北美化学作业代写 过氧化氢酶

2020-02-07 08:53

2013年，研究人员Cantemir, A.等质疑温度以及添加物和底物的存在与否如何影响哺乳动物过氧化氢酶的动力学和温度失活(使用孵育和iso转换方法)。底物浓度采用朗伯-比尔定律计算。研究人员得出结论，过氧化氢存在时，过氧化氢酶的失活明显更大。无底物时，过氧化氢酶与添加剂的初始反应速率随温度的升高呈指数下降趋势。研究小组观察到，过氧化氢酶在水和底物作用下的最大活化温度为40摄氏度。该研究为过氧化氢酶的动力学研究提供了有价值的信息。本研究将有助于我们预测、理解和解释温度(自变量)对过氧化氢酶活性的影响。在热化学反应中，研究人员考察了过氧化氢酶分解过氧化氢的动力学。在四通道等温微热量计中，在pH值为7.4、温度范围为10 ~ 30℃的条件下观察反应。利用这些数据，研究人员计算了这些反应的热力学量。首先，研究小组计算了-87.55±0.72 kJ/mol的反应焓，然后计算了-119 kJ/mol的25度吉布斯能。根据活化能和动力学参数的实验值，设计一个函数k(T)来确定速率常数k。一旦绘制，很明显，温度的增加增加了速率常数。如研究中所述，由于活化能低，反应速率常数高表示反应是自发的。因此，在本实验温度范围内，过氧化氢酶催化的分解反应速率随温度升高而增加。本研究证明，在酶的作用下，该反应是自发的、劳力化的。热力学和熵的定律支持这个反应。这个反应的特征是相关的，因为这个反应几乎与我在观察基于产气速率的过氧化氢酶动力学时进行的反应相同。同时，本研究为理解该反应的性质提供了基础知识。
北美化学作业代写 过氧化氢酶
In 2013, researchers Cantemir, A. et al. questioned how temperature and the presence or absence of additives and substrate affect the kinetics and temperature inactivation of mammalian catalase (using incubation and iso conversional methods). Substrate concentrations were calculated using Lambert-Beer Law. The researchers concluded that the inactivation of catalase was significantly larger when hydrogen peroxide was present. When the substrate was absent, the initial rate of reaction for catalase with additives decreased exponentially with temperature increase. The team observed that the maximum for catalase activation with water and substrate was forty degrees Celsius. This study holds valuable information about the kinetics of catalase. This study will provide insight into how we can predict, understand and interpret the effects of temperature (independent variable) on the rate of catalase activity.In Thermochimica Acta, researchers examined the decomposition kinetics of hydrogen peroxide by catalase. The reactions were observed at a pH of 7.4 and within a temperature range of ten to thirty degrees Celsius in a four-channel isothermal microcalorimeter. Using the data, researchers calculated the thermodynamic quantities of the reactions. First, the team calculated the enthalpy of reaction, found at -87.55 ± 0.72 kJ/mol, then the Gibbs Energy at twenty-five degrees, calculated at -119 kJ/mol. The rate constant, k, was determined by devising a function, k(T), with experimental values of activation energy and kinetic parameters. Once plotted, it was apparent that an increase in temperature increased the rate constant. As stated in the study, a high rate constant indicates a spontaneous reaction, due to the low activation energy. Thus, within the temperature range in this experiment, the rate of the decomposition reaction catalyzed by catalase increased with temperature. This study proved that this reaction is spontaneous and exergonic with the help of the enzyme. The laws of thermodynamics and entropy favor this reaction. The characteristics of this reaction are relevant as this reaction is nearly identical to the reaction I conducted when observing the kinetics of catalase based on the rate of gas production. As well, this study provides the foundational knowledge for understanding the nature of this reaction.

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