酶解—磷酸化协同改性猪血红蛋白制备工艺优化及特性分析  

Optimization of preparation process and characteristics analysis of porcine hemoglobin modified by enzymatic hydrolysis-phosphorylation

作　　者：苏克楠 刘丽莉[1,2,3,4] 程伟伟 丁玥 徐宝成 SU Kenan;LIU Lili;CHENG Weiwei;DING Yue;XU Baocheng(School of Food and Biotechnology,Henan University of Science and Technology,Luoyang,Henan 471023,China;National Teaching Demonstration Center for Food Processing and Safety,Luoyang,Henan 471023,China;Henan International Joint Laboratory of Food Processing and Quality Safety Control,Luoyang,Henan 471023,China;Henan Engineering Technology Research Center for Food Microbiology,Luoyang,Henan 471023,China)

机构地区：[1]河南科技大学食品与生物工程学院,河南洛阳471023 [2]食品加工与安全国家级教学示范中心,河南洛阳471023 [3]河南省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 [4]食品微生物河南省工程技术研究中心,河南洛阳471023

出　　处：《食品与机械》2024年第9期36-43,共8页Food and Machinery

基　　金：河南省科技攻关专项(编号:242102110092);河南省重大科技攻关项目(编号:221100110500);洛阳市科技攻关项目—公益项目(编号:2101021A)。

摘　　要：[目的]为高值化利用猪血,提升猪血红蛋白(hemoglobin pig,Hb)的应用范围。[方法]对Hb进行了酶解—磷酸化协同改性,并探索最佳制备条件及特性变化。采用响应面试验确定最优参数,研究协同改性对猪血红蛋白(enzymatic hydrolysis-phosphorylation of porcine hemoglobin,HP-Hb)的影响。[结果]磷酸化的最优参数为磷酸盐添加量10 g/100 mL、pH 9、猪血红蛋白肽(pig hemoglobin peptide,H-Hb)添加量8 g/100 mL、反应时间2.1 h。与Hb和H-Hb相比,HP-Hb的乳化性能和抗氧化性显著提升,电泳结果表明,相对分子质量并无明显变化。结构分析表明磷酸根大部分接入在N原子上;二级结构的变化,增强了HP-Hb的结构稳定性;HP-Hb的热稳定性增强,而其微观结构更加松散。[结论]酶解—磷酸化协同改性处理明显改善了猪血红蛋白的乳化性能、抗氧化性能和热稳定性,说明协同改性是一种较为可行的改善蛋白质的方法。[Objective]This study aimed to make high-value use of pig blood and improve the application range of pig hemoglobin(Hb).[Methods]Hb was modified by enzymolysis and phosphorylation,and its optimum preparation conditions and characteristics were explored.The optimal parameters were determined by response surface test to study the effect of enzymatic hydrolysis-phosphorylation of porcine hemoglobin(HP-Hb).[Results]The optimal parameters for phosphorylation were 10 g/100 mL phosphate addition,pH 9,8 g/100 mL pig hemoglobin peptide(pig hemoglobin peptide,H-Hb)addition,and a reaction time of 2.1 hours.Compared with Hb and H-Hb,HP-Hb showed significantly improved emulsification properties and antioxidant activity.Electrophoresis results indicated no significant change in molecular weight.Structural analysis revealed that the phosphate groups were mostly attached to the N atoms.The change of secondary structure of HP-Hb enhanced its structural stability.[Conclusion]Enzymolysis phosphorylation co-modification significantly improved the emulsification property,antioxidant property and thermal stability of porcine hemoglobin,indicating that co-modification is a feasible method to improve protein.

关 键 词：协同改性 酶解 猪血红蛋白 磷酸化 结构特性 

分 类 号：TS251.93[轻工技术与工程—农产品加工及贮藏工程]