Effect of endogenous proteases and heat shock protein 70 on myofibril dissociation during refrigeration in tilapia

  • FAN Mingliang ,
  • HAO Shuxian ,
  • LI Laihao ,
  • CHEN Shengjun ,
  • CEN Jianwei ,
  • WU Yanyan ,
  • WEI Ya ,
  • XIANG Huan ,
  • HUANG Hui
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  • 1(College of Food Science, Shanghai Ocean University, Shanghai 201306, China)
    2(South China Sea Fisheries Research Institute, China Academy of Fisheries Science, National Aquatic Products Processing Technology R&D Centre, Key Laboratory of Aquatic Products Processing, Ministry of Agriculture and Rural Affairs,Guangzhou 510300, China)
    3(Key Laboratory of Efficient Utilization and Processing of Marine Fishery Resources of Hainan Province, Sanya Tropical Fisheries Research Institute, Sanya 572018, China)

Received date: 2022-10-10

  Revised date: 2022-11-11

  Online published: 2023-06-30

Abstract

In order to investigate the relationship between endogenous proteases and heat shock protein 70(HSP 70) with myofibrillar dissociation of tilapia during refrigeration, experiments were performed to determine the changes in myofibril fragmentation index, myofibrillar dissociation, endogenous protease activity, and HSP 70 content of tilapia meat during vacuum-packed refrigeration at 4℃ for 48 h, and the correlation analysis was performed. Results showed that an overall increasing trend in the change of myofibril fragmentation index during the refrigeration of fish, ending at 3.52 times the initial value. The dissociated myosin heavy chain and actin content showed an increasing trend, eventually increasing by 70% and 65% respectively from the initial values. The pH were decreasing followed by a slight recovery with a range of 6.5 to 7.0. The activities of cathepsin B and L showed a constant increase, and the activities of cathepsin D and calpain showed a trend of increasing and then decreasing, and reached the maximum at 8 and 12 h, respectively. HSP 70 content showed an increase followed by a decrease, reaching a maximum at 4 h and finally decreasing by 22.27% compared to the initial value. Myofibril fragmentation index showed a highly significant positive correlation with cathepsin B and L activities (P<0.01), and with myofibrillar dissociation of both myosin heavy chain and actin content were highly significantly positively correlated (P<0.01) and negatively correlated with HSP 70 content (P<0.05). HSP 70 can stabilize myofibril structure by binding to thick and thin filaments of myofibrils. HSP 70 content was significantly negatively correlated with cathepsin L (P<0.05). Cathepsin B and L are essential proteases affecting the integrity of myofibrillar, and cathepsin L may affect the dissociation of thick and thin filaments of myogenic fibers by degrading HSP 70.

Cite this article

FAN Mingliang , HAO Shuxian , LI Laihao , CHEN Shengjun , CEN Jianwei , WU Yanyan , WEI Ya , XIANG Huan , HUANG Hui . Effect of endogenous proteases and heat shock protein 70 on myofibril dissociation during refrigeration in tilapia[J]. Food and Fermentation Industries, 2023 , 49(11) : 140 -146 . DOI: 10.13995/j.cnki.11-1802/ts.033884

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