摘要
从中式香肠中提取肌浆蛋白和肌原纤维蛋白,并测定其羰基值、巯基值和蛋白浊度,以及蛋白质降解情况和溶解性,确定蛋白氧化对蛋白聚集性、水解性和溶解性的影响。研究结果表明:蛋白羰基含量都显著增长,巯基含量显著下降。蛋白氧化导致蛋白溶液浊度上升,蛋白表面疏水性增加,以及蛋白发生不同程度的降解。蛋白溶解性实验表明氢键、疏水作用力、二硫键和离子键是形成香肠蛋白三维网状结构的主要作用力。
Sarcoplasmic proteins and myofibrillar proteins were extracted from Chinese sausage. Protein carbonyl, sulfydryl group contents and protein turbidity, protein degradation and solubility were measured and the effect of protein oxidation on aggregation, proteolysis and solubility during drying process was studied. The protein carbonyl content was increased and SH group number was decreased. Protein turbidity and Surface hydrophobicity (H0) in- creased, which was associated with the degree of protein oxidation. Proteolytic susceptibility was influenced by the de- gree of protein oxidation. The protein solubility determinations suggested that hydrogen bonds, hydrophobic interac- tions, disulphide bonds and ionic bonds are the main bonds in forming three-dimensional network structure of sausage proteins.
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2014年第7期193-198,共6页
Food and Fermentation Industries
基金
国家自然科学基(31371792)
江苏省高校自然科学研究项目(12KJD550006)
江苏省科技计划项目(BE2013390)
南通市科技计划项目(HL2013007)
扬州市科技攻关专项(2012069
yz2012070)
关键词
香肠
蛋白
氧化
微观作用力变化
sausage, protein, oxidation, micro force changes