Skip to main content

Advertisement

SpringerLink
Log in

Isolation of β-lactoglobulin from buffalo milk and characterization of its structure changes as a function of pH and ionic strength

  • Original Paper
  • Published:
Journal of Food Measurement and Characterization Aims and scope Submit manuscript

Abstract

β-lactoglobulin (β-lg) is one of the most widely used proteins in food industry. Purification of β-lg from buffalo milk while maintaining its native structure is of practical influence to the industry. This research demonstrated that β-lg can be separated efficiently from whey using 70 g kg− 1 NaCl at pH 2.0, which showed higher yield and activity of β-lg. It was found that the presence of NaCl or the changing of pH had no influence on the secondary structure of β-lg while they significant influenced the tertiary structure of β-lg. More hydrophobic groups were exposed with increasing NaCl concentration. Presence of low concentration of NaCl inhibited the exposure of Trp while the exposure of Trp was increased in the presence of high concentration of NaCl. In contrast, pH changes did not influence the exposure of Trp while the decrease of pH in the range of 7.5–5.5 decreased the exposure of hydrophobic groups to the hydrophilic environment.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  1. C. Morr, Functionality of heated milk proteins in dairy and related foods. J. Dairy Sci. 68, 2773–2781 (1985)

    Article  CAS  Google Scholar 

  2. H. Lindmark-Månsson, A. Timgren, G. Aldén, M. Paulsson, Two-dimensional gel electrophoresis of proteins and peptides in bovine milk. Int. Dairy J. 15, 111–121 (2005)

    Article  Google Scholar 

  3. J. Mounsey, B. O’Kennedy, M.A. Fenelon, A. Brodkorb, The effect of heating on β-lactoglobulin–chitosan mixtures as influenced by pH and ionic strength. Food Hydrocoll. 22, 65–73 (2008)

    Article  CAS  Google Scholar 

  4. P. Mailliart, B. Ribadeau-dumas, Proteins from whey retentate by NaCl salting out at low pH. J. Food Sci. 53, 743–746 (1998)

    Article  Google Scholar 

  5. K.K. Fox, V.H. Holsinger, L.P. Posati, M.J. Pallansch, Separation of β-lactoglobulin from other milk serum proteins by trichloroacetic acid. J. Dairy Sci. 50, 1363–1367 (1967)

    Article  CAS  Google Scholar 

  6. S. Bhattacharjee, C. Bhattacharjee, S. Datta, Studies on the fractionation of β-lactoglobulin from casein whey using ultrafiltration and ion-exchange membrane chromatography. J. Memb. Sci. 275, 141–150 (2006)

    Article  CAS  Google Scholar 

  7. M. Santos, J. Teixeira, L. Rodrigues, Fractionation of the major whey proteins and isolation of β-Lactoglobulin variants by anion exchange chromatography. Sep. Purif. Technol. 90, 133–139 (2012)

    Article  CAS  Google Scholar 

  8. X. Li, Z. Luo, H. Chen, Y. Cao, Isolation and antigenicity evaluation of β-lactoglobulin form buffalo milk. J. Biotechnol. 136, 2258–2264 (2008)

    Google Scholar 

  9. F. Guyomarc’h, A. Law, D.G. Dalgleish, Formation of soluble and micelle-bound protein aggregates in heated milk. J. Agric. Food Chem. 51, 4652–4660 (2003)

    Article  Google Scholar 

  10. L. Donate, F. Guyomarc’h, Formation and properties of the whey protein/κ-casein complexes in heated skim milk—a review. Dairy Sci. Technol. 89, 3–29 (2009)

    Article  Google Scholar 

  11. S.G. Anema, S.K. Lee, H. Klostermeyer, Rennet-induced aggregation of heated pH-adjusted skim milk. J. Agric. Food Chem. 59, 8413–8422 (2011)

    Article  CAS  Google Scholar 

  12. I. Ayala-Hernández, A. Hassan, H.D. Goff, M. Corredig, Effect of protein supplementation on the rheological characteristics of milk permeates fermented with exopolysaccharide-producing Lactococcus lactis subsp. cremoris. Food Hydrocoll. 23, 1299–1304 (2009)

    Article  Google Scholar 

  13. A. Bals, U. Kulozik, Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus. Int. Dairy J. 13, 903–908 (2003)

    Article  CAS  Google Scholar 

  14. H. Kim, E.A. Decker, D.J. Mcclements, Influence of protein concentration and order of addition on thermal stability of beta-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH. Langmuir 3, 134–139 (2011)

    Google Scholar 

  15. A.M. Chuah, T. Kuroiwa, I. Kobayashi, M. Nakajima, The influence of polysaccharide on the stability of protein stabilized oil-in-water emulsion prepared by microchannel emulsification technique. Colloids Surf. A. 440, 136–144 (2014)

    Article  CAS  Google Scholar 

  16. J.M. Brun, D.G. Dalgleish, Some effects of heat on the competitive adsorption of caseins and whey proteins in oil-in-water emulsions. Int. Dairy J. 99, 323–327 (1999)

    Article  Google Scholar 

  17. D.G. Dalgleish, H.D. Goff, J.M. Brun, B. Luan, Exchange reactions between whey proteins and caseins in heated soya oil-in-water emulsion systems-overall aspects of the reaction. Food Hydrocoll 16, 303–311 (2002)

    Article  CAS  Google Scholar 

  18. J. Leman, T. Doga, Effect of temperature and high pressure on foaming properties of beta-lactoglobulin salted out at pH 2. Commun Agric Appl Biol Sci 68, 489–492 (2003)

    CAS  Google Scholar 

  19. H.M. Zhu, S. Damodaran, Heat-Induced Conformational-Changes in Whey Protein Isolate and Its Relation to Foaming Properties. J. Agr. Food. Chem 42, 846–855 (1994)

    Article  CAS  Google Scholar 

  20. V. Raikos, Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocoll 24, 259–265 (2010)

    Article  CAS  Google Scholar 

  21. PWJR Caessens, S. Visser, H. Gruppen, Method for the isolation of bovine β-lactoglobulin from a cheese whey protein fraction and physicochemical characterization of the purified product. Int. Dairy J 7, 229–235 (1997)

    Article  CAS  Google Scholar 

  22. U.K. Lammli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685 (1970)

    Article  Google Scholar 

  23. Fox PF, Advanced dairy chemistry proteins part A, 3rd ed. McSweeney P, Fox P. (springer, Editors. New York, 2003)

  24. F.Y. Jr, M. Zhang, J. Chen, Y. Liang, Structural changes of α-lactalbumin induced by low pH and oleic acid. Biochim. Biophys. Acta 1764, 1389–1396 (2006)

    Article  Google Scholar 

  25. G. Râpeanu, G. Bahrim, I. Aprodu, pH and heat-induced structural changes of bovine apo-a-lactalbumin. Food Chem 131, 956–963 (2012)

    Article  Google Scholar 

  26. G. Braunitzer, J. Liberatori, H. Liberatori, The primary structure of the β-Lactoglobulin of the waterbuffalo (Bubalus arnee), Z. Naturforsch C. 34, 880–881 (1979)

    Article  CAS  Google Scholar 

  27. HHJ de Jongh, T. Gröneveld, J. de Groot, Mild isolation procedure discloses new protein structural properties of β-lactoglobulin. J. Dairy Sci. 84, 562–571 (2001)

    Article  Google Scholar 

  28. J. Chandrapala, B. Zisu, M. Palmer, S. Kentish, M. Ashokkumar, Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrason. Sonochem. 18, 951–957 (2011)

    Article  CAS  Google Scholar 

  29. J.E. Matsuura, M.C. Manning, Heat-induced gel formation of beta-lactoglobulin: a study on the secondary and tertiary structure as followed by circular dichroism spectroscopy. J. Agric. Food Chem. 42, 1650–1656 (1994)

    Article  CAS  Google Scholar 

  30. D. Renard, J. Lefebvre, Effects of pH and salt environment on the association of beta-lactoglobulin revealed by intrinsic fluorescence studies. Int. J. Biol. Macromol. 22, 41–49 (1998)

    Article  CAS  Google Scholar 

  31. J. Godovac-Zimmermann, G. Braunitzer, Modern aspects of the primary structure and function of β-lactoglobulins. Milchwissenschaft 42, 294–297 (1987)

    CAS  Google Scholar 

  32. N. Taulier, T.V. Chalikian, Characterization of pH-induced transitions of beta-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies. J. Mol. Biol 314, 873–889 (2001)

    Article  CAS  Google Scholar 

  33. C. Bhattacharjee, K.P. Das, Thermal unfolding and refolding of β-lactoglobulin. Eur. J. Biochem 267, 3957–3964 (2000)

    Article  CAS  Google Scholar 

  34. J.R. Albani, J. Vogelaer, L. Bretesche, D. Kmiecik, Tryptophan 19 residue is the origin of bovine β-lactoglobulin fluorescence. J. Pharm. Biomed. Anal 91, 144–150 (2014)

    Article  CAS  Google Scholar 

Download references

Acknowledgements

The authors gratefully acknowledge financial support from the Open Foundation of State Key Laboratory of Dairy Biotechnology, P. R. China and financially supported by Guangxi University Science Foundation for Doctor (XBZ160258).

Author information

Authors and Affiliations

  1. Bright Dairy and Food Co. Ltd., Shanghai, State Key Laboratory of Dairy Biotechnology, Shanghai, 200436, People’s Republic of China

    Quanyang Li

  2. College of Light Industry and Food Engineering, Guangxi University, Nanning, 530 004, People’s Republic of China

    Zhengtao Zhao, Hong Li & Quanyang Li

Authors
  1. Zhengtao Zhao
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Hong Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Quanyang Li
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Quanyang Li.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Zhao, Z., Li, H. & Li, Q. Isolation of β-lactoglobulin from buffalo milk and characterization of its structure changes as a function of pH and ionic strength. Food Measure 11, 948–955 (2017). https://doi.org/10.1007/s11694-017-9468-7

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11694-017-9468-7

Keywords

Search

Navigation