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中国精品科技期刊2020
李丙子, 魏红艳, 雷芸, 陈骋, 张玉斌. 体外孵化模型中乳酸盐对肌红蛋白结构影响的机理[J]. 食品工业科技, 2020, 41(21): 1-7,14. DOI: 10.13386/j.issn1002-0306.2020020148
引用本文: 李丙子, 魏红艳, 雷芸, 陈骋, 张玉斌. 体外孵化模型中乳酸盐对肌红蛋白结构影响的机理[J]. 食品工业科技, 2020, 41(21): 1-7,14. DOI: 10.13386/j.issn1002-0306.2020020148
LI Bing-zi, WEI Hong-yan, LEI Yun, CHEN Cheng, ZHANG Yu-bin. Mechanism of the Effect of Lactate on the Structure of Myoglobin in the in Vitro Hatching Model[J]. Science and Technology of Food Industry, 2020, 41(21): 1-7,14. DOI: 10.13386/j.issn1002-0306.2020020148
Citation: LI Bing-zi, WEI Hong-yan, LEI Yun, CHEN Cheng, ZHANG Yu-bin. Mechanism of the Effect of Lactate on the Structure of Myoglobin in the in Vitro Hatching Model[J]. Science and Technology of Food Industry, 2020, 41(21): 1-7,14. DOI: 10.13386/j.issn1002-0306.2020020148

体外孵化模型中乳酸盐对肌红蛋白结构影响的机理

Mechanism of the Effect of Lactate on the Structure of Myoglobin in the in Vitro Hatching Model

  • 摘要: 为了研究乳酸盐与肌红蛋白(Myogolobin,Mb)血红素辅基的相互作用机制。本试验以牦牛背最长肌为原材料,对牦牛背最长肌中的肌红蛋白进行分离纯化,纯化后加入乳酸钙,在4 ℃条件下贮藏0、12、24、36、72 h,建立体外模型系统,采用紫外-可见吸收光谱、荧光光谱和圆二色光谱测定其在特征峰的吸光度,研究肌红蛋白的结构变化。结果表明紫外-可见光谱在冷藏期间4个时间点409 nm的特征峰处吸收强度都略有增加,但峰位和峰形几乎没变化;荧光光谱在597 nm处发射峰强度减弱,肌红蛋白的铁卟啉环的发射峰位置也未发生位移,但荧光强度随着贮藏时间的延长而减弱;圆二色谱表明对照组和处理组在远紫外区192、208和222 nm 3个特征峰的形状和肩峰的位置未发生明显改变,在190~240 nm处的图谱在乳酸钙处理组中和对照组一样曲线平滑。说明了乳酸盐和Mb的共价加合作用并未发生在血红素辅基上,而是通过非血红素配体结合的方式对肌红蛋白进行调节。

     

    Abstract: In order to study the interaction mechanism between lactate and myoglobin(Mb)heme prosthetic group,the longissimus dorsi was used as the raw material. Mb was separated and purified before adding calcium lactate. It was stored at 4 ℃ for 0,12,24,36,and 72 h,using ultraviolet-visible absorption spectrum,fluorescence spectrum and circular dichroism spectrum to determine the absorbance of the characteristic peak. The results showed that the absorption intensity of the ultraviolet-visible spectrum at the characteristic peak of 409 nm at four time points during refrigeration was slightly increased,but the peak position and peak shape barely changed;the intensity of the emission peak of the fluorescence spectrum at 597 nm weakened. The position of the emission peak of the porphyrin ring of Mb did not shift,but the fluorescence intensity weakened with the extension of storage time;circular dichroism chromatography showed that the shape and shoulder of the three characteristic peaks in the far ultraviolet region of 192,208 and 222 nm in the control and treatment groups The position of the peak did not change significantly,and the pattern at 190~240 nm in the calcium lactate treatment group was smooth like the control group. It shows that the covalent addition of lactate and Mb does not occur on the heme prosthetic group,but regulates myoglobin through non-heme ligand binding.

     

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