Faist V, Müller C, Drusch S, Erbersdobler H F
University of Kiel, Institute for Human Nutrition and Food Science, Duesternbrooker Weg 17, D-24105 Kiel, Germany.
Nahrung. 2001 Jun;45(3):218-21. doi: 10.1002/1521-3803(20010601)45:3<218::AID-FOOD218>3.0.CO;2-Q.
In the present study, a promising strategy to study nutritional effects of selected chemical reaction products formed in heat treated protein containing foods is addressed. In due course, a selective fortification of different marker compounds for lysine damage in casein-sugar mixtures was performed to provide model systems being applicable to investigate biological effects of the cross-link lysinoalanine (LAL), the MRPs fructoselysine (FL) and N epsilon-carboxymethyllysine (CML) in a casein-linked preparation. The three different model proteins, casein-LAL, casein-FL and casein-CML were prepared by heating casein either in strong alkaline conditions at 105 degrees C for 1 h, in the presence of glucose at 65 degrees C for 68 h, or in the presence of glyoxylic acid at 37 degrees C for 19 h. Finally, the degree of lysine modification achieved was 39%, 75% and 55% for the casein-LAL, casein-FL and casein-CML, respectively. The calculation of lysine recovery and the respective analysis of each single modified casein (LAL-, FL- and CML-MP) for the selected fortified compound and each other compound vice versa proved that the individual procedure provides a specific fortification for LAL, FL and CML, respectively. The modified proteins are suitable as reference model proteins to be investigated for specific biological and toxicological effects of casein-linked LAL, FL and CML.
在本研究中,探讨了一种有前景的策略,用于研究热处理含蛋白质食品中形成的特定化学反应产物的营养效应。在适当的时候,对酪蛋白-糖混合物中赖氨酸损伤的不同标记化合物进行了选择性强化,以提供适用于研究交联赖氨酰丙氨酸(LAL)、美拉德反应产物果糖赖氨酸(FL)和N-ε-羧甲基赖氨酸(CML)在酪蛋白连接制剂中的生物学效应的模型系统。通过在105℃的强碱性条件下加热酪蛋白1小时、在65℃的葡萄糖存在下加热68小时或在37℃的乙醛酸存在下加热19小时,制备了三种不同的模型蛋白,即酪蛋白-LAL、酪蛋白-FL和酪蛋白-CML。最后,酪蛋白-LAL、酪蛋白-FL和酪蛋白-CML的赖氨酸修饰程度分别为39%、75%和55%。对选定强化化合物以及反之对其他每种化合物的赖氨酸回收率计算和对每种单一修饰酪蛋白(LAL-、FL-和CML-MP)的相应分析证明,该单独程序分别为LAL、FL和CML提供了特异性强化。修饰后的蛋白质适合作为参考模型蛋白,用于研究酪蛋白连接的LAL、FL和CML 的特定生物学和毒理学效应。