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Protein-to-film adhesion as examined by amino analysis of protein binding to three different packaging films.

A weak protein solution extracted from chicken breast meat was exposed to three types of packaging materials. The crude myofibrillar protein solution (12.0 mg protein/mL buffer) was suspended in a 0.6M NaCl/NaPO4 buffer, then placed in bags made from either polyethylene (nonbinding film), a nylon blend (binding film), or Surlyn (binding film). Two separate experiments were conducted to determine the effects of exposure time at a constant temperature and varying endpoint exposure temperatures on the amount of bound protein by amino acid analysis. Bound amino acids were quantified and grouped by class based on functional side group. It was theorized that differences in the amount of bound amino acid class was linked to the mechanism by which the meat-to-film binding occurs. The protein solution was sealed in bags and held in a water bath for 5 s, 20 min, 40 min, and 60 min at 25.8 C for the timed experiment and heated from 25.8 C to 40, 55, 70, and 80 C for the temperature experiment. Protein adhesion occurred due to exposure of the solution to all films at 25.8 C. Greater protein adhesion was found in the two binding films than in the nonbinding film after 60 min of exposure. Heating the protein solution increased adhesion for the Surlyn film and showed a clear delineation in the degree of binding between the film types. Surlyn bound the most protein, followed by the nylon blend and then polyethylene. Bound protein increased in the Surlyn film with heating to 80 C, whereas the polyethylene did not show an increase in the amount of bound protein. Increases in binding observed between 55 and 80 C for Surlyn may be associated with transitional and conformational changes in muscle proteins that affect the adhesion of meat to the film surface.