相关实验视频

Updated: Sep 18, 2025

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

动力和热处理参数的分布基于α-氨基酶失活数据

George N Stoforos¹, Maria Kontopanou¹, Maria C Giannakourou²

¹Department of Food Science and Human Nutrition, Agricultural University of Athens, Athens, Greece.

Journal of food science

|June 24, 2025

概括

这项研究使用蒙特卡洛方法确定了alpha-amylase的热失活动力学. 随机分析为食品加工提供可靠的致死率计算,这对于确保产品安全和质量至关重要.

科学领域:

食品科学食品科学食品科学
生物技术是生物技术.
化学工程是化学工程的重要组成部分.

背景情况:

确保食品质量和安全需要了解酶和微生物的热失活动力学.
来自Aspergillus oryzae的α-氨酶是食品加工中的关键酶,其热稳定性至关重要.

研究的目的:

为了研究来自阿斯伯吉勒斯菌的α-amylase的热无活化动力学.
使用随机蒙特卡洛程序估计动力参数,如小数减小时间 (D_T) 和z值.
评估参数变化对热过程死亡率计算的影响.

主要方法:

在60°C,70°C,80°C和90°C的温度下研究了alpha-amylase的热失活.
使用随机蒙特卡洛程序来估计动力参数及其频率分布.
应用数学校正处理过程中的温度变化,使用F值概念.

主要成果:

阿尔法氨基酶D_75°C和z值分布正常,平均值分别为4.22 ± 0.63分钟和13.00 ± 0.98°C (99%置信区间).
该研究证明了随机分析在评估参数变化对致死率计算的影响中的实用性.
参数的频率分布,而不是配对值,足以进行可靠的致死率计算.

结论:

随机分析,特别是使用蒙特卡洛方法,是优化热处理和酶失活的宝贵工具.
提出的方法允许在食品加工中进行可靠的致死率计算,即使使用非线性动态和可变参数.
这种方法提高了热过程设计的准确性,有助于提高食品安全和质量.

更多相关视频

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

相关概念视频

Enzyme Kinetics

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

Arrhenius Plots

Arrhenius Plots

The Arrhenius equation relates the activation energy and the rate constant, k, for chemical reactions. In the Arrhenius equation, k = Ae−Ea/RT, R is the ideal gas constant, which has a value of 8.314 J/mol·K, T is the temperature on the kelvin scale, Ea is the activation energy in J/mole, e is the constant 2.7183, and A is a constant called the frequency factor, which is related to the frequency of collisions and the orientation of the reacting molecules.
The Arrhenius equation can be used...

Introduction to Enzyme Kinetics

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...