza cheese manufactured by culture or direct acidification[J].Journal of Dairy Science,2003,86(12):3 841-3 848.
[5]MIMOUNI A,DEETH H C,WHITTAKER A K,et al.Rehydration process of milk protein concentrate powder monitored by static light scattering[J].Food Hydrocolloids,2009,23(7):1 958-1 965.
[6]UDABAGE P,PUVANENTHIRAN A,YOO J A,et al.Modified water solubility of milk protein concentrate powders through the application of static high pressure treatment[J].Journal of Dairy Research,2012,79(1):76-83.
[7]MIMOUNI A,DEETH H C,WHITTAKER A K,et al.Investigation of the microstructure of milk protein concentrate powders during rehydration:alterations during storage[J].Journal of Dairy Science,2010,93(2):463-472.
[8]HUNTER R J,HEMAR Y,PINDER D N,et al.Effect of storage time and temperature of milk protein concentrate(MPC85)on the renneting properties of skim milk fortified with MPC85[J].Food Chemistry,2011,125(3):944-952.
[9]MAO X Y,TONG P S,GUALCO S,et al.Effect of Na Cl addition during diafiltration on the solubility,hydrophobicity,and disulfide bonds of 80%milk protein concentrate powder[J].Journal of Dairy Science,2012,95(7):3 481-3 488.
[10]SIKAND V,TONG P S,ROY S,et al.Solubility of commercial milk protein concentrates and milk protein isolates[J].Journal of Dairy Science,2011,94(12):6 194-6 202.
[11]POST A E,ARNOLD B,WEISS J,et al.Effect of temperature and p H on the solubility of caseins:environmental influences on the dissociation ofαS-andβ-casein[J].Journal of Dairy Science,2012,95(4):1 603-1 616.
[12]BEHERA P,KUMAR R,SANDEEP I V R,et al.Casein hydrolysates enhance osteoblast proliferation and differentiation in mouse bone marrow culture[J].Food Bioscience,2013,2:24-30.
[13]PREMLAL RANJITH H M,LEWIS M J,MAW D.Production of calcium-reduced milks using an ion-exchange resin[J].Journal of Dairy Research,1999,66(1):139
[14]VAN KREVELD A,VAN MINNENG.Calcium and magnesium ion activity in raw milk and processed milk[J].Nederlandsch Melk-en Zuiveltijdschrift,1955,9:1-29.
[15]SILVA N N,PIOT M,DE CARVALHOA F,et al.p Hinduced demineralization of casein micelles modifies their physico-chemical and foaming properties[J].Food Hydrocolloids,2013,32(2):322-330.
[16]MCMAHON D J,DU H,MCMANUSW R,et al.Microstructural changes in casein supramolecules during acidification of skim milk[J].Journal of Dairy Science,2009,92(12):5 854-5 867.
[17]MARCHIN S,PUTAUX J L,PIGNON F,et al.Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle x-ray scattering/ultrasmall-angle x-ray scattering[J].The Journal of Chemical Physics,2007,126(4):045101.
[18]NG-KWAI-HANG K F,OTTER D E,LOWEE,et al.Influence of genetic variants ofβ-lactoglobulin on milk composition and size of casein micelles[J].Milchwissenschaft,2002,57(6):303-306.
[19]WALSTRA P.On the stability of casein micelles[J].Journal of Dairy Science,1990,73(8):1 965-1 979.