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LOW‐TEMPERATURE, LONG‐TIME HEATING OF BOVINE MUSCLE 2. Changes in Electrophoretic Patterns
Author(s) -
LAAKKONEN E.,
SHERBON J. W.,
WELLINGTON G. H.
Publication year - 1970
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.1365-2621.1970.tb12132.x
Subject(s) - tenderness , electrophoresis , chemistry , polyacrylamide gel electrophoresis , muscle protein , myoglobin , water soluble , water holding capacity , gel electrophoresis , food science , biochemistry , chromatography , biology , skeletal muscle , anatomy , enzyme , organic chemistry
SUMMARY: Polyacrylamide gel electrophoresis was used to follow changes in the nature of the water‐soluble proteins and juices of bovine muscle during low‐temperature heating. The slowestmoving anodic proteins were coagulated first. The myoglobins and myoalbumins were altered significantly only by holding the meat at 60°C. The largest changes in tenderness and amount of water‐soluble material in the meat occurred at the same temperatures under which the slow‐moving proteins were denatured. The most heat‐sensitive proteins detected were denatured before there were significant changes in tenderness or water‐soluble substance content.