Zhang Longteng, Li Qian, Hong Hui, Luo Yongkang, Lametsch René
Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
Department of Food Science, University of Copenhagen, 1958 Frederiksberg C, Denmark.
Food Res Int. 2020 Nov;137:109678. doi: 10.1016/j.foodres.2020.109678. Epub 2020 Sep 17.
A differential proteome analysis using label-free strategy was conducted to elucidate the stunning stress-induced proteome changes and its relationship to textural softening in silver carp (Hypophthalmichthys molitrix) fillets. Compared with the muscle proteome of fillets stunned by percussion, ice/water and gill cut stunning resulted in 43 differentially abundant proteins (DAPs) that were involved in muscle contraction, energy metabolism, antioxidant defense, protein turnover, etc., and gill cut-stunned fillets showed the most significant proteome changes with 28 up- and down-regulated DAPs. In addition, textural softening was more obvious in ice/water- and gill cut-treated fillets and was closely correlated to 21 DAPs including fast muscle troponin T, fragments of myosin, superoxide dismutase [Cu-Zn], ribosomal protein L38, isoform 2 of heat shock cognate 70, two subunits of proteasome, etc., and those DAPs were selected as potential proteomic markers to trace the accelerated textural softening in stunning-stressed fillets.
采用无标记策略进行差异蛋白质组分析,以阐明鲢鱼(Hypophthalmichthys molitrix)鱼片因致昏应激引起的蛋白质组变化及其与质地软化的关系。与击晕、冰/水致昏和切鳃致昏的鱼片肌肉蛋白质组相比,冰/水致昏和切鳃致昏导致43种差异丰富蛋白质(DAPs),这些蛋白质参与肌肉收缩、能量代谢、抗氧化防御、蛋白质周转等过程,切鳃致昏的鱼片显示出最显著的蛋白质组变化,有28种上调和下调的DAPs。此外,冰/水处理和切鳃处理的鱼片质地软化更明显,并且与21种DAPs密切相关,包括快肌肌钙蛋白T、肌球蛋白片段、超氧化物歧化酶[Cu-Zn]、核糖体蛋白L38、热休克同源蛋白70的异构体2、蛋白酶体的两个亚基等,这些DAPs被选为潜在的蛋白质组学标记物,以追踪致昏应激鱼片加速的质地软化。