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从Penicillium chrysogenum中净化和表征L-氨酸减小酶

Hamed M El-Shora¹, Nessma A El-Zawawy², Mohamed A Abd El-Rheem²

¹Department of Botany, Faculty of Science, Mansoura University, Mansoura, Egypt. shora@mans.edu.eg.

BMC microbiology

|January 31, 2024

概括

来自Penicillium chrysogenum的L-氨酸减小酶 (ADI) 被净化并进行了表征. 这种酶由于其催化特性和稳定性,具有工业和生物技术应用的潜力.

科学领域:

生物化学生物化学
酶学是一种酶学.
微生物生物技术微生物生物技术

背景情况:

L-氨酸减小酶 (ADI) 将氨酸水解成氨和氨.
素被认为是医疗保健中有益的天然补充剂.
了解ADI的特性对于其潜在的应用至关重要.

研究的目的:

从Penicillium chrysogenum中净化和表征L-氨酸减弱酶 (ADI).
为了研究净化的ADI的最佳条件和稳定性.
确定酶的辅因子要求和活性位点特征.

主要方法:

使用硫酸沉,DEAE纤维素和Sephadex G200染色学净化ADI.
确定酶活性,特异性活性,分子量,最佳温度和pH值.
研究酶动力学,热稳定性以及各种化学剂的无活化/激活.

主要成果:

ADI净化了17.2倍,产量为4.6%,特异活性为50U/mg.
在40°C和pH值6.0时观察到最佳活性;量化了热稳定性.
该酶是一种金属酶,需要硫基,基,基,基,基和基组进行催化,并由ATP,ADP,AMP,氨酸和dithiothreitol激活.

结论:

来自P. chrysogenum的净化ADI表现出有利的生化特性.
该酶的特性表明它是一种金属酶,其活性需要特定的氨基酸残留物.
来自P. chrysogenum的ADI是各种工业和生物技术应用的有希望的候选者.

关键词:

激活活动激活活动活动群活动群活动群氨酸减小酶的作用运动学运动学在P.chrysogenum中使用.净化净化净化净化

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