Preparation of Thermosensitive Polymer Immobilized Horseradish Peroxidase and its Application in Catalytic Degradation of Phenol

IF 2.3 4区化学 Q3 CHEMISTRY, PHYSICAL

Catalysis Letters Pub Date : 2024-06-22 DOI:10.1007/s10562-024-04730-x

Yuanyuan Li, Yuanyuan Chen, Tongyu Li, Yongqing Song, Jiacong Wu, Juan Han, Yun Wang

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Abstract

The immobilized horseradish peroxidase (P1-HRP) was prepared based on the affinity interaction between the phenylborate group in mVBA-b-p (AAm co AN) polymer (P1) and the adjacent dihydroxy group in horseradish peroxidase (HRP). The immobilization conditions of P1-HRP were optimized. Under the conditions of P1 concentration of 20 mg/mL, pH 8, temperature of 50 ℃, and immobilization time of 2 h, the HRP was immobilized to obtain the optimal immobilization amount (84.7 mg/g). The successful preparation of P1-HRP was demonstrated through characterizations such as laser scanning confocal microscopy (LCSM), scanning electron microscope (SEM), dynamic light scattering (DLS) and thermogravimetric analyzer (TGA). P1-HRP exhibited excellent pH stability, thermal stability and storage stability compared to the free horseradish peroxidase. P1-HRP had shown good application value in the degradation of phenol pollutants. After 10 repetitions of phenol degradation, the relative enzyme activity of P1-HRP could still be retained by 55.62%, indicating its good reusability. The optimal conditions for the catalytic degradation of phenol by P1-HRP were optimized. After catalytic degradation of phenol for 60 min under the same conditions, the degradation rate of P1-HRP (92.33%) was higher than that of free horseradish peroxidase (85.32%).

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热敏聚合物固定化辣根过氧化物酶的制备及其在催化降解苯酚中的应用

根据 mVBA-b-p (AAm co AN) 聚合物（P1）中的苯基硼酸酯基团与辣根过氧化物酶（HRP）中相邻的二羟基之间的亲和力作用，制备了固定化辣根过氧化物酶（P1-HRP）。对 P1-HRP 的固定条件进行了优化。在 P1 浓度为 20 mg/mL、pH 值为 8、温度为 50 ℃、固定时间为 2 h 的条件下，固定 HRP 得到了最佳固定量（84.7 mg/g）。通过激光扫描共聚焦显微镜（LCSM）、扫描电子显微镜（SEM）、动态光散射（DLS）和热重分析仪（TGA）等表征，证明了 P1-HRP 的成功制备。与游离辣根过氧化物酶相比，P1-HRP 具有优异的 pH 稳定性、热稳定性和储存稳定性。P1-HRP 在降解苯酚污染物方面具有良好的应用价值。在重复降解苯酚 10 次后，P1-HRP 的相对酶活性仍能保持 55.62%，表明其具有良好的重复使用性。对 P1-HRP 催化降解苯酚的最佳条件进行了优化。在相同条件下催化降解苯酚 60 分钟后，P1-HRP 的降解率（92.33%）高于游离辣根过氧化物酶的降解率（85.32%）。

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来源期刊

Catalysis Letters 化学-物理化学

CiteScore

5.70

自引率

3.60%

发文量

327

审稿时长

1 months

期刊介绍： Catalysis Letters aim is the rapid publication of outstanding and high-impact original research articles in catalysis. The scope of the journal covers a broad range of topics in all fields of both applied and theoretical catalysis, including heterogeneous, homogeneous and biocatalysis. The high-quality original research articles published in Catalysis Letters are subject to rigorous peer review. Accepted papers are published online first and subsequently in print issues. All contributions must include a graphical abstract. Manuscripts should be written in English and the responsibility lies with the authors to ensure that they are grammatically and linguistically correct. Authors for whom English is not the working language are encouraged to consider using a professional language-editing service before submitting their manuscripts.