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

被引:34
作者
Holt, C [1 ]
McPhail, D
Nylander, T
Otte, J
Ipsen, RH
Bauer, R
Ogendal, L
Olieman, K
de Kruif, KG
Léonil, J
Mollé, D
Henry, G
Maubois, JL
Pérez, MD
Puyol, P
Calvo, M
Bury, SM
Kontopidis, G
McNae, I
Sawyer, L
Ragona, L
Zetta, L
Molinari, H
Klarenbeek, B
Jonkman, MJ
Moulin, J
Chatterton, D
机构
[1] Hannah Res Inst, Ayr KA6 5HL, Scotland
[2] Univ Lund, Dept Phys Chem 1, S-22100 Lund, Sweden
[3] Royal Vet & Agr Univ, Dept Dairy & Food Sci, DK-1958 Frederiksberg, Denmark
[4] Royal Vet & Agr Univ, Dept Math & Phys, DK-1871 Frederiksberg C, Denmark
[5] NIZO Food Res, NL-6710 BA Ede, Netherlands
[6] INRA, Rech Technol Laitiere Lab, F-35042 Rennes, France
[7] Fac Vet, Zaragoza 50013, Spain
[8] Univ Edinburgh, Inst Cell & Mol Biol, Edinburgh EH9 3JR, Midlothian, Scotland
[9] CNR, Ist Chim Macromol, Lab NMR, I-20131 Milan, Italy
[10] Univ Verona, Dept Sci & Tecnol, I-37134 Verona, Italy
[11] Borculo Domo Ingredients, NL-7271 AB Borculo, Netherlands
[12] Friesland Coberco Dairy Foods Res Ctr Deventer, NL-7418 BA Deventer, Netherlands
[13] Armor Proteines SAS, F-35460 Le Pont, St Brice En Cog, France
[14] MD Foods Ingredients, DK-6920 Videbaek, Denmark
关键词
alpha-lactalbumin; beta-lactoglobulin; ellipsometry; microcalorimetry; NMR spectroscopy; rheology; whey protein concentrate; whey protein isolate; x-ray crystallography;
D O I
10.1046/j.1365-2621.1999.00326.x
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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 beta-lactoglobulin % on the recovered % showed that the nine samples could be placed in three distinct groups with beta-lactoglobulin weight % of 70.9 +/- 1.1 (Group 1), 62.0 +/- 3.4 (Group 2) and 39.5 +/- 4.9 (Group 3). Measurements by H-1-NMR spectroscopy, on 3 of the samples confirmed that the native fold still predominated in the beta-lactoglobulin. beta-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 Groups 1 and 2 with a more prominent peak due to alpha-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 beta-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.
引用
收藏
页码:587 / 601
页数:15
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