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辣根过氧化物酶（HRP）被过氧化氢失活动力学。

Inactivation kinetics of horseradish peroxidase (HRP) by hydrogen peroxide.

机构信息

Grupo de Investigación en Bioeconomía y Sostenibilidad Agroalimentaria, Escuela de Administración de Empresas Agropecuarias, Facultad Seccional Duitama, Universidad Pedagógica y Tecnológica de Colombia, Duitama, Colombia.

Instituto de Investigaciones en Ciencia y Tecnología de Materiales (INTEMA), CCT - Mar del Plata. CONICET, Mar del Plata, Argentina.

出版信息

Sci Rep. 2023 Aug 17;13(1):13363. doi: 10.1038/s41598-023-39687-1.

DOI:10.1038/s41598-023-39687-1
PMID:37591893
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10435507/
Abstract

In recent years, the peroxidase enzymes have generated wide interest in several industrial processes, such as wastewater treatments, food processing, pharmaceuticals, and the production of fine chemicals. However, the low stability of the peroxidases in the presence of hydrogen peroxide (HO) has limited its commercial use. In the present work, the effect of HO on the inactivation of horseradish peroxidase (HRP) was evaluated. Three states of HRP (E, E, and E) were identified. While in the absence of HO, the resting state E was observed, in the presence of low and high concentrations of HO, E and E were found, respectively. The results showed that HRP catalyzed the HO decomposition, forming the species E, which was catalytically inactive. Results suggest that this loss of enzymatic activity is an intrinsic characteristic of the studied HRP. A model from a modified version of the Dunford mechanism of peroxidases was developed, which was validated against experimental data and findings reported by the literature.

摘要

近年来，过氧化物酶在许多工业过程中引起了广泛的兴趣，例如废水处理、食品加工、制药和精细化学品的生产。然而，过氧化物酶在过氧化氢 (HO) 存在下的低稳定性限制了其商业用途。在本工作中，评估了 HO 对辣根过氧化物酶 (HRP) 失活的影响。鉴定了 HRP 的三种状态 (E、E 和 E)。在没有 HO 的情况下，观察到静止状态 E，而在低浓度和高浓度 HO 的存在下，分别发现了 E 和 E。结果表明，HRP 催化 HO 的分解，形成无催化活性的 E 物种。结果表明，这种酶活性的丧失是所研究的 HRP 的固有特性。针对实验数据和文献报道，开发了一个经过修改的 Dunford 过氧化物酶机制模型，并对其进行了验证。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/71ecfb66f954/41598_2023_39687_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/e748de4ee649/41598_2023_39687_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/e547cb410ea9/41598_2023_39687_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/f93d54253f8a/41598_2023_39687_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/5031e0ecb607/41598_2023_39687_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/12c1f848c0db/41598_2023_39687_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/0b3b87671e70/41598_2023_39687_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/739ee8d7f23d/41598_2023_39687_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/a0f135ce5ca5/41598_2023_39687_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/71ecfb66f954/41598_2023_39687_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/e748de4ee649/41598_2023_39687_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/e547cb410ea9/41598_2023_39687_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/f93d54253f8a/41598_2023_39687_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/5031e0ecb607/41598_2023_39687_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/12c1f848c0db/41598_2023_39687_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/0b3b87671e70/41598_2023_39687_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/739ee8d7f23d/41598_2023_39687_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/a0f135ce5ca5/41598_2023_39687_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c692/10435507/71ecfb66f954/41598_2023_39687_Fig9_HTML.jpg

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