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Alpha‐Helical Structure of Fish Actomyosin: Changes during Setting
Author(s) -
OGAWA MASAHIRO,
KANAMARU JUN,
MIYASHITA HIROKI,
TAMIYA TORU,
TSUCHIYA TAKAHIDE
Publication year - 1995
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.1365-2621.1995.tb05659.x
Subject(s) - circular dichroism , fish <actinopterygii> , incubation , chemistry , helix (gastropod) , helicity , alpha helix , crystallography , biophysics , biochemistry , biology , medicine , zoology , physics , fishery , particle physics , gastropoda
Participation of the α‐helix in setting was investigated using circular dichroism. The α‐helicity of the actomyosin from eight species of fish decreased during incubation at 30°C or at 40°C. The extent and pattern of decrease differed among species. When rate of decrease was plotted vs rate of increase in strength of gel preincubated at 30°C or at 40°C, the two factors correlated closely. We propose that the unfolding of α‐helix initiated setting.