氧化及不同离子强度下猪肉肌原纤维蛋白结合风味物质的研究

甘潇; 赵玲; 吴倩; 陈希文

doi:10.13386/j.issn1002-0306.2022010139

氧化及不同离子强度下猪肉肌原纤维蛋白结合风味物质的研究

doi: 10.13386/j.issn1002-0306.2022010139

甘潇^{1, 2,},
赵玲¹,
吴倩^{1, 2},
陈希文^{1, 2, ,}

1.
绵阳师范学院生命科学与技术学院，四川绵阳 621000
2.
动物疫病防控与健康养殖工程技术研究中心，四川绵阳 621000

基金项目: 川菜发展研究中心项目（CC20Z21）；绵阳师范学院科研启动项目（QD2020A16）。

详细信息

作者简介:
甘潇（1980−），女，博士，副教授，研究方向：肉品科学与食品发酵，E-mail：26624899@qq.com

通讯作者:
陈希文（1977−），男，博士，教授，研究方向：动物健康养殖与有害残留物监测，E-mail：327276060@qq.com

中图分类号: TS251.1
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- 文章访问数: 91
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- 被引次数: 0
出版历程
- 收稿日期: 2022-01-18
- 网络出版日期: 2022-10-20
- 刊出日期: 2022-11-23

Effects of Oxidation and Different Ionic Environment on the Binding of Pork Myofibrillar Protein to Flavor Substances

GAN Xiao^{1, 2
,},
ZHAO Ling¹,
WU Qian^{1, 2},
CHEN Xiwen^{1, 2
, ,}

1.
School of Life Science & Technology, Mianyang Teachers’ College, Mianyang 621000, China
2.
Engineering Technology Research Center of Animal Disease Control and Healthy Breeding, Mianyang 621000, China

摘要

摘要: 文章研究了猪肉肌原纤维蛋白氧化导致其结构功能发生改变及氧化和不同离子条件下其结合风味物质的能力变化。实验选择了2-甲基丁醛、3-甲基丁醛、己醛、辛醛、壬醛等5种风味物质，利用顶空结合气相色谱观察肌原纤维蛋白结合风味物质的能力。结果表明：经氧化的肌原纤维蛋白二级结构及功能发生了变化。氧化处理的肌原纤维蛋白对2-甲基丁醛和壬醛有促释放的作用，对3-甲基丁醛、己醛和辛醛的作用呈2,2-偶氮二(2-甲基丙基咪)二盐酸盐（AAPH）浓度依赖性。Na⁺的添加促进了氧化蛋白对己醛的释放，而Na⁺、K⁺、Ca²⁺和Mg²⁺的添加促进了氧化蛋白对2-甲基丁醛、3-甲基丁醛、辛醛和壬醛的吸收。因此，在肉及肉制品的加工贮藏过程，氧化易造成蛋白结构和功能的改变，进而影响蛋白质结合风味物质的能力；另外，氯化钠在肉制品中被其它盐部分替代造成蛋白质所处的离子环境发生改变，导致蛋白质结合风味物质的能力改变，从而使肉制品风味发生改变。
- 猪肉 /
- 肌原纤维蛋白 /
- 氧化 /
- 顶空进样 /
- 气相色谱
Abstract: The changes of structure and function of pork myofibrillar protein induced by oxidation and its ability to bind flavor substances under different ionic conditions were studied. 2-methyl-butanal, 3-methyl-butanal, hexanal, octanal and nonanal were selected as volatile compounds in the experiment. The ability of myofibrillar protein to bind volatile compounds was observed by headspace combined gas chromatography. The results confirmed that the secondary structure and function of oxidized myofibrillar protein changed. Oxidized myofibrillar protein could promote the release of 2-methyl-butanal and nonanal. Moreover, the effect of oxidized myofibrillar protein on 3-methyl-butanal, hexanal and octanal was dependent on AAPH concentration. The addition of Na⁺ promoted the release of hexanal, while the addition of Na⁺, K⁺, Ca²⁺ and Mg²⁺ promoted the absorption of 2-methyl-butanal, 3-methyl-butanal, octanal and nonal. Consequently, during the processing and storage of meat and meat products, oxidation of meat protein could change its structure and function, and then affect the ability of protein to combine flavor substances. In addition, sodium chloride is partially replaced by other salts in meat products, resulting in changes in the ionic environment of proteins, resulting in changes in the ability of proteins to combine flavor substances, thus changing the flavor of meat products.
- pork /
- myofibrillar protein /
- oxidation /
- headspace sampling /
- gas chromatography

HTML全文

图 1 氧化处理MP羰基含量的变化

Figure 1. Changes in carbonyl content of MP upon oxidation

注：不同字母代表差异显著，P<0.05；图2、图4~图5同。

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图 2 氧化处理MP巯基含量的变化

Figure 2. Changes in sulfhydryl content of MP upon oxidation

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图 3 氧化处理MP色氨酸荧光的变化

Figure 3. Changes in tryptophan fluorescence of MP upon oxidation

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图 4 氧化处理MP表面疏水性的变化

Figure 4. Changes in protein surface hydrophobicity of MP upon oxidation

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图 5 氧化处理MP可溶性的变化

Figure 5. Changes in solubility of MP upon oxidation

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图 6 氧化对MP结合特征风味物质能力的影响

Figure 6. Effect of oxidation on the ability of MP to bind characteristic flavor substances

注：不同字母代表同一物质组间差异显著（P<0.05）；图7同。

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图 7 不同Na⁺、K⁺ 、Ca²⁺、Mg²⁺浓度对氧化处理的MP结合风味物质能力的影响

Figure 7. Effects of different sodium, potassium, calcium and magnesium concentrations on the flavor substances of oxidized MP binding properties

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