Yu Tzer-Yang, Morton James D, Clerens Stefan, Dyer Jolon M
Food & Bio-Based Products, AgResearch Lincoln Research Centre, Private Bag 4749, Christchurch 8140, New Zealand; Wine, Food & Molecular Biosciences, Lincoln University, Faculty of Agriculture and Life Sciences, PO Box 85084, Canterbury 7647, New Zealand.
Wine, Food & Molecular Biosciences, Lincoln University, Faculty of Agriculture and Life Sciences, PO Box 85084, Canterbury 7647, New Zealand.
Meat Sci. 2016 Sep;119:80-8. doi: 10.1016/j.meatsci.2016.04.024. Epub 2016 Apr 21.
Protein modifications of meat cooked by typical dry-heat methods (e.g., roasting) are currently not well understood. The present study utilised a shotgun proteomic approach to examine the molecular-level effect of roasting on thin lamb longissimus thoracis et lumborum patties, in terms of changes to both the protein profile and amino acid residue side-chain modifications. Cooking caused aggregation of actin, myosin heavy chains and sarcoplasmic proteins. Longer roasting time resulted in significantly reduced protein extractability as well as protein truncation involving particularly a number of myofibrillar and sarcoplasmic proteins, e.g., 6-phosphofructokinase, beta-enolase, l-lactate dehydrogenase A chain, alpha-actinin-3, actin and possibly myosin heavy chains. Modifications that have potential influence on nutritional properties, including carboxyethyllysine and a potentially glucose-derived N-terminal Amadori compound, were observed in actin and myoglobin after roasting. This study provided new insights into molecular changes resulting from the dry-heat treatment of meat, such as commonly used in food preparation.
目前，对于采用典型干热方法（如烤制）烹饪肉类所产生的蛋白质修饰了解尚浅。本研究采用鸟枪法蛋白质组学方法，从蛋白质谱变化和氨基酸残基侧链修饰两方面，研究烤制对薄切羊胸腰段最长肌肉饼的分子水平影响。烹饪导致肌动蛋白、肌球蛋白重链和肌浆蛋白聚集。较长的烤制时间会显著降低蛋白质的可提取性，并导致蛋白质截短，尤其是一些肌原纤维和肌浆蛋白，如6-磷酸果糖激酶、β-烯醇化酶、L-乳酸脱氢酶A链、α-辅肌动蛋白-3、肌动蛋白以及可能的肌球蛋白重链。烤制后，在肌动蛋白和肌红蛋白中观察到了对营养特性有潜在影响的修饰，包括羧乙基赖氨酸和一种可能源自葡萄糖的N端阿马多里化合物。本研究为肉类干热处理（如食品制备中常用的方法）所导致的分子变化提供了新见解。
