唐玲玲,严金红,徐慧倩,邓尚贵,缪文华.低温等离子体对南美白对虾肌肉蛋白质性质和结构的影响[J].食品安全质量检测学报,2022,13(10):3083-3089
低温等离子体对南美白对虾肌肉蛋白质性质和结构的影响
Effects of cold atmospheric plasma on protein properties and structure of Penaeus vannamei
投稿时间:2022-03-29  修订日期:2022-05-17
DOI:
中文关键词:  南美白对虾  肌肉蛋白质  低温等离子体  蛋白质氧化
英文关键词:Penaeus vannamei  muscle protein  cold atmospheric plasma  protein oxidation
基金项目:浙江省公益技术研究计划项目(LGJ20C200002)
作者单位
唐玲玲 浙江海洋大学食品与药学学院 
严金红 浙江海洋大学食品与药学学院 
徐慧倩 浙江海洋大学食品与药学学院 
邓尚贵 浙江海洋大学食品与药学学院 
缪文华 浙江海洋大学食品与药学学院 
AuthorInstitution
TANG Ling-Ling Department of Food Science and Pharmaceutics, Zhejiang Ocean University 
YAN Jin-Hong Department of Food Science and Pharmaceutics, Zhejiang Ocean University 
XU Hui-Qian Department of Food Science and Pharmaceutics, Zhejiang Ocean University 
DENG Shang-Gui Department of Food Science and Pharmaceutics, Zhejiang Ocean University 
MIAO Wen-Hua Department of Food Science and Pharmaceutics, Zhejiang Ocean University 
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中文摘要:
      目的 研究低温等离子体(cold atmospheric plasma, CAP)对南美白对虾肌肉蛋白质性质和结构的影响。方法 采取不同等离子体条件(电压: 20、40、60 kV; 时间: 1、2、3 min)对南美白对虾肌肉蛋白进行处理, 通过分析肌浆蛋白、肌原纤维蛋白、表面疏水性、总巯基含量、Ca2+-ATPase活性、十二烷基硫酸钠-聚丙烯酰胺电泳(sodium dodecyl sulfate polyacrylamide gel electrophoresis, SDS-PAGE)指标, 探讨CAP对南美白对虾肌肉蛋白的影响。结果 与对照组相比, 随着处理时间和电压的增加, 虾体的肌浆蛋白、肌原纤维蛋白含量、总巯基含量、Ca2+-ATPase活性均显著下降(P<0.05), 而表面疏水性显著升高(P<0.05)。处理条件为60 kV、3 min时, 样品各指标变化最明显。SDS-PAGE电泳显示肌原纤维蛋白的肌球蛋白重链条带增强, 副肌球蛋白条带逐渐消失, 在分子量为25 kDa附近出现新的蛋白条带。结论 CAP处理能导致南美白对虾肌肉氧化, 蛋白质变性。
英文摘要:
      Objective To investigate the effects of cold atmospheric plasma (CAP) on protein properties and structure of Penaeus vannamei. Methods The muscle protein of Penaeus vannamei were treated with different CAP conditions (voltage: 20, 40, 60 kV; time: 1, 2, 3 min), and the index such as myogen, myofibrillar protein, surface hydrophobicity, total sulfhydryl content, Ca2+-ATPase activity, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were investigated. Results Compared with the control group, with the increase of treatment time and voltage, the myogen, myofibrillar protein content, total sulfhydryl content and Ca2+-ATPase activity of shrimp decreased significantly (P<0.05), while the surface hydrophobicity increased significantly (P<0.05). when the treatment condition was 60 kV, 3 min, the changes of each index of the sample were the most obvious. The SDS-PAGE showed that the myosin heavy chain of myofibrin enhanced, the accessory myosin bands gradually disappeared, and new protein bands appeared near the molecular weight of 25 kDa. Conclusion CAP treatment promotes muscle oxidation of Penaeus vannamei, leading to protein denaturation.
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