Effect of temperature and/or pressure on tomato pectinesterase activity

被引：62

作者：

Van den Broeck, I ^{[1
]}

Ludikhuyze, LR ^{[1
]}

Van Loey, AM ^{[1
]}

Hendrickx, ME ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Fac Agr & Appl Biol Sci, Lab Food Technol, Dept Food & Microbial Technol, B-3001 Heverlee, Belgium

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2000年 / 48卷 / 02期

关键词：

tomato pectinesterase; thermal stability; pressure stability; kinetics; activation;

D O I：

10.1021/jf990569n

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

The activity of tomato pectinesterase (PE) was studied as a function of pressure (0.1-900 MPa) and temperature (20-75 degrees C). Tomato PE was rather heat labile at atmospheric pressure (inactivation in the temperature domain 57-65 degrees C), but it was very pressure resistant. Even at 900 MPa and 60 degrees C the inactivation was slower as compared to the same treatment at atmospheric pressure. At atmospheric pressure, optimal catalytic activity of PE was found at neutral pH and a temperature of 55 degrees C. Increasing pressure up to 300 MPa increased the enzyme activity as compared to atmospheric pressure. A maximal enzyme activity was found at 100-200 MPa combined with a temperature of 60-65 degrees C. The presence of Ca(2+) ions (60 mM) decreased the enzyme activity at atmospheric pressure in the temperature range 45-60 degrees C but increased enzyme activity at elevated pressure (up to 300 MPa). Maximal enzyme activity in the presence of Ca(2+) ions was noted at 200- 300 MPa in combination with a temperature of 65-70 degrees C.

引用

页码：551 / 558

页数：8

共 53 条

[51] Influence of pH, benzoic acid, EDTA, and glutathione on the pressure and/or temperature inactivation kinetics of mushroom polyphenoloxidase [J].