食品与发酵工业 >

2020 , Vol. 46 >Issue 20: 1 - 8

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.024414

研究报告

不同超声辅助解冻方式对海鲈鱼肌原纤维蛋白的影响

  • 蔡路昀 ,
  • 许晴 ,
  • 曹爱玲
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  • 1(浙江大学 宁波研究院, 浙江 宁波,315100);
    2(浙江大学 生物系统工程与食品科学学院,智能食品技术与装备国家与地方联合工程实验室,浙江 杭州,310058);
    3(杭州海关,浙江 杭州,311208)
博士,副教授(本文通讯作者,E-mail:cailuyun@zju.edu.cn)

收稿日期: 2020-05-10

  修回日期: 2020-06-11

  网络出版日期: 2020-11-12

基金资助

国家重点研发计划(2018YFD0901106);国家自然科学基金项目(31401478)

收起

Effects of different ultrasound-assisted thawing methods on the myofibrillar protein of the sea bass (Perca fluviatilis)

  • CAI Luyun ,
  • XU Qing ,
  • CAO Ailing
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  • 1(Ningbo Research Institute, Zhejiang University, Ningbo 315100, China);
    2(College of Biosystems Engineering and Food Science, National & Local Joint Engineering Laboratory of Intelligent Food Techology and Equipment, Zhejiang University, Hangzhou 310058, China);
    3(Hangzhou Customs, Hangzhou 311208, China)

Received date: 2020-05-10

  Revised date: 2020-06-11

  Online published: 2020-11-12

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摘要

从蛋白质的结构、聚集程度和氧化程度方面,探究不同解冻方式(超声微波解冻、超声远红外解冻、超声欧姆解冻、超声真空解冻和超声解冻)对海鲈鱼肌原纤维蛋白理化性质的影响,以期从分子水平上初步了解不同解冻方式引起肌原纤维蛋白变性的机理。蛋白质的结构变化通过拉曼光谱、紫外吸收光谱和内源荧光光谱来监测。拉曼光谱结果表明,所有解冻方式中超声微波解冻的α-螺旋含量最高,有效地维持了蛋白质结构。紫外吸收光谱和内源荧光光谱表明,超声微波解冻能较好地保留蛋白质的三级结构,而超声解冻的蛋白质结构受损严重。粒径、Zeta电位和十二烷基磺酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate polyacrylamide gel electrophoresis,SDS-PAGE)可以分析蛋白质的聚集程度。与新鲜样品相比,所有解冻方式的粒径和Zeta电位均无显著差异(P>0.05)。超声微波解冻的电泳条带与新鲜样品最接近,这表明蛋白质降解程度较低。总巯基含量和溶解度可以反映蛋白质的氧化程度。超声远红外解冻和超声微波解冻的总巯基含量与新鲜样品最接近,超声真空的溶解度与新鲜样品最接近。综上所述,超声微波解冻能较好地维持肌原纤维蛋白的理化性质。

关键词： 海鲈鱼; 超声解冻; 蛋白质结构; 蛋白质聚集; 蛋白质氧化

本文引用格式

蔡路昀 , 许晴 , 曹爱玲 . 不同超声辅助解冻方式对海鲈鱼肌原纤维蛋白的影响[J]. 食品与发酵工业, 2020 , 46(20) : 1 -8 . DOI: 10.13995/j.cnki.11-1802/ts.024414

Abstract

The effects of different thawing methods (ultrasonic microwave thawing, ultrasonic far-infrared thawing, ultrasonic ohmic thawing, ultrasonic vacuum thawing, and ultrasound thawing) on the physicochemical properties of the myofibrillar protein in sea bass were investigated from the protein structure, aggregation degree and oxidation degree. The structural changes of the myofibrillar protein were monitored by Raman spectra, ultraviolet absorption spectra and intrinsic fluorescence spectra. These indicators could help to preliminarily understand the mechanism of myofibrillar protein denaturation caused by different thawing methods at the molecular level. The result of Raman spectra showed that the content of α-helix thawed by ultrasonic microwave thawing was the highest among all thawing methods, which maintaining the protein structure effectively. The ultraviolet absorption spectra and intrinsic fluorescence spectra showed that the ultrasonic microwave thawing could retain the tertiary structure of the protein better, but the structure of the protein thawed by ultrasound was seriously damaged. Particle size, Zeta potential and SDS-PAGE were used to analyze the degree of protein aggregation. Compared with the fresh sample, the particle size and Zeta potential of all the thawing methods were no significantly difference (P>0.05). The electrophoretic band of ultrasonic microwave thawing was the closest to the fresh sample, which indicated the degradation degree of the protein was lower. The contents of total sulfhydryl by ultrasonic far-infrared thawing and ultrasonic microwave thawing were closest to that of the fresh sample, and the solubility by ultrasonic vacuum thawing was the closest to that of the fresh sample. In summary, ultrasonic microwave thawing method is the best to maintain the physicochemical properties of myofibrin.

Key words： sea bass; ultrasound thawing; protein structures; protein aggregation; protein oxidation

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