研究可能影响鸭肉肌动球蛋白解离的多种因素,包括内部因素(AMP、IMP、ADP、ATP、Ca2+、PO43-)和外部因素(NaCl腌制、不同种类磷酸盐腌制)。以肌动球蛋白提取物和鸭肉为原料,主要应用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)和蛋白质印迹(Western blotting)法进行检测。结果表明:在4 ℃条件下,经过8、16 mmol/L的AMP、IMP处理和25~50 mmol/L PO43-处理的肌动球蛋白,检测到肌动蛋白条带浓度明显增加;经过8、16 mmol/L ADP处理和0.1~5.0 mmol/L Ca2+处理后的肌动球蛋白,检测到肌动蛋白条带浓度无明显变化。腌制对肌动球蛋白解离无明显影响。
This study illustrated multiple potential factors influencing actomyosin dissociation, including internal factors (AMP, IMP, ADP, ATP, Ca2+, and PO43-) and external factors (marinated with NaCl or with different phosphate salts). Actomyosin was extracted from duck breast muscle and the protein composition was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and western-blot analysis. Results: The density of actin bands was increased significantly when the actomyosin was treated with 8, 16 mmol/L AMP or IMP or with 25-50 mmol/L PO43- at 4 ℃, whereastreatment with 8, 16 mmol/L ADP or with 0.1-5 mmol/L Ca2+ did not result in a significant change in actin band densities. These results suggest that marinating duck muscle with different salts has no significant effects on actomyosin dissociation.