SEPARATION OF SOY‐SPUN FIBER, EGG ALBUMEN, AND WHEAT GLUTEN BLEND BY SODIUM DODECYL SULFATE GEL ELECTROPHORESIS

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Abstract
Commercial soy spun fiber, egg albumen, wheat gluten, and a mixture of these proteins were subjected to a variety of electrophoretic techniques to find a procedure that could separate, detect, and characterize components of the individual proteins in a simulated meat analog system. Of the techniques utilized, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) provided the only effective separation of the protein components. Sample handling conditions in the SDS‐PAGE dispersion solution included the use of heat, 2‐mercaptoethanol (ME), and centrifugation. Samples centrifuged prior to electrophoresis gave superior patterns to those not centrifuged. Heat treatment of samples had no noticeable effect on separation patterns. Protein separation and resolution for all three protein sources were clear and distinct but considerably different in samples without and with added ME, the latter tending to decrease the number of large molecular weight components and increase low molecular weight components. While a majority of the protein components of soy‐spun fiber, egg albumen, and wheat gluten showed similar mobilities, there were several proteins or protein subunits with distinct mobilities in the presence or absence of ME. Therefore, SDS‐PAGE could be used to separate and identify these proteins and to study processing induced changes in commercial meat analogs containing blends of these proteins.