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首页> 外文期刊>Bioprocess and Biosystems Engineering >Improved thermal stability of phytase from Yersinia intermedia by physical adsorption immobilization on amino-multiwalled carbon nanotubes
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Improved thermal stability of phytase from Yersinia intermedia by physical adsorption immobilization on amino-multiwalled carbon nanotubes

机译:通过在氨基 - 多壁碳纳米管上的物理吸附固定,改善了yersinia介质的植物酶的热稳定性

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摘要

Phytase is used in poultry diets to hydrolyze and release of phytate-bound phosphorus. Immobilization on nanomaterials optimizes enzyme's thermal stability and reusability. This study aimed to immobilize the recombinant phytase from Yersinia intermedia on the surface of amino-multi-walled carbon nanotubes (amino-MWCNTs) by physical adsorption. For this, zeta potential measurement, FTIR spectroscopic analysis, scanning electron microscope (SEM), kinetic as well as thermodynamic parameters were used to characterize immobilized phytase on amino-MWCNTs. According to results, the optimum temperature of the immobilized phytase increased from 50 to 70 degrees C and also thermal and pH stability improved considerably. Moreover, immobilization led to an increase in the value of K-m and k(cat) from 0.13 to 0.33 mM and 2220 to 2776 s(-1), respectively. In addition, the changes in activation energy of thermal inactivation (Delta E-a (D)(#)), the free energy of thermal inactivation (Delta G(D)(#)) and the enthalpy of thermal inactivation (Delta H-D(#)) for immobilized phytase increased by +11.05, +24.7 and +11.4 kj/mole, respectively, while the value of the change in the entropy of thermal inactivation (Delta S-D(#)) decreased by - 0.04 kj/mole.K. Overall, our results showed that adsorption immobilization of phytase on amino-MWCNTs increases thermal, pH and storage stability as well as some of kinetic parameters.
机译:植酸酶用于家禽饮食中,以水解和释放植酸结合的磷。固定在纳米材料上优化酶的热稳定性和可重用性。该研究旨在通过物理吸附将来自yersinia介质的重组植酸酶固定在氨基 - 多壁碳纳米管(氨基-MWCNT)表面上。为此,使用Zeta电位测量,FTIR光谱分析,扫描电子显微镜(SEM),动力学以及热力学参数来表征氨基-MWCNT上的固定化植酸酶。根据结果​​,固定化植酸酶的最佳温度从50℃增加到70℃,并且热量和pH稳定性显着提高。此外,固定化导致分别从0.13至0.33mm和2220至2776 s(-1)的k-m和k(猫)的值增加。此外,热失活激活能量的变化(Delta EA(D)(D)(#)),热灭活的自由能(Delta G(D)(#))和热灭活的焓(Delta HD(#) )对于固定的植酸酶分别增加+11.05,+ 24.7和+11.4 kJ / mole,而热失活熵的变化的值(Delta SD(Delta SD(Delta SD)减少 - 0.04kJ / mol.K。总体而言,我们的结果表明,氨基-MWCNT上的植酸酶的吸附固定增加了热,pH和储存稳定性以及一些动力学参数。

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