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Some physico-chemical properties of nine commercial or semi-commercial whey protein concentrates, isolates and fractions

Summary The physico‐chemical properties are reported for a group of whey protein powders prepared on a commercial or semi‐commercial scale by three companies and chemically characterized as described elsewhere (Holt et al., 1999). The dependence of the apparent β‐lactoglobulin % on the recovered % s...

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Published in:International journal of food science & technology 1999-10, Vol.34 (5-6), p.587-601
Main Authors: Holt, Carl, McPhail, Deborah, Nylander, Tommy, Otte, Jeanette, Ipsen, Richard H., Bauer, Rogert, Øgendal, Lars, Olieman, Kees, de Kruif, Kees G., Léonil, Joëlle, Mollé, Daniel, Henry, Gwénaële, Maubois, Jean Louis, Pérez, M. Dolores, Puyol, Pilar, Calvo, Miguel, Bury, Stella M., Kontopidis, George, McNae, Iain, Sawyer, Lindsay, Ragona, Laura, Zetta, Lucia, Molinari, Henriette, Klarenbeek, Bert, Jonkman, Margrethe J., Moulin, Jacques, Chatterton, Dereck
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Language:English
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Summary:Summary The physico‐chemical properties are reported for a group of whey protein powders prepared on a commercial or semi‐commercial scale by three companies and chemically characterized as described elsewhere (Holt et al., 1999). The dependence of the apparent β‐lactoglobulin % on the recovered % showed that the nine samples could be placed in three distinct groups with β‐lactoglobulin weight % of 70.9 ± 1.1 (Group 1), 62.0 ± 3.4 (Group 2) and 39.5 ± 4.9 (Group 3). Measurements by 1H‐NMR spectroscopy, on 3 of the samples confirmed that the native fold still predominated in the β‐lactoglobulin. β‐lactoglobulin could be crystallized from all the powders and the normal space group and cell dimensions were determined for the 8 samples that gave crystals of good enough quality for X‐ray studies. Differential scanning microcalorimetry of samples dispersed in a phosphate buffer showed a clear difference between Goups 1 and 2 with a more prominent peak due to α‐lactalbumin in the Group 2 samples. Light scattering and size exclusion chromatography showed that two types of aggregates were present to a variable extent in all the samples and after a heat treatment, the larger aggregates tended to predominate in Group 2. The rheology measurements, also made in the phosphate buffer, showed a difference of gel stiffness during heat treatment between the Group 1 and Group 2 samples with the exception of the BORCwpc+ sample. Within each group, gel stiffness increased with the degree of lactoslylation of the β‐lactoglobulin. Interfacial measurements on samples dispersed in water presented a more complex pattern of behaviour although surface tension measurements at the air water interface of the Group 2 samples showed a two‐step pattern of surface tension decrease with time, compared to a single step pattern in the Group 1 samples.
ISSN:0950-5423
1365-2621
DOI:10.1046/j.1365-2621.1999.00326.x