食品科学 ›› 2021, Vol. 42 ›› Issue (1): 124-131.doi: 10.7506/spkx1002-6630-20191105-052

• 食品工程 • 上一篇    下一篇

二次杀菌对贮藏期间酱卤羊肚肌原纤维蛋白氧化、特性及结构的影响

侯然,赵伟,卢士玲,韩平,刘璐,艾延文,董娟   

  1. (1.石河子大学食品学院,新疆 石河子 832000;2.江南大学食品学院,江苏 无锡 214000)
  • 发布日期:2021-01-18
  • 基金资助:
    国家自然科学基金地区科学基金项目(31660480);石河子大学高层次人才科研启动项目(RCSX201714)

Effect of Secondary Sterilization on Oxidation, Characteristics and Structure of Myofibrillar Protein in Sauced Sheep Tripe during Storage

HOU Ran, ZHAO Wei, LU Shiling, HAN Ping, LIU Lu, AI Yanwen, DONG Juan   

  1. (1. The Food College, Shihezi University, Shihezi 832000, China;2. School of Food Science and Technology, Jiangnan University, Wuxi 214000, China)
  • Published:2021-01-18

摘要: 为了探明超高压处理和热处理对酱卤羊肚肌原纤维蛋白氧化、特性及结构的影响。本实验以未经二次杀菌处理的样品为空白(CN),对酱卤羊肚分别进行400 MPa、15 min超高压处理(ultra-high pressure treatment,UHPT)和85 ℃水浴40 min热处理(heat treatment,HT),真空包装后4 ℃条件下贮藏,通过测定肌原纤维蛋白羰基含量、总巯基含量、蛋白组成、溶解度和浊度,分析两种二次杀菌方式对蛋白氧化及特性的影响;同时采用光谱法(紫外吸收光谱、内源荧光光谱和拉曼光谱)对蛋白结构进行分析。结果表明:贮藏初期经过超高压和热处理后的肌原纤维蛋白羰基含量均上升更快,并且UHPT组整体高于HT组。贮藏期间各组总巯基含量呈先下降后上升的趋势,并且相比CN组,HT组和UHPT组在贮藏前期下降速率更快,十二烷基硫酸钠-聚丙烯酰胺凝胶电泳结果表明,二次杀菌后,主要受到影响的蛋白为肌动蛋白和原肌球蛋白。超高压和热处理均会显著提高蛋白浊度(P<0.05),但超高压处理的影响较小。光谱分析表明,两种二次杀菌方式均使色氨酸残基向非极性环境转移,并且α-螺旋相对含量降低、无规卷曲相对含量增加、折叠比上升,且随贮藏时间的延长,结构产生了有序到无序的转变。相关性分析表明:贮藏时间与总巯基含量、溶解度、α-螺旋相对含量具有显著相关性,并且蛋白氧化与蛋白特性和结构之间存在一定的相关性。超高压作为二次杀菌方式在尽可能保证贮藏期间酱卤羊肚的品质的同时具有更大的优势。

关键词: 超高压;热处理;蛋白氧化;酱卤羊肚;肌原纤维蛋白

Abstract: In order to investigate the effects of ultra-high pressure (UHP) and heat treatment on the oxidation, characteristics and structure of myofibrillar protein in sauced sheep tripe, samples were subjected to ultra-high pressure treatment (UHPT) with 400 MPa for 15 min or heat treatment (HT) in water bath at 85 ℃ for 40 min, packaged in vacuum and stored at 4 ℃. An untreated sample was used as a control. The effect of the treatments on myofibrillar protein oxidation and properties was evaluated through measuring carbonyl content, total sulfhydryl content, protein composition, solubility and turbidity. The protein structure was analyzed by ultraviolet absorption spectroscopy, endogenous fluorescence spectroscopy and Raman spectroscopy. The results showed that the carbonyl content of both the treated samples increased faster in the early storage period than did the control, and in general a higher level was observed in the UHPT group in comparison with the HT group. During storage, total sulfhydryl content decreased first and then increased for all groups, and dropped faster in the early storage period in both treatment groups compared with the control group. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that secondary sterilization mainly affected actin and tropomyosin. Both treatments significantly affected the turbidity of myofibrillar protein solution (P < 0.05) with the effect of UHP being weaker. Spectral analysis showed that both treatments transferred tryptophan residues to a non-polar environment, resulting in a decrease in the relative content of α-helix and an increase in the relative content of random coil and folding ratio. The treated protein was transformed from an ordered to a disordered state with the prolongation of storage time. Correlation analysis showed that storage time was significantly correlated with total sulfhydryl content, solubility, and the relative contents of α-helix, and protein oxidation was correlated with protein properties and structure. UHP was more advantageous in preserving the quality of sauced sheep tripe during storage.

Key words: ultra-high pressure; heat treatment; protein oxidation; sauced sheep tripe; myofibrillar protein

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