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The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water
Author(s) -
ITO Yukiko,
TATSUMI Ryuichi,
WAKAMATSU JunIchi,
NISHIMURA Takanori,
HATTORI Akihito
Publication year - 2003
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1046/j.1344-3941.2003.00134.x
Subject(s) - myofibril , titin , chemistry , solubilization , biochemistry , loin , polyacrylamide , skeletal muscle , chromatography , chicken breast , polyacrylamide gel electrophoresis , sarcomere , myocyte , biology , anatomy , food science , enzyme , microbiology and biotechnology , polymer chemistry
Myofibrillar proteins of vertebrate skeletal muscles are insoluble in solutions of ionic strength that approximate physiological conditions. We established a method to solubilize more than 80% of chicken breast muscle myofibrillar proteins in water for the use of meat as a source of food protein. SDS‐polyacrylamide gel electrophoretic patterns of water‐soluble myofibrillar proteins demonstrated that all identified myofibrillar proteins except connectin/titin were soluble in water. A part of α‐actinin was released from myofibrils by repeated washing with 2.5 mmol/L NaCl and 5 mmol/L L‐histidine solution, and subsequent destruction of connectin/titin in washed myofibrils by ultrasonication resulted in solubilization of a large fraction of chicken breast muscle myofibrillar proteins in water. Myofibrillar proteins of chicken leg, pork loin, beef shoulder loin, and lamb were also solubilized in water using this procedure.