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ɛ‐(γ‐Glutamyl)lysine Crosslink Formation in Sardine Myofibril Sol during Setting at 25°C
Author(s) -
TSUKAMASA YASUYUKI,
SATO KENJI,
SHIMIZU YUTAKA,
IMAI CHIHARU,
SUGIYAMA MASAAKI,
MINEGISHI YUTAKA,
KAWABATA MAKOTO
Publication year - 1993
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.1365-2621.1993.tb09358.x
Subject(s) - sardine , myofibril , lysine , chemistry , incubation , breaking strength , food science , salt (chemistry) , tissue transglutaminase , biochemistry , enzyme , fishery , biology , materials science , organic chemistry , fish <actinopterygii> , amino acid , composite material
The quantitative change of ɛ‐(y‐glutamyl)lysine (EGL) crosslink and relationship between crosslink content and gel‐strength were examined on salt‐ground myofibril sol from sardine ( Sardinops melanostictus ) during incubation at 25°C. In the presence of EGTA, no EGL crosslinks were detected in myofibril sol and gelation did not occur. The EGL crosslink content and breaking strength of gels increased in proportion to incubation time. High correlation was observed between the logarithm of breaking strength and logarithm of EGL crosslink content (r=0.987). The EGL crosslinks formed by transglutaminase are important in the setting of sardine meat sol at < 30°C.