Isolation, Purification and Enzymatic Properties of Nuclease P1 Fermented by Penicillium citrinum

被引：0
|
作者：
Li M. [1 ,2 ,3 ]
Yu H. [1 ,2 ,3 ]
Yu C. [1 ,2 ,3 ]
Wu Y. [1 ,2 ,3 ]
Gong D. [1 ,2 ,3 ]
机构：
[1] Three Gorges University, Yichang
[2] China Key Laboratory of Light Industry Functional Yeast, China Three Gorges University, Yichang
[3] Angel Yeast Co.,Ltd, Special Enzyme Division, Yichang
来源：
Science and Technology of Food Industry | 2021年 / 42卷 / 07期
关键词：
enzymatic property; kinetic parameter; nuclease P1; purification;
D O I：
10.13386/j.issn1002-0306.2020050212
中图分类号：
学科分类号：
摘要：
The nuclease P1 was purified to obtain pure component by activated carbon decolorization, (NH4)2SO4 precipitation, desalination and gel chromatography and its enzymatic properties was investigated. This purified enzyme had a specific activity of 33967 U/mg protein after 8.48-fold purification. The Michaelis constant (Km), the maximum reaction rates (Vm) and the catalytic constant (Kcat) of the purified enzyme were 2.50 mmol/L, 0.0864 mmol/(mL·min) and 252.43 s−1, respectively. The optimization pH and temperature for the nuclease P1 were at pH5.5 and 75 ℃. The enzyme was stable in the temperature range from 60 to 75 ℃ and in the pH range from 4.0 to 6.0. Zn2+ had a positive effect on the enzyme activity, while Cu2+ was a strong inhibitor of nuclease P1, Ni2+、Fe2+、Mn2+ had the different inhibition. This research laid a scientific foundation for the extensive application of the enzyme. © 2021 Authors. All rights reserved.
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页码：89 / 94
页数：5
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