酶解-磷酸化协同改性对猪血红蛋白功能特性和结构的影响  

Effects of Synergistic Enzymatic-Phosphorylation Modification on the Functional Properties and Structure of Porcine Haemoglobin

作　　者：苏克楠 刘丽莉[1] 杨乐 王梦雨 SU Kenan;LIU Lili;YANG Le;WANG Mengyu(College of food and Bioengineering,Henan University of science and technology,National Experimental Teaching Demonstration Center for Food Processing and Security,Henan International Joint Laboratory of food processing and quality and safety control,Luoyang,Henan 471023)

机构地区：[1]河南科技大学食品与生物工程学院/食品加工与安全国家级教学示范中心/食品加工与质量安全控制河南省国际联合实验室,河南洛阳471023

出　　处：《核农学报》2023年第10期2028-2033,共6页Journal of Nuclear Agricultural Sciences

基　　金：2021年洛阳市社会发展专项(2101021A);国家自然科学基金项目(U1704114);河南省重大科技专项(221100110500);国家级大学生创业计划训练项目(202210464032)。

摘　　要：为改善猪血红蛋白(Hb)的功能特性,探究协同改性对猪血红蛋白的影响,本研究以猪血红蛋白和猪血红蛋白肽(H-Hb)为对照,采用酶解-磷酸化协同改性(HP)的方法对猪血红蛋白进行处理,并对协同改性后酶解-磷酸化猪血蛋白(HP-Hb)的功能特性和结构进行了研究。功能特性分析表明,与Hb和H-Hb相比,HP-Hb的溶解度明显提高,乳化活性指数提高了12.42和6.30 m^(2)·g^(-1)(P<0.05),乳化稳定性提高了6.37%和3.04%(P<0.05),起泡性提高了7.59%、4.42%(P<0.05),起泡稳定性提高了3.93%和4.42%(P<0.05)。结构分析表明,与Hb和H-Hb相比,酶解使HP-Hb的肽链断裂,暴露更多氨基酸基团,磷酸根大部分连接在N原子上,P-N和PO43-的增加使部分红外吸收峰变强;同时其热变性温度分别提高了14.00和20.67℃。微观结构分析表明,协同改性使蛋白结构发生了变化,分子结构由紧密的块状结构变成松散的块状结构,周围有较小的颗粒杂乱分布。综上,协同改性是一种较为可行的修饰方法,处理后的猪血红蛋白的功能特性和稳定性得到提升。本研究为猪血红蛋白的改性提供了新思路,为猪血红蛋白在食品加工中的应用研究提供了理论基础及参考。In order to improve the functional properties of porcine hemoglobin(Hb)and enhance product value,this study employed an enzymatic-phosphorylation(HP)method for the modification of porcine hemoglobin.To investigate the effects of the synergistic modification on porcine hemoglobin,porcine hemoglobin and enzymedigested porcine hemoglobin peptides(H-Hb)were used as control groups,and the functional properties and structure of the enzymatic-phosphorylated porcine hemoglobin(HP-Hb)were studied.The analysis of functional properties showed that compared to the control groups,the solubility of HP-Hb was significantly improved with an increased emulsion activity index of 12.42 and 6.30 m^(2)·g^(-1)(P<0.05),as well as increased emulsion stability of 6.37%and 3.04%(P<0.05).The foamability of HP-Hb increased by 7.59%and 4.42%compared to the control groups(P<0.05),and the foam stability increased by 3.93%and 4.42%(P<0.05).Structural analysis showed that enzymatic digestion caused peptide chain breakage in HP-Hb,exposing more amino acid groups.Most of the phosphate groups were linked to the N atoms,and the increased presence of P-N and PO43-resulted in stronger infrared absorption peaks.Furthermore,the thermal stability of HP-Hb was significantly improved by 14.00 and 20.67℃compared to H-Hb and Hb,respectively.Microstructural analysis revealed that dual modification caused a change in protein structure,transforming the molecular structure from compact block-like structure to loosely arranged blocks with smaller particle dispersion.Overall,the results indicated that HP dual modification was a feasible modification method to enhance the functional properties and stability of porcine hemoglobin.This study provides new insights for the modification of porcine hemoglobin and serves as a theoretical basis and reference for further research on the application of porcine hemoglobin in food processing.

关 键 词：猪血红蛋白 酶解 磷酸化 功能特性 结构分析 

分 类 号：TS251.93[轻工技术与工程—农产品加工及贮藏工程]