食品科学

• 基础研究 • 上一篇    下一篇

超高压处理对凡纳滨对虾原肌球蛋白构象的影响

胡志和,张晴青,吴子健,薛 璐,贾 莹,王星璇   

  1. 天津商业大学生物技术与食品科学学院,天津市食品生物技术重点实验室,天津 300134
  • 出版日期:2016-12-15 发布日期:2016-12-21

Effect of Ultra-High Pressure Treatment on Tropomyosin Conformation in Litopenaeus vannamei

HU Zhihe, ZHANG Qingqing, WU Zijian, XUE Lu, JIA Ying, WANG Xingxuan   

  1. Tianjin Key Laboratory of Food Biotechnology, School of Biotechnology and Food Science,Tianjin University of Commerce, Tianjin 300134, China
  • Online:2016-12-15 Published:2016-12-21

摘要: 以凡纳滨对虾的原肌球蛋白(tropomyosin,TM)为原料,研究不同超高压条件下引发的TM构象变化。采用压力0.1~800 MPa,处理时间10~40 min,温度10~37 ℃处理TM,圆二色光谱法检测其二级结构变化,荧光光度法检测其荧光强度变化,DNA Star Protean软件预测可塑性。结果显示,超高压处理对TM的二级结构无显著影响,不同超高压条件下TM三级结构有显著变化。在实验压力范围内,300 MPa处理的TM疏水性氨基酸暴露程度最小;700 MPa处理后暴露程度最高。经预测,TM的可塑性区域占总氨基酸序列的72.9%。因此,超高压条件下TM的二级结构稳定,三级结构变化较大,三级结构的变化可能与其可塑性区域的比例较高有关。

关键词: 原肌球蛋白, 超高压处理, 蛋白质结构, 圆二色光谱, 荧光光谱

Abstract: The objective of this paper was to explore the effect of ultra-high pressure treatmnet on tropomyosin (TM)
conformation in Litopenaeus vannamei. After being treated under different conditions (pressure: 0.1–800 MPa; holding
time: 10–40 min; temperature: 10–37 ℃), the secondary and tertiary structure of TM was tested by circular dichroism (CD)
spectroscopy and fluorospectrophotometry, and the flexible region was predicted using DNA Star Protean software. Results
showed that the secondary structure of TM did not change significantly, while the tertiary structure significantly changed
after ultra-high pressure treatment. In the pressure range tested, the number of surface-exposed hydrophobic amino acids in
TM was the smallest at 300 MPa, and was the largest at 700 MPa. The flexible region in TM accounted for 72.9% of the total
amino acid sequence. Therefore, the secondary structure of TM was stable and the tertiary structure was unstable after ultrahigh
pressure treatment. The tertiary structure change of TM may be related to its higher proportion of flexibile region.

Key words: tropomyosin, ultra-high prssure treatment, protein conformation, circular dichroism spectroscopy, fluorospectrophotometry

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