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Adsorption and Catalytic Activity of Alakaline Phosphatase on Halloysite Surface
Russian Journal of Physical Chemistry A ( IF 0.7 ) Pub Date : 2021-07-15 , DOI: 10.1134/s0036024421070050
L. F. Atyaksheva 1 , T. I. Ibrahimzade 1 , I. A. Kasyanov 1 , A. Yu. Fastov 2 , S. A. Fastov 3
Affiliation  

Abstract

It is shown that the values of adsorption, the type of adsorption isotherms, and the catalytic activity and thermal stability of alkaline phosphatase on halloysite surfaces depend on the texture of aluminosilicate nanotubes. The maximum values of the limiting adsorption are obtained on samples with the smallest specific surface area (28 and 50 m2/g): 18 and 23 mg/g or 0.69 and 0.54 mg/m2, respectively. It is found that the adsorption layers of alkaline phosphatase on surfaces of halloysite are more stable than the enzyme in solution. The effective rate constants of inactivation at 59°С vary within 0–2.3 × 10−4 s−1 for heterogeneous samples. In solution at the optimum pH of enzyme stability, they are 12.5 × 10−4 s−1. The catalytic activity of the adsorption layers of alkaline phosphatase is no more than 1% of the activity of the native enzyme.



中文翻译:

碱性磷酸酶在埃洛石表面的吸附和催化活性

摘要

结果表明,吸附值、吸附等温线的类型以及碱性磷酸酶在埃洛石表面的催化活性和热稳定性取决于铝硅酸盐纳米管的织构。在具有最小比表面积(28 和 50 m 2 /g)的样品上获得了极限吸附的最大值:分别为 18 和 23 mg/g 或 0.69 和 0.54 mg/m 2。结果表明,碱性磷酸酶在埃洛石表面的吸附层比溶液中的酶更稳定。对于异质样品,59°С 灭活的有效速率常数在 0–2.3 × 10 -4 s -1范围内变化。在酶稳定性最适 pH 的溶液中,它们是 12.5 × 10 -4s -1。碱性磷酸酶吸附层的催化活性不超过天然酶活性的1%。

更新日期:2021-07-16
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