This study used a selective precipitation method to isolate κ-and β-casein with a ratio similar to human caseins from goat micellar casein concentrates (MCC), and then also tried scale-up production.Optimization of process parameters for critical steps including redissolution, casein-calcium complexation, αs-casein precipitation and low-temperature equilibration resulted in κ-and β-casein with high recovery and purity.At laboratory scale, the yields for κ- and β-caseins reached 85.7% and 97.3%, with purities being 18.0% and 68.7%, respectively.In scale-up production with 60 L MCC solution, κ- and β-caseins yields reached 76.4% and 88.7%, with purities of 18.0% and 67.6%, respectively.Washing the precipitate one or more times reduced ash content to be less than 5%.This method brings the proportion of goat caseins closer to that of human caseins, thereby enhancing the application value of MCC in fields such as infant.
MIAO Guangyong
,
TAO Xiumei
,
PENG Xiaoyu
,
GAO Yu
,
WANG Shanshan
,
WU Tong
,
LIU Dasong
,
ZHOU Peng
. Separation, preparation, and scale-up production of goat κ- and β-casein ingredients[J]. Food and Fermentation Industries, 2025
, 51(22)
: 79
-88
.
DOI: 10.13995/j.cnki.11-1802/ts.042471
[1] NEHIR EL S, KARAKAYA S, SIMSEK S, et al.In vitro digestibility of goat milk and kefir with a new standardised static digestion method (INFOGEST cost action) and bioactivities of the resultant peptides[J].Food & Function, 2015, 6(7):2322-2330.
[2] MAATHUIS A, HAVENAAR R, HE T, et al.Protein digestion and quality of goat and cow milk infant formula and human milk under simulated infant conditions[J].Journal of Pediatric Gastroenterology and Nutrition, 2017, 65(6):661-666.
[3] 张静, 洪欣慧紫, 陶秀梅, 等.羊乳酪蛋白κ和β亚组分的共富集及婴幼儿体外消化性研究[J].食品与发酵工业, 2025, 51(4):75-82.
ZHANG J, HONG X H Z, TAO X M, et al.Study on co-enrichment of caprine casein κ and β subfractions and in vitro digestibility of infants[J].Food and Fermentation Industries, 2025, 51(4):75-82.
[4] ZHANG J P, DU X Y, JIANG S L, et al.Formulation of infant formula with different casein fractions and their effects on physical properties and digestion characteristics[J].Food & Function, 2022, 13(2):769-780.
[5] SCHUBERT T, ERGIN I, PANETTA F, et al.Application of a temperature-controlled decanter centrifuge for the fractionation of αs-, β- and κ-casein on pilot scale[J].International Dairy Journal, 2021, 122:105148.
[6] POST A, EBERT M, HINRICHS J.β-casein as a bioactive precursor-processing for purification[J].Australian Journal of Dairy Technology, 2009, 64(1):84-88.
[7] ATAMER Z, POST A E, SCHUBERT T, et al.Bovine β-casein:Isolation, properties and functionality.A review[J].International Dairy Journal, 2017, 66:115-125.
[8] MARKOSKA T, DANILOSKI D, VASILJEVIC T, et al.Structural changes of β-casein induced by temperature and pH analysed by nuclear magnetic resonance, Fourier-transform infrared spectroscopy, and chemometrics[J].Molecules, 2021, 26(24):7650.
[9] 罗桂心. 山羊乳酪蛋白组分的分离及消化性研究[D].无锡:江南大学, 2023.
LUO G X.Study on fractionation and digestibility of caprine casein fractions[D].Wuxi:Jiangnan University, 2023.
[10] RENZONE G, ARENA S, SCALONI A.Cross-linking reactions in food proteins and proteomic approaches for their detection[J].Mass Spectrometry Reviews, 2022, 41(5):861-898.
[11] LIU X C, JIANG Y, AHRNÉ L M, et al.Temperature effects on calcium binding to caseins[J].Food Research International, 2022, 154:110981.
[12] POST A E, ARNOLD B, WEISS J, et al.Effect of temperature and pH on the solubility of caseins:Environmental influences on the dissociation of αS- and β-casein[J].Journal of Dairy Science, 2012, 95(4):1603-1616.
[13] MEKMENE O, GAUCHERON F.Determination of calcium-binding constants of caseins, phosphoserine, citrate and pyrophosphate:A modelling approach using free calcium measurement[J].Food Chemistry, 2011, 127(2):676-682.
[14] KERN L, FABRE O, SCHER J, et al.Chemical fractionation of caseins by differential precipitation:Influence of pH, calcium addition, protein concentration and temperature on the depletion in α- and β-caseins[J].International Journal of Food Science & Technology, 2020, 55(2):542-552.
[15] MELNYCHYN P, WOLCOTT J M.Simple procedure for isolation of alphas-casein[J].Journal of Dairy Science, 1967, 50(12):1863-1867.
[16] THEKKILAVEEDU S, KRISHNASWAMI V, MOHANAN D P, et al.Lactic acid‐mediated isolation of alpha-, beta- and kappa-casein fractions by isoelectric precipitation coupled with cold extraction from defatted cow milk[J].International Journal of Dairy Technology, 2020, 73(1):31-39.
[17] DOWNEY W K, MURPHY R F.The temperature-dependent dissociation of β-casein from bovine casein micelles and complexes[J].Journal of Dairy Research, 1970, 37(3):361-372.
[18] POST A E, HINRICHS J.Suitability of commercial caseinates in comparison to micellar casein as raw material for isolation of food-grade β-casein[J].Milchwissenschaft, 2010, 65(2):195-198.
[19] SCHIFFER S, SCHEIDLER E, KIEFER T, et al.Effect of temperature, added calcium and pH on the equilibrium of caseins between micellar state and milk serum[J].Foods, 2021, 10(4):822.
[20] THIENEL K J F, HOLDER A, SCHUBERT T, et al.Fractionation of milk proteins on pilot scale with particular focus on β-casein[J].International Dairy Journal, 2018, 79:73-77.
[21] ANEMA S G, KLOSTERMEYER H.ζ-Potentials of casein micelles from reconstituted skim milk heated at 120 ℃[J].International Dairy Journal, 1996, 6(7):673-687.
[22] POST A E, HINRICHS J.Large-scale isolation of food-grade β-casein[J].Milchwissenschaft, 2011, 66(4):361-364.