食品科学 ›› 2011, Vol. 32 ›› Issue (5 ): 16-21.doi: 10.7506/spkx1002-6630-201105004

• 基础研究 • 上一篇    下一篇

冷藏条件下中国对虾肌肉蛋白质的生化特性

李 姣,李学鹏,励建荣*,朱军莉   

  1. 浙江工商大学食品与生物工程学院,浙江省食品安全重点实验室
  • 收稿日期:2010-06-17 修回日期:2011-01-19 出版日期:2011-03-15 发布日期:2011-03-03
  • 通讯作者: 励建荣 E-mail:lijianrong@zjgsu.edu.cn
  • 基金资助:
    国家“863”计划项目(2007AA091806);浙江省研究生创新项目(YK2008062);
    浙江工商大学研究生科研创新基金项目(1110 XJ 1509106)

Biochemical Properties of Muscle Protein from Fenneropenaeus chinensis during Chilled Storage

LI Jiao,LI Xue-peng,LI Jian-rong*,ZHU Jun-li#br#   

  1. Food Safety Key Laboratory of Zhejiang Province, College of Food Science and Biotechnology,
    Zhejiang Gongshang University, Hangzhou 310035, China
  • Received:2010-06-17 Revised:2011-01-19 Online:2011-03-15 Published:2011-03-03
  • Contact: LI Jian-rong E-mail:lijianrong@zjgsu.edu.cn

摘要: 以肌肉基本营养成分、蛋白质组成、肌动球蛋白盐溶性、巯基含量、Ca2+-ATPase活性、疏水性及SDS-PAGE分析等作为测定指标,考察中国对虾在冷藏时肌肉蛋白质的生化特性变化规律。结果表明,中国对虾肌肉是典型的高蛋白[(21.75±0.12)%]、低脂肪[(1.21±0.03)%]型食物;随着贮藏时间的延长,肌原纤维蛋白和肌基质蛋白的含量减少,肌浆蛋白含量先增加后减少,碱溶性蛋白含量逐渐增加;肌动球蛋白的盐溶性先上升后下降;巯基(-SH)数贮藏前期下降缓慢,第6天后显著下降;Ca2+-ATPase活性显著下降,且与贮藏时间呈显著线性相关(R0℃= -0.991,R4℃= -0.998),但0℃和4℃两组之间差异不显著。疏水性随贮藏时间延长显著增加,并呈显著线性关系(R0℃= 0.976,R4℃= 0.995),且0℃和4℃两组之间差别显著。SDS-PAGE结果显示,肌动蛋白、肌球蛋白重链、原肌球蛋白和分子质量为67kD的蛋白均发生了明显的降解。综合各指标的变化情况,表明随着冷藏时间的延长,蛋白质变性加剧,总体变性程度为0℃时小于4℃。Ca2+-ATPase活性和疏水性与贮藏时间呈显著线性关系,可以作为蛋白质变性程度的指示指标。

关键词: 中国对虾, 肌肉, 蛋白质, 生化特性

Abstract: In order to explore changes in biochemical properties of muscle proteins from Chinese shrimps (Fenneropenaeus chinensis) during storage at 0 or 4 ℃, basic nutrients, protein composition, salt soluble actomyosin, sulfhydryl content, Ca2+-ATPase activity and hydrophobicity were determined and SDS-PAGE analysis was also conducted at two-day intervals. The results showed that the muscle of Chinese shrimps was a typical food with relatively high protein ((21.75 ± 0.12)%) and low fat ((1.21± 0.03)%). With the extension of storage time, a decrease trend in myofibrillar protein and muscle matrix protein, a pattern of initial increase and final decrease in sarcoplasmic protein and actomyosin, a gradual increase trend in alkali soluble protein and a slow decrease in sulfhydryl content were observed for the muscle of Chinese shrimps. Meanwhile, a significant reduction of Ca2+-ATPase activity was also determined, which exhibited an obvious linear relationship with storage time (R0 ℃= 0.991, R4 ℃ = 0.998). However, the values of the above parameters at 0 ℃ did not significantly differ from those at 4 ℃. Hydrophobicity significantly increased with the extension of storage time, and revealed an obvious linear relationship with storage time (R0 ℃ = 0.976, R4 ℃ = 0.995). SDS-PAGE analysis showed that actin, myosin heavy chain, actomyosin and the protein with a molecule weight of 67 kD were obviously degraded during the storage. Based on a comprehensive consideration of these changes in various indicators, the denaturation of proteins was enhanced due to the extension of storage time. The degree of degradation at 4 ℃ was higher than that at 0 ℃. Ca2+-ATPase activity and hydrophobicity displayed a strong correlation with storage time, which can be considered to indicate the degradation of muscle protein during chilled storage.

Key words: Chinese shrimp (Fenneropenaeus chinensis), muscle, protein, biochemical property

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