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当前位置: 首页 > 文章 > Fenton体系的优化及其对酪蛋白的氧化作用 食品科学 2014,35 (13) 74-80
Position: Home > Articles > Optimization of Fenton Reaction System and Its Inductive Effect on Casein Oxidation FOOD SCIENCE 2014,35 (13) 74-80

Fenton体系的优化及其对酪蛋白的氧化作用

作  者：
刘建垒;景浩
单  位：
中国农业大学食品科学与营养工程学院
关键词：
酪蛋白;Fenton体系;氧化;优化;化学及结构特性
摘  要：
酪蛋白是乳与乳粉中的主要蛋白组分,在加工和贮藏过程中会发生氧化反应从而影响产品的品质。研究Fenton体系诱导的酪蛋白氧化后化学及结构特性的变化。首先对Fenton体系中Fe2+浓度、抗坏血酸(ascorbic acid,Asc)浓度、H2O2浓度进行了优化,以酪蛋白为靶分子,采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳研究了Fenton体系主要成分以及体系的温度和时间对酪蛋白氧化程度的影响;并进一步研究了氧化后酪蛋白的溶解性、变性程度、总巯基含量及羰基含量的变化。结果表明:当Fenton体系中Fe2+浓度为0.8 mmol/L,EDTANa2浓度为1 mmol/L,H2O2浓度为10 mmol/L,Asc浓度为0.8 mmol/L,酪蛋白质量浓度为5 mg/mL,37℃条件下加热4 h时,酪蛋白氧化程度最明显。随着Fe2+浓度、Asc浓度、H2O2浓度、氧化温度的升高和氧化时间的延长,酪蛋白4个组分条带的密度均逐渐减小,并在相应的高分子区域出现逐渐致密的新条带;但随着酪蛋白质量浓度的升高,酪蛋白条带的变化减小。酪蛋白氧化后,其溶解度和巯基含量显著降低,变性程度和羰基含量显著升高。综上所述,酪蛋白氧化后发生蛋白交联和氨基酸功能基团变化,导致蛋白的变性程度增大以及溶解度下降。
译  名：
Optimization of Fenton Reaction System and Its Inductive Effect on Casein Oxidation
作  者：
LIU Jian-lei;JING Hao;College of Food Science and Nutritional Engineering,China Agricultural University;
关键词：
casein;;Fenton reaction system;;oxidation;;optimization;;chemical and structural properties
摘  要：
Casein consists of about 80% of the proteins of milk or milk powder, which is susceptible to oxidation during food processing and storage. Fenton reaction-induced casein oxidation and the associated chemical and structural changes were investigated. The effects of the main components in the Fenton reaction system as well as reaction temperature and time on casein oxidation were investigated by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE), and the conc entrations of Fe2+, ascorbic acid, and H2O2 were optimized. Fenton reaction-induced casein oxidation and its chemical and structural changes were assessed by changes in solubility, degree of protein denaturation, and total sulfhydryl and carbonyl contents of casein. Results showed that casein was oxidized to a great degree in the Fenton system containing 0.8 mmol/L FeSO4, 1 mmol/L EDTANa2, 10 mmol/L H2O2, 0.8 mmol/L ascorbic acid, 5 mg/mL casein after incubation at 37 ℃ for 4 h. The electrophoretic patterns indicated decreases in band intensity of casein and increases in density of the high molecular weight(HMW) protein bands. These changes were greater with increasing concentrations of Fe2+, ascorbic acid, and H2O2 in the Fenton reaction sy stem as well as temperature and time. Smaller changes in the casein bands were seen with increasing its concentration. Solubility and total sulfhydryl content were decreased, and degree of protein denaturation and carbonyl content were increased after oxidization of casein. In conclusion, casein oxidation leads to cross-linking into high molecular weight(HMW) substances and modifi cation of functional groups of amino acid residues, which consequently results in decreased protein solubility and increased protein denaturation degree.

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