Chaijan M, Benjakul S, Visessanguan W, Lee S, Faustman C
Department of Food Technology, School of Agricultural Technology, Walailak University, Nakhon Si Thammarat, 80160, Thailand.
J Food Sci. 2008 Jun;73(5):C292-8. doi: 10.1111/j.1750-3841.2008.00749.x.
Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb-natural actomyosin (NAM) model at 4 degrees C. Increases in metmyoglobin (MetMb) formation and the relative content of bound Mb were observed, as were decreases in whiteness and Ca(2+)-ATPase activity (P < 0.05). During the first 6 h of incubation, Mb bound preferably to myosin at domains other than the head portion, as evidenced by measurable ATPase activity. The potential binding of Mb to myosin heads occurred after 24-h incubation as evidenced by the marked decrease in Ca(2+)-ATPase activity of the NAM-Mb mixture when compared to that of NAM alone (P < 0.05). The interaction between fish Mb and myofibrillar proteins was more pronounced with increased storage time; formation of high-molecular-weight aggregates (> 206 kDa) also increased with time. Electrophoretic study revealed that disulfide bonds were not involved in Mb-NAM interactions.
在4℃下，在肌红蛋白-天然肌动球蛋白（NAM）模型中研究了鱼类肌红蛋白（Mb）与肌原纤维蛋白之间的相互作用。观察到高铁肌红蛋白（MetMb）形成增加、结合型Mb的相对含量增加，同时白度和Ca(2+)-ATP酶活性降低（P < 0.05）。在孵育的最初6小时内，Mb优先结合到肌球蛋白头部以外的区域，可测量的ATP酶活性证明了这一点。孵育24小时后，Mb与肌球蛋白头部发生潜在结合，与单独的NAM相比，NAM-Mb混合物的Ca(2+)-ATP酶活性显著降低证明了这一点（P < 0.05）。随着储存时间的延长，鱼类Mb与肌原纤维蛋白之间的相互作用更加明显；高分子量聚集体（> 206 kDa）的形成也随时间增加。电泳研究表明，二硫键不参与Mb-NAM相互作用。
