Preventive effects of amino acids and glutathione on the formaldehyde-induced denaturation of myofibrillar proteins

• Published in: Fisheries science Vol. 69; no. 3; pp. 605 - 614
• Main Authors: Abe, E. (Hokkaido Univ., Sapporo (Japan)), Hayakawa, K, Kimura, M, Kimura, I, Seki, N
• Format: Journal Article
• Language: English
• Published: Melbourne, Australia Blackwell Science Pty 01.06.2003
• Subjects: AMINES; AMINO ACIDS; cysteine; DENATURATION; FISH; FORMALDEHYDE; GLUTATHIONE; histidine; MUSCLE FIBRES; myofibril; PROTEINS; surimi; trimethylamine‐N‐oxide; walleye pollack
• ISSN: 0919-9268; 1444-2906
• DOI: 10.1046/j.1444-2906.2003.00663.x

Formaldehyde (FA)‐induced denaturation of myofibrillar proteins and its prevention were investigated by means of measuring the solubility, adenosine triphosphatase (ATPase) activity, and thermal gel formability of myofibrils and surimi proteins in the presence and absence of free amino acids and glutathione, reduced form. The addition of FA decreased the solubility of myofibrils in 0.5 M NaCl at pH 7.0 and 0°C depending on its concentration and incubation time. The solubility decrease was completely inhibited by the presence of equal, twofold, and threefold amounts of cysteine (Cys), glutathione, and histidine (His) to the amount of FA, respectively. Myofibrillar Ca‐ATPase was markedly activated at the initial phase and then decreased later by the addition of FA. The K‐ATPase was inactivated with an increase in the amount of FA. The FA‐induced changes in both ATPase activities were inhibited in the presence of Cys and His. Thermal gel formability of surimi paste increased only in a short period after the addition of a low concentration of FA. Practically, FA inhibited the thermal gelation and setting effect through the inactivation of transglutaminase. In the presence of Cys, His or glutathione, a strong elastic surimi gel was produced because FA‐induced detrimental effects were inhibited.