Isolation and purification of lactoferrin and immunoglobulin G from bovine colostrum with serial cation-anion exchange chromatography

作者: Mian-bin Wu , Yin-jun Xu

DOI: 10.1007/S12257-008-0159-4

关键词: ChromatographyColostrumCentrifugationChemistryLactoferrinIon chromatographySodiumIon exchangeElutionImmunoglobulin G

摘要: High-value dairy proteins such as lactoferrin (LF) and immunoglobulin (IgG) were separated from bovine colostrum. The whey was initially adjusted to pH 6.8 with 1 mol/L NaOH then went through centrifugation, precipitation, filtration eliminate the fat caseins in treated further ultra-filtrated partially remove both other carbohydrates under 50 kD molecular weight. Then passed cation anion exchange columns series. LF IgG adsorbed on exchanger, respectively, due their different pI. Both washed de-ionized water followed by successive elution sodium chloride solutions of increasing molarities (0.27 0.85 mol/L; 17 51 mmol/L) a stepwise manner, respectively. After desalted, freeze-dried. Finally, respective purities 95.0% 96.6% obtained.

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