Hostname: page-component-586b7cd67f-t7czq Total loading time: 0 Render date: 2024-11-24T11:07:38.751Z Has data issue: false hasContentIssue false
  • English
  • Français

Diafiltration affects the gelation properties of concentrated casein micelle suspensions obtained by filtration

Published online by Cambridge University Press:  14 May 2020

Zhengtao Zhao ,
Isis Renhe ,
Robert Fu  and
Milena Corredig
Zhengtao Zhao
Affiliation:
Food Science, University of Guelph, Guelph, OntarioN1G 1W5, Canada
Isis Renhe
Affiliation:
Food Science, University of Guelph, Guelph, OntarioN1G 1W5, Canada
Robert Fu
Affiliation:
GayLea Foods, Research and Development, Speedvale Avenue, Guelph, OntarioN1H1J5, Canada
Milena Corredig*
Affiliation:
Food Science, University of Guelph, Guelph, OntarioN1G 1W5, Canada iFood Center, Food Science, Aarhus University, AarhusN 8200, Denmark
*
Author for correspondence: Milena Corredig, Email: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

Using membrane filtration it is possible to selectively concentrate proteins and, in the case of microfiltration, concentrate casein micelles. During filtration, water is often added and this practice, called diafiltration, causes further release of permeable components and maintains filtration efficiency. Filtration causes changes in composition of the protein as well as the soluble phase, including soluble calcium, which is a critical factor controlling the gelation properties of the casein micelles in milk. It was hypothesized that concentrates obtained using membrane filtration with or without diafiltration would have different gelation behavior. To test this hypothesis, two concentrates of similar casein micelle volume fraction were prepared, using spiral wound polymeric microfiltration membranes with a 800 kDa molecular weight cutoff, with or without diafiltration. The concentrates showed a gelation behavior comparable to that of skim milk, with a similar gelation time and with a higher firmness, due to the higher number of protein linkages in the network. In contrast, the hydrolysis of κ-casein by chymosin and casein aggregation were inhibited in diafiltered casein micelle suspensions. When the concentrates were recombined with the original skim milk to a final concentration of 5% protein, which re-established a similar soluble phase composition, differences in gelation behavior were no longer observed: both treatments showed similar gelation time and gel firmness. These results confirmed that membrane filtration can result in concentrates with different functionality, and that ionic environmental conditions are critical to the aggregation behavior of casein micelles. This is of particular significance in industrial settings where these fractions are used as a way to standardize proteins in cheese making.

Keywords

Casein micellesconcentrated milkMicrofiltrationDiafiltrationrheologyrennet gelation
Type
Research Article
Information
Journal of Dairy Research , Volume 87 , Issue 2 , May 2020 , pp. 248 - 254
Copyright
© The Author(s), 2020. Published by Cambridge University Press on behalf of Hannah Dairy Research Foundation.

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

*

Current address: Zhengtao Zhao, Parmalat Canada Limited, Research and Development, London, Ontario, Canada.

†

Current address: Isis Renhe, Instituto de Laticínios Cândido Tostes, Empresa de Pesquisa Agropecuária de Minas Gerais – EPAMIG, Tenente Luiz de Freitas 116, Juiz de Fora – MG 36045-560, Brazil.

References

Alexander, M, Nieh, M-P, Ferrer, MA and Corredig, M (2011) Changes in the calcium cluster distribution of ultrafiltered and diafiltered fresh skim milk as observed by small angle neutron scattering. Journal of Dairy Research 78, 349–356.CrossRefGoogle ScholarPubMed
Bonfatti, V, Grigoletto, L, Cecchinato, A, Gallo, L and Carnier, P (2008) Validation of a new reversed-phase high-performance liquid chromatography method for separation and quantification of bovine milk protein genetic variants. Journal of Chromatography A 1195, 101–106.CrossRefGoogle ScholarPubMed
Choi, J, Horne, DS and Lucey, JA (2007) Effect of insoluble calcium concentration on rennet coagulation properties of milk. Journal of Dairy Science 90, 2612–2623.CrossRefGoogle ScholarPubMed
Corredig, M and Salvatore, E (2016) Enzymatic coagulation of milk. In McSweeney, P and O'Mahony, J (eds) Advanced Dairy Chemistry. New York: Springer, pp. 287–307CrossRefGoogle Scholar
Corredig, M, Krishnakutti Nair, P, Li, Y, Eshpari, H and Zhao, Z (2019) Invited review: understanding the behavior of caseins in milk concentrates. Journal of Dairy Science 102, 4772–4782.CrossRefGoogle ScholarPubMed
Dalgleish, D (1980) Effect of milk concentration on the rennet coagulation time. Journal of Dairy Research 47, 231–235.CrossRefGoogle Scholar
Dalgleish, D (1983) Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength. Journal of Dairy Research 50, 331–340.CrossRefGoogle Scholar
De Kruif, CG (1998) Supra-aggregates of casein micelles as a prelude to coagulation. Journal of Dairy Science 81, 3019–3028.CrossRefGoogle Scholar
De Kruif, CG and Zhulina, EB (1996) κ-casein as a polyelectrolyte brush on the surface of casein micelles. Colloids and Surfaces A: Physicochemical and Engineering Aspects 117, 151–159.CrossRefGoogle Scholar
Gaygadzhiev, Z, Massel, V, Alexander, M and Corredig, M (2012) Addition of sodium caseinate to skim milk inhibits rennet-induced aggregation of casein micelles. Food Hydrocolloids 26, 405–411.CrossRefGoogle Scholar
Jaeggi, JJ, Martinelli, C, Johnson, ME and Lucey, JA (2011) Standardization of milk using cold ultrafiltration retentates for the manufacture of Swiss cheese: effect of altering coagulation conditions on yield and cheese quality. Journal of Dairy Science 94, 2719–2730.Google Scholar
Krishnakutti Nair, P and Corredig, M (2015) Rennet-induced gelation of concentrated milk in the presence of sodium caseinate: differences between milk concentration using ultrafiltration and osmotic stressing. Journal of Dairy Science 98, 27–36.CrossRefGoogle Scholar
Li, Y and Corredig, M (2019) Acid induced gelation behavior of skim milk concentrated by membrane filtration. Journal of Texture Studies 51, 101–110.Google ScholarPubMed
López-Fandiño, R, Acedo, MI and Ramos, M (1993) Comparative study by HPLC of caseinmacropeptides from cows’, ewes’ and goats’ milk. Journal of Dairy Research 60, 117–121.CrossRefGoogle Scholar
Lucey, JA, Gorry, C, Kennedy, BO, Kalab, M and Fox, PF (1996) Effect of acidification and neutralization of milk on some physico-chemical properties of casein micelles. International Dairy Journal 6, 257–272.CrossRefGoogle Scholar
Martin, GJO, Williams, RPW and Dunstan, DE (2010) Effect of manufacture and reconstitution of milk protein concentrate powder on the size and rennet gelation behaviour of casein micelles. International Dairy Journal 20, 128–131.CrossRefGoogle Scholar
Mishra, R, Govindasamy-Lucey, S and Lucey, J (2005) Rheological properties of rennet-induced gels during the coagulation and cutting process: impact of processing conditions. Journal of Texture Studies 36, 190–212.CrossRefGoogle Scholar
Nelson, BK and Barbano, DM (2005) A microfiltration process to maximize removal of serum proteins from skim milk before cheese making. Journal of Dairy Science 88, 1891–1900.CrossRefGoogle ScholarPubMed
Rahimi Yazdi, S, Ferrer, MA and Corredig, M (2010) Non-suppressed ion chromatographic determination of total calcium in milk. Journal of Dairy Science 93, 1788–1793.CrossRefGoogle Scholar
Renhe, IRT and Corredig, M (2018) Effect of partial whey protein depletion during membrane filtration on thermal stability of milk concentrates. Journal of Dairy Science 101, 8757–8766.CrossRefGoogle ScholarPubMed
Renhe, IRT, Zhao, Z and Corredig, M (2019) A comparison of the heat stability of fresh milk protein concentrates obtained by microfiltration, ultrafiltration and diafiltration. Journal of Dairy Research 86, 347–353.CrossRefGoogle ScholarPubMed
Requena, T, Fontecha, J and Goude, H (1999) Effect of different membrane separation technologies (ultrafiltration and microfiltration) on the texture and microstructure of semihard low-fat cheeses. Journal of Agriculture and Food Chemistry 47, 558–565.Google Scholar
Sandra, S and Corredig, M (2013) Rennet induced gelation of reconstituted milk protein concentrates: the role of calcium and soluble proteins during reconstitution. International Dairy Journal 29, 68–74.CrossRefGoogle Scholar
Sandra, S, Cooper, C, Alexander, M and Corredig, M (2011) Coagulation properties of ultrafiltered milk retentates measured using rheology and diffusing wave spectroscopy. Food Research International 44, 951–956.CrossRefGoogle Scholar
Waungana, A, Singh, H and Bennett, RJ (1999) Rennet coagulation properties of skim milk concentrated by ultrafiltration: effects of heat treatment and pH adjustment. Food Research International 31, 645–651.CrossRefGoogle Scholar
Zhao, Z and Corredig, M (2016a) Influence of sodium chloride on the colloidal and rennet coagulation properties of concentrated casein micelle suspensions. Journal of Dairy Science 99, 6036–6045.CrossRefGoogle Scholar
Zhao, Z and Corredig, M (2016b) Short communication: serum composition of milk subjected to re-equilibration by dialysis at different temperatures, after pH adjustments. Journal of Dairy Science 99, 2588–2593.CrossRefGoogle Scholar