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

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.