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三疣梭子蟹(Portunus trituberculatus)冻藏过程中肌肉蛋白质生化特性的变化

黄琳 张莉 武丹露

海洋科学2017,Vol.41Issue(6):41-47,7.
海洋科学2017,Vol.41Issue(6):41-47,7.DOI:10.11759/hykx20151224003

三疣梭子蟹(Portunus trituberculatus)冻藏过程中肌肉蛋白质生化特性的变化

Changes in the biochemical properties of muscle protein of swimming crab (Portunus trituberculatus) during frozen storage

黄琳 1张莉 1武丹露1

作者信息

  • 1. 中国海洋大学 食品科学与工程学院, 山东 青岛 266003
  • 折叠

摘要

Abstract

This study analyzed the changes in the biochemical characteristics of muscle protein during frozen stor-age at –20℃ or –40℃ based on nutrient composition, protein composition, myofibrillar protein content, Ca2+-ATPase ac-tivity, sulfhydryl group content, disulfide bond content, and SDS-PAGE analysis of myofibrillar protein of swim-ming crab. Results showed that the muscle of the swimming crab was a typical food with a high protein content. With extension of the duration of frozen storage, the water-soluble protein content increased and then decreased, the salt-soluble protein and -insoluble protein contents decreased, and the content of alkaline-soluble protein increased gradually. Myofibrillar protein content, Ca2+-ATPase activity, and sulfhydryl group content decreased with prolon-gation of the duration of frozen storage, whereas the disulfide bond content showed an increasing trend, with a sig-nificant difference between the two groups at –20℃ and –40℃ (p < 0.05). The SDS-PAGE results showed that all types of proteins of myofibrillar protein were degraded to different degrees, and the degradation was more apparent at ?20℃ than at ?40℃. Therefore, frozen storage at –40℃ has minimal effect on the biochemical characteristics of muscle protein.

关键词

三疣梭子蟹(Portunustrituberculatus)/肌肉/蛋白质/生化特性

Key words

swimming crab (Portunus trituberculatus)/muscle/protein/biochemical properties

分类

轻工纺织

引用本文复制引用

黄琳,张莉,武丹露..三疣梭子蟹(Portunus trituberculatus)冻藏过程中肌肉蛋白质生化特性的变化[J].海洋科学,2017,41(6):41-47,7.

基金项目

Province Natural Science Foundation of Shandong, NO.ZR2015CM010山东省自然科学基金项目(ZR2015CM010) (ZR2015CM010)

海洋科学

OA北大核心CSCDCSTPCD

1000-3096

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