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食品与发酵工业  2021, Vol. 47 Issue (16): 72-77    DOI: 10.13995/j.cnki.11-1802/ts.027553
  研究报告 本期目录 | 过刊浏览 | 高级检索 |
精氨酸对反复冻融肌原纤维蛋白结构及凝胶性能的调控
邓文辉1, 韩馨蕊2, 常露2, 李朝蕊2, 刘子萌2, 曹云刚2*
1(陕西理工大学 体育学院,陕西 汉中,723000)
2(陕西科技大学 食品与生物工程学院,陕西 西安,710021)
Regulation mechanism of arginine on the structure and gelling properties of myofibrillar protein treated with repeated freezing-thawing
DENG Wenhui1, HAN Xinrui2, CHANG Lu2, LI Zhaorui2, LIU Zimeng2, CAO Yungang2*
1(College of Physical Education, Shaanxi University of Science and Technology, Hanzhong 723000, China)
2(School of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi′an 710021, China)
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摘要 研究添加不同浓度L-精氨酸(L-arginine,L-Arg,0.0、1.0、3.0、5.0 和 10.0 mmol/L)对反复冻融肌原纤维蛋白(myofibrillar protein,MP)理化性质以及胶凝行为的影响,为合理调控冷冻损伤肉蛋白凝胶性能提供理论依据。采用圆二色谱和内源性色氨酸荧光探究L-精氨酸处理对反复冻融MP二级和三级结构的影响;通过测定粒度和溶解度反映L-精氨酸处理对MP聚集情况的影响;借助流变仪和物性测试仪等探究L-精氨酸处理对MP凝胶性能的影响。结果表明,L-Arg处理显著改变了反复冻融MP的空间结构,主要表现为α-螺旋含量的显著上升;L-Arg处理降低了反复冻融MP的粒径,显著提高了其溶解度和凝胶得率,但明显降低了储能模量、凝胶强度和凝胶白度,L-Arg浓度越高对MP凝胶性能的影响越大。因此,单独采用L-Arg处理可以显著提高反复冻融MP的凝胶得率,但会明显降低其凝胶强度。
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邓文辉
韩馨蕊
常露
李朝蕊
刘子萌
曹云刚
关键词:  肌原纤维蛋白  反复冻融  L-精氨酸  圆二色谱  流变性能  凝胶性能    
Abstract: The effects of different concentrations of L-arginine (L-Arg, 0.0, 1.0, 3.0, 5.0 and 10.0 mmol/L) on the physicochemical properties and gelation behavior of repeatedly freeze-thawed myofibrillar protein (MP) were studied in order to provide a theoretical basis for the reasonable regulation of gelling properties of freezing damaged meat proteins. The effects of L-Arg at different concentrations on the secondary and tertiary structures of repeatedly freeze-thawed MP were investigated by circular dichroism spectroscopy and intrinsic tryptophan fluorescence of proteins, respectively. The changes of aggregation of MP with L-Arg treatments were analyzed via the test of particle size and solubility. And the effects of L-Arg treatments on the gelling properties of MP were investigated by rheometer and physical property tester. The results revealed that L-Arg significantly changed the spatial structure of repeated freezing thawing MP, mainly manifested as a significant increase in the content of alpha helix. The addition of L-Arg decreased the particle size of repeatedly freeze-thawed MP, significantly increased the solubility and cooking yield, and obviously reduced the storage modulus (G′), gel strength and gel whiteness. The higher the L-Arg concentration, the greater the impact of L-Arg on the gel performance of repeatedly freeze-thawed MP. Therefore, the treatment with L-Arg alone significantly improved the cooking yield of repeatedly freeze-thawed MP, while remarkably reduced the gel strength.
Key words:  myofibrillar protein    freezing-thawing    L-arginine    circular dichroism    rheological properties    gelling properties
收稿日期:  2021-04-06      修回日期:  2021-04-26                发布日期:  2021-09-10      期的出版日期:  2021-08-25
基金资助: 陕西省科技厅自然科学基础研究计划项目(2019JQ-397);陕西省教育厅专项科研项目(15JK1114);陕西省体育局常规科研项目(2020037)
作者简介:  硕士,副教授(曹云刚副教授为通讯作者,E-mail: caoyungang@sust.edu.cn)
引用本文:    
邓文辉,韩馨蕊,常露,等. 精氨酸对反复冻融肌原纤维蛋白结构及凝胶性能的调控[J]. 食品与发酵工业, 2021, 47(16): 72-77.
DENG Wenhui,HAN Xinrui,CHANG Lu,et al. Regulation mechanism of arginine on the structure and gelling properties of myofibrillar protein treated with repeated freezing-thawing[J]. Food and Fermentation Industries, 2021, 47(16): 72-77.
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http://sf1970.cnif.cn/CN/10.13995/j.cnki.11-1802/ts.027553  或          http://sf1970.cnif.cn/CN/Y2021/V47/I16/72
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