Characterizes casein-based films.
USDA-ARS scientists had previously shown that films based on C[O.sub.2]-precipitated casein possess greater hydrophobicity. This leads to lower water solubility, compared to films made from commercial calcium caseinate. The investigators studied C[O.sub.2] casein films using transmission electron microscopy (TEM) and compared them with films derived from acid casein, sodium caseinate and calcium caseinate. Their goal was to gain insight into differences in film properties, particularly water solubility, that are caused by different processing methods.
The researchers found that some alteration had occurred in the structure of casein micelles in C[O.sub.2] casein They are similar to those found in acid casein, which is insoluble in water. They think that the large aggregates shown in the TEM images of C[O.sub.2] casein film, relative to the smaller aggregates seen for calcium caseinate film, may be caused by changes in protein-protein interactions on the micellar level. They may be attributable to certain characteristics, such as water solubility.
These scientists generally are looking to develop new food and nonfood uses for whey and casein, as well as for nonfat dry milk, through basic research and process development engineering. Specifically, new processing techniques for the production of edible films from milk proteins are being investigated to expand their use in new food and nonfood products. On one front, casein molecular models developed previously by the scientists will be used to guide production of enriched fractions of the individual caseins.
Further information. Phoebe Qi, USDA-ARS Dairy Processing and Products Research, 600 E. Mermaid Lane, Wyndmoor, PA 19038; phone: 215-233-6438; fax: 215-233-6795; email: firstname.lastname@example.org.
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|Publication:||Emerging Food R&D Report|
|Date:||May 1, 2006|
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