尿素对肌原纤维蛋白热诱导凝胶非共价键作用力及特性的影响  

Effect of Urea Addition on Non-Covalent Intermolecular Forces and Properties of Heat-Induced Myofibrillar Protein Gel

作　　者：张兴[1] 杨玉玲[1] 王静宇[1] 张自业 ZHANG Xing;YANG Yuling;WANG Jingyu;ZHANG Ziye(Collaborative Innovation Center for Modern Grain Circulation and Safety, Key Laboratory of Grains and Oils Quality Control and Processing, College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, China)

机构地区：[1]南京财经大学食品科学与工程学院,江苏省现代粮食流通与安全协同创新中心,江苏高校粮油质量安全控制及深加工重点实验室,江苏南京210023

出　　处：《食品科学》2017年第11期12-17,共6页Food Science

基　　金：国家自然科学基金面上项目(31371798);江苏省高校优势学科建设工程项目

摘　　要：研究尿素对肌原纤维蛋白凝胶非共价键作用力和特性的影响及其调控机制,揭示凝胶作用力和特性之间的关系,并探讨通过添加尿素研究凝胶氢键和疏水作用方法的科学性。分别用0.0~0.4 mol/L尿素处理肌原纤维蛋白并加热制成凝胶,用Zeta电位仪测定其静电相互作用;利用拉曼光谱仪测定其疏水相互作用与氢键;用离心法和质构仪测定相应尿素浓度条件下热诱导凝胶的保水性、硬度和弹性。结果表明,随着尿素浓度增大,热诱导凝胶的Zeta电位绝对值由7.83 m V下降到5.55 m V;S_0-ANS从698.5逐渐增大到885.3;I_(760 cm^(-1))/I_(1 003 cm^(-1))由0.957 1降到0.849 3;I_(850 cm^(-1))/I_(830 cm^(-1))先下降后上升;随着尿素浓度增大,凝胶保水性、硬度和弹性都存在下降的现象。相关性分析表明静电相互作用、表面疏水性和疏水相互作用显著影响肌原纤维蛋白热诱导凝胶保水性和质构特性。The effect and regulatory mechanism of urea on the properties and non-covalent intermolecular forces ofheat-induced myofibrillar protein gel were studied.The relationship between intermolecular forces and gel propertieswas explored.This study discussed whether urea addition is a scientific method for studying gel hydrogen bondingand hydrophobic interaction.Heat-induced myofibrillar protein gels containing0.0?0.4mol/L urea were prepared.Theelectrostatic interaction was measured using a zeta potential analyzer.The hydrophobic interaction and hydrogen bondingwere measured using a Raman spectrometer.The water-holding capacity,hardness and springiness of the gels weremeasured by a centrifugation method and a texture analyzer.As urea concentration increased,the absolute value of zetapotential of the gels decreased from7.83to5.55mV,and the surface hydrophobicity(S0-ANS)of myofibrillar proteinincreased from698.5to885.3.The I760cm-1/I1003cm-1ratio(normalized intensity)decreased from0.9571to0.8493,while theI850cm-1/I830cm-1ratio declined first and then increased.The water-holding capacity,hardness and springiness exhibiteda declining trend.Correlation analysis showed that electrostatic interaction,surface hydrophobicity and hydrophobicinteraction had a significant effect on water-holding capacity and texture characteristics of heat-induced protein gel.

关 键 词：肌原纤维蛋白凝胶 尿素 静电相互作用 疏水相互作用 氢键 

分 类 号：TS201.2[轻工技术与工程—食品科学]