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Heat‐induced Gelation of Chicken Gizzard Myosin
Author(s) -
MORITA JUNICHIRO,
SUGIYAMA HIROYUKI,
KONDO KEIJI
Publication year - 1994
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.1365-2621.1994.tb08112.x
Subject(s) - myosin , gizzard , chemistry , ionic strength , ionic bonding , chromatography , biophysics , ion , biochemistry , biology , organic chemistry , aqueous solution , paleontology
Chicken gizzard myosin solution formed a gel when heated above 40°C. The rigidity of the gel was constant above 65°C. Maximum pH for gel formation was 5.9 at 0.6M and 5.7 at 0.15M KCl. Higher rigidity of the myosin gel was observed at low ionic strength than at high ionic strength. Rigidities of myosin at 0.6M KCl increased by (mg/mL) 2.5 and at 0.15M (mg/mL) 1, 4 myosin concentration. The strength of gizzard myosin gels was comparable to that of myosin gels from chicken breast muscle under similar conditions.