Stability of microbial transglutaminase to high pressure treatment

被引：1

作者：

Sabine Lauber

Ivonne Noack

Henning Klostermeyer

Thomas Henle

机构：

[1] Lehrstuhl für Chemie der Biopolymere,

[2] Technische Universität München,undefined

[3] 85354 Freising,undefined

[4] Germany,undefined

[5] Institut für Lebensmittelchemie,undefined

[6] Technische Universität Dresden,undefined

[7] 01062 Dresden,undefined

[8] Germany,undefined

来源：

European Food Research and Technology | 2001年 / 213卷

关键词：

Isothermal pressure inactivation Microbial transglutaminase Inactivation kinetics Activation volume High pressure treatment;

D O I：

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学科分类号：

摘要：

The isothermal pressure inactivation of microbial transglutaminase in 0.2 M tris-acetate buffer (pH 6.0) was studied at 20, 40 and 60 °C. The inactivation kinetics followed a first order kinetic model. With increasing pressure at constant temperature, a consistent increase in inactivation rate constants k was noted, pointing to a negative activation volume ΔV*. The values of ΔV* were calculated as –7.1 cm3/mol at 20 °C, –17.4 cm3/mol at 40 °C and –2.3 cm3/mol at 60 °C, indicating a reduced pressure sensitivity at high temperature. A casein-based system was used to prove that transglutaminase is capable of cross-linking protein under high pressure, indicating that the enzyme can be used in combination with high pressure treatment of food.

引用

页码：273 / 276

页数：3