Effect of water activity on the thermal stability of Thermomyces lanuginosus xylanases for process time-temperature integration

被引：7

作者：

Gogou, Eleni ^{[1
]}

Katapodis, Petros ^{[2
]}

Christakopoulos, Paul ^{[2
]}

Taoukis, Petros S. ^{[1
]}

机构：

[1] Natl Tech Univ Athens, Sch Chem Engn, Lab Food Chem & Technol, Athens 15780, Greece

[2] Natl Tech Univ Athens, Sch Chem Engn, Biotechnol Lab, Athens 15780, Greece

来源：

JOURNAL OF FOOD ENGINEERING | 2010年 / 100卷 / 04期

关键词：

beta-Xylanase; Water activity; Enzyme indicator; Thermal processing; Time temperature integrators; THERMOPHILIC FUNGUS; ALPHA-AMYLASE; INACTIVATION KINETICS; STERILIZATION PROCESSES; HORSERADISH-PEROXIDASE; HEAT; PURIFICATION; ENZYMES; APPLICABILITY; LIPOXYGENASE;

D O I：

10.1016/j.jfoodeng.2010.05.014

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

Three strains of the thermophilic fungus Thermomyces lanuginosus were used to produce beta-xylanases. The thermal stability of these xylanases at low levels of water activity was studied. Isothermal inactivation experiments were performed in the temperature range of 100-130 degrees C. Reduction of water activity to 0.63 and as low as 0.13 had a drastic effect on the observed D and z-values. At water activity of 0.13 the D-120 degrees C and z-values of the three xylanases ranged from 20.4 to 37.6 min and from 23.3 to 28.9 degrees C, respectively. The applicability of the developed kinetic models was tested under time-temperature profiles representative of typical thermal processes. The developed systems can be applied as time-temperature integrators (TTI) at this high thermal processing range. Calculations demonstrated that the use of a triple xylanase TTI system could provide acceptable F-values prediction for z-values lower than the achieved range. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：649 / 655

页数：7

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