Premium
Formation of ε‐(γ‐Glutamyl) Lysine Cross‐Link in Cured Horse Mackerel Meat Induced by Drying
Author(s) -
KUMAZAWA Y.,
SEGURO K.,
TAKAMURA M.,
MOTOKI M.
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.tb06112.x
Subject(s) - lysine , myosin , chemistry , horse mackerel , food science , mackerel , fish <actinopterygii> , biochemistry , biology , fishery , amino acid
Block meat cut from horse mackerel was cured in 3M NaCl (pH 7.5) in the presence and absence of 5 mM EDTA for 3 hr at 4°C. During drying at 30°C, changes in the myosin heavy chain and ε‐(γ‐glutamyl)lysine isopeptide bonds in the meat were observed. After 20 hr drying, cross‐linking of the myosin heavy chain was observed and ε‐(γ‐glutamyl)lysine bonds increased eight fold. These changes were inhibited in the presence of EDTA. These results suggested that trans‐glutaminase was probably involved in the cross‐linking reaction of the myosin heavy chain in the manufacture of dried fish (“Himono” in Japan).