食品科学 ›› 2022, Vol. 43 ›› Issue (15): 28-35.doi: 10.7506/spkx1002-6630-20210519-228

• 基础研究 • 上一篇    

预处理对南美白对虾剥壳效果和肌原纤维蛋白的影响

杨肖杰,黄卉,李来好,杨贤庆,岑剑伟,潘创,魏涯,赵永强,郝淑贤,林织   

  1. (1.中国水产科学研究院南海水产研究所,农业农村部水产品加工重点实验室,国家水产品加工技术研发中心,广东 广州 510300;2.上海海洋大学食品学院,上海 201306;3.广东顺欣海洋渔业集团有限公司,广东 阳江 529800)
  • 发布日期:2022-08-30
  • 基金资助:
    国家重点研发计划重点专项(2018YFD0700901-2);广东省重点领域研发计划项目(2019B020225001); 中国水产科学研究院基本科研业务项目(2020TD69);“扬帆计划”引进创新创业团队专项(2015YT02H109)

Effect of Pretreatment on the Peeling and Myofibrillar Protein of Pacific White Shrimps

YANG Xiaojie, HUANG Hui, LI Laihao, YANG Xianqing, CEN Jianwei, PAN Chuang, WEI Ya, ZHAO Yongqiang, HAO Shuxian, LIN Zhi   

  1. (1. Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National Research and Development Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China; 2. College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China; 3. Guangdong Shunxin Ocean Fishery Group Co., Ltd., Yangjiang 529800, China)
  • Published:2022-08-30

摘要: 采用不同方法(酶、冷冻和冰盐)对南美白对虾进行预处理,比较处理后虾壳可剥性及剥壳后虾仁质构,分析肌原纤维蛋白的理化指标和结构变化,探究预处理辅助剥壳效果及其对南美白对虾肌原纤维蛋白的影响。结果表明,与冷冻和冰盐处理相比,3.5 h酶处理辅助剥壳的剥壳用功较少,且完全剥壳率与其他两种方法无显著差异(P>0.05);Ca2+-ATPase活力、总巯基与活性巯基含量、内源荧光强度明显低于鲜虾,但除Ca2+-ATPase活力外,降低程度明显不及冷冻和冰盐处理组;其表面疏水性与鲜虾无显著差异(P>0.05),羰基含量与冰盐处理组无显著差异(P>0.05)。傅里叶变换红外光谱结果显示,预处理后肌原纤维蛋白的α-螺旋、β-转角相对含量都无显著变化(P>0.05),但酶和冰盐处理组均出现了β-折叠向无规卷曲的转变。结合十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)结果可知,冷冻和冰盐处理只改变了蛋白的结构而没有引起SDS-PAGE图谱的变化,酶处理引起了部分大分子质量蛋白质的降解,但虾肉质构特性与冷冻/冰盐处理差异不明显。

关键词: 辅助剥壳;南美白对虾;肌原纤维蛋白;理化性质;蛋白结构

Abstract: In this study, the effects of different pretreatments (enzymatic treatment, freezing and soaking in ice-salt solution mixture) on the peeling of the Pacific white shrimp Penaeus vannamei and myofibrillar proteins in it were investigated. Shrimp peelability, the texture of peeled shrimps and the physicochemical and structural characteristics of myofibrillar proteins were analyzed after pretreatment. The results showed that compared with the two other pretreatments, enzymatic pretreatment for 3.5 h reduced the work required to peel shrimps and resulted in no significant difference in complete peeling rate (P > 0.05). The enzymatic treatment markedly decreased Ca2+-ATPase activity, the contents of total sulfhydryl and active sulfhydryl and intrinsic fluorescence intensity. The contents of total sulfhydryl and active sulfhydryl and intrinsic fluorescence intensity but not Ca2+-ATPase activity were decreased less by the enzymatic treatment than by freezing and ice-salt solution treatment. Enzymatically treated shrimps had no significant difference in surface hydrophobicity and protein carbonyl content compared with fresh and ice salt-treated samples, respectively (P > 0.05). Fourier transform infrared (FTIR) spectroscopic analysis showed that the contents of α-helix and β-turn in myofibrillar proteins were not significantly changed after pretreatment (P > 0.05), but the enzymatic and ice-salt treatments resulted in the transformation of β-sheet to random coil. The results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that freezing and ice-salt treatment changed the conformation but not the SDS-PAGE pattern of myofibrillar proteins. The enzymatic treatment caused the degradation of some macromolecular proteins, but did not cause a significant difference in the texture characteristics of shrimp meat compared with freezing and ice-salt treatment.

Key words: peeling; Pacific white shrimps; myofibrillar protein; physicochemical properties; protein structure

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