Thermal denaturation of recombinant human lysozyme from rice: effect of pH and comparison with human milk lysozyme

被引：6

作者：

Castillo, Eduardo ^{[1
]}

Franco, Indira ^{[1
]}

Perez, Maria D. ^{[1
]}

Calvo, Miguel ^{[1
]}

Sanchez, Lourdes ^{[1
]}

机构：

[1] Univ Zaragoza, Fac Vet, E-50013 Zaragoza, Spain

来源：

EUROPEAN FOOD RESEARCH AND TECHNOLOGY | 2011年 / 233卷 / 06期

关键词：

Human recombinant lysozyme; Human milk lysozyme; Differential scanning calorimetry; Thermodynamical parameters; EXPRESSION; PURIFICATION; STABILITY; RESIDUES; INFANTS; FORMULA; BINDING; SYSTEMS; PLANTS;

D O I：

10.1007/s00217-011-1612-8

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Thermal denaturation of recombinant human lysozyme from rice has been studied by differential scanning calorimetry at acidic (4.2), neutral (7.2) and basic (9.2) pH levels at various heating rates, and it has been compared with thermal denaturation of human lysozyme isolated from milk at the same pH levels at a heating rate of 10 A degrees C/min. Data obtained from heat-induced unfolding and subsequent refolding after heating indicate that thermal denaturation of both lysozymes undergoes a two-state process. The maximum temperature of the endothermic peaks and the enthalpy change of denaturation indicate that recombinant and milk lysozymes possess similar thermostability, which is higher at acidic than at neutral pH. On the other hand, both proteins are more thermolabile at basic pH. Lysozyme from human milk shows a higher tendency to aggregate than recombinant human lysozyme from rice during the thermal denaturation process.

引用

页码：1067 / 1073

页数：7

共 34 条

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