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当前位置: 首页 > 文章 > 糖基化对β-乳球蛋白结构的影响 食品科学 2015,36 (15) 75-80
Position: Home > Articles > Effect of Glycation on Structural Properties of β-Lactoglobulin FOOD SCIENCE 2015,36 (15) 75-80

糖基化对β-乳球蛋白结构的影响

作  者：
李晓明;孔阳辉;吕丽爽
单  位：
南京师范大学金陵女子学院
关键词：
β-乳球蛋白;圆二色谱;二羰基化合物;结构
摘  要：
目的:考察还原糖以及活性二羰基化合物诱导的β-乳球蛋白(β-lactoglobulin,β-lg)发生糖基化后结构的变化。方法:运用气相色谱法检测β-乳球蛋白+乳糖糖基化反应体系中二羰基化合物的产生,并通过紫外-可见分光光度法、圆二色谱法、体积排阻色谱法定性分析不同活性羰基引发糖基化反应对β-lg结构的改变。结果:β-乳球蛋白+乳糖糖基化反应体系可以迅速产生二羰基化合物,在125℃条件下,30 min后,丙酮醛和乙二醛含量高达207μg/g和180μg/g,而后逐渐减少并趋于稳定(150μg/g)。光谱学实验结果表明,还原糖以及活性二羰基化合物可以有效地诱导β-lg结构从β-折叠转变为α-螺旋;通过体积排阻色谱实验,β-lg加热糖基化后在120~190 min有新的产物色谱峰产生。结论:还原糖和活性二羰基化合物能有效地诱导β-lg糖基化反应,引起其蛋白二级结构的改变。
译  名：
Effect of Glycation on Structural Properties of β-Lactoglobulin
作  者：
LI Xiaoming;KONG Yanghui;Lü Lishuang;Ginling College, Nanjing Normal University;
关键词：
β-lactoglobulin;;circular dichroism;;dicarbonyl compounds;;structure
摘  要：
Purposes: To study the structural changes of β-lactoglobulin(β-lg) after glycation induced by reducing sugar or dicarbonyl compounds. Methods: The content of dicarbonyl compounds produced from β-lg and lactose was determined by gas chromatography. The structural changes of β-lg caused by glycation initiated by different active carbonyl groups were evaluated by ultraviolet(UV)-visible spectrophotometry, circular dichroism and size exclusion chromatography. Results: Dicarbonyl compounds were produced by β-lg glycation. The contents of methylglyoxal and glyoxalall reached the highest levels at 207 μg/g and 180 μg/g respectively after heating for 30 minutes. Then, the quantity of dicarbonyl compounds began to decline, and remained at approximately 150 μg/g. The UV-visible and circular dichroism spectra showed effective transformation of β-sheet to α-helix induced by glycation. By Sephadex G-75 sizeexclusion chromatography, a new absorption peak was detected between 120 and 190 min, indicating the occurrence of β-lg glycation. Conclusion: Reducing sugar and dicarbonyl compounds have a very strong role in β-lg glycation reaction and consequently may change the structure of β-lg significantly.

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