Chu George Hao, Sterling Clarence
Dept. of Food Science and Technology, University of California, Davis, Calif, U.S.A.
J Texture Stud. 1970 Mar;1(2):214-222. doi: 10.1111/j.1745-4603.1970.tb00725.x.
The white muscle of the Sacramento blackfish (Orthodon microlepidotus) was processed by freezing, dehydration, and cooking. Myosin was extracted immediately afterwards or following a period of storage in order to examine evidence for denaturation. The tests used were the solubility of whole muscle protein and the intrinsic viscosity, isoelectric point, ATPase activity, ultra-violet absorption spectrum, and optical rotatory dispersion of purified myosin extract. Almost all measures used showed that denaturation increased in the order: fresh < frozen < frozen-stored < dehydrated < dehydrated-stored < cooked.
对萨克拉门托黑鱼(Orthodon microlepidotus)的白肌进行冷冻、脱水和烹饪处理。随后立即提取肌球蛋白,或在储存一段时间后提取,以检验变性证据。所采用的测试包括全肌肉蛋白的溶解度、特性粘度、等电点、ATP酶活性、紫外吸收光谱以及纯化肌球蛋白提取物的旋光色散。几乎所有所采用的测量结果都表明,变性程度按以下顺序增加:新鲜<冷冻<冷冻储存<脱水<脱水储存<烹饪。