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GEL STRUCTURE OF NONMEAT PROTEINS AS RELATED TO THEIR ABILITY TO BIND MEAT PIECES
Author(s) -
SIEGEL D. G.,
CHURCH K. E.,
SCHMIDT G. R.
Publication year - 1979
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1979.tb06418.x
Subject(s) - chemistry , myosin , gluten , food science , sodium , salt (chemistry) , calcium , sodium caseinate , biochemistry , egg white , skimmed milk , chromatography , biophysics , biology , organic chemistry
Investigations on the binding abilities of some nonmeat proteins showed that those studied were inferior to the binding ability previously reported for myosin. Their binding abilities in the presence of 8% salt and 2% sodium tripolyphosphate were ranked from highest to lowest as wheat gluten, egg white, corn gluten, calcium reduced dried skim milk, bovine blood plasma, isolated soy protein and sodium caseinate. Structures of gels formed by these proteins and mixtures of them with crude myosin showed that a three dimensional network of protein fibers is not indicative of good binding ability. The types of molecular interactions stabilizing their gel structures are thought to be more important.