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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: mc@food.au.dk
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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.

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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.

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