利用过氧化物酶库方法鉴定催化氟化芳烃降解的植物过氧化物酶

IF 3.9 4区 生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Ashton Ware, Sally Hess, David Gligor, Sierra Numer, Jack Gregory, Carson Farmer, Gregory M. Raner, Hector E. Medina
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引用次数: 0

摘要

在这项工作中,一系列粗制植物过氧化物酶(包括辣根(HRP)和葫芦属的六个成员)证明了单氟和多氟酚类化合物的降解能力。通过文库筛选法确定了高活性样本,其中对 50 多种粗制植物样本进行了初步评估,以确定其对 4-氟苯酚的脱氟活性。在 HRP、南瓜皮(PKS)和南瓜皮(BNS)中观察到了最高的浓度,它们对所有测试底物的内在分解率都是最高的。虽然随着酚类底物氟化程度的增加,HRP 的活性会显著降低,但 PKS 的活性仅略有降低。此外,硅学研究表明,HRP 的活性位点不能很好地容纳额外氟的立体体积,导致底物与催化血红素对接得更远,从而减慢了催化速率。我们认为 PKS 的活性位点可能更大,能更接近全氟底物,因此与 HRP 酶相比能保持更高的活性。不过,我们建议对过氧化物酶进行详细的动力学特性研究。总之,PKS 的高催化活性及其每克组织的高产率使其成为开发降解含氟芳烃的环境友好型生物催化方法的绝佳候选物。最后,文库方法成功地鉴定出了降解多氟芳烃化合物(PFAC)的高活性样本,这表明该方法在寻找其他降解多氟芳烃化合物的先进催化剂时可能会派上用场。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Identification of Plant Peroxidases Catalyzing the Degradation of Fluorinated Aromatics Using a Peroxidase Library Approach

Identification of Plant Peroxidases Catalyzing the Degradation of Fluorinated Aromatics Using a Peroxidase Library Approach

In this work, the degradation of mono- and polyfluorinated phenolic compounds was demonstrated by a series of crude plant peroxidases, including horseradish root (HRP) and six members of the Cucurbita genus. Highly active samples were identified using a library screening approach in which more than 50 crude plant samples were initially evaluated for defluorination activity toward 4-fluorophenol. The highest concentrations were observed in the HRP, pumpkin skin (PKS), and butternut squash skin (BNS), which consistently gave the highest intrinsic rates of decomposition for all the substrates tested. Although HRP exhibited a significant decrease in activity with increased fluorination of the phenolic substrate, PKS showed only minor reductions. Furthermore, in silico studies indicated that the active site of HRP poorly accommodates the steric bulk of additional fluorines, causing the substrate to dock farther from the catalytic heme and thus slowing the catalysis rate. We propose that the PKS active site might be larger, allowing closer access to the perfluorinated substrate, and therefore maintaining higher activity compared to the HRP enzyme. However, detailed kinetic characterization studies of the peroxidases are recommended. Conclusively, the high catalytic activity of PKS and its high yield per gram of tissue make it an excellent candidate for developing environmentally friendly biocatalytic methods for degrading fluorinated aromatics. Finally, the success of the library approach in identifying highly active samples for polyfluorinated aromatic compound (PFAC) degradation suggests the method may find utility in the quest for other advanced catalysts for PFAS degradation.

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来源期刊
Engineering in Life Sciences
Engineering in Life Sciences 工程技术-生物工程与应用微生物
CiteScore
6.40
自引率
3.70%
发文量
81
审稿时长
3 months
期刊介绍: Engineering in Life Sciences (ELS) focuses on engineering principles and innovations in life sciences and biotechnology. Life sciences and biotechnology covered in ELS encompass the use of biomolecules (e.g. proteins/enzymes), cells (microbial, plant and mammalian origins) and biomaterials for biosynthesis, biotransformation, cell-based treatment and bio-based solutions in industrial and pharmaceutical biotechnologies as well as in biomedicine. ELS especially aims to promote interdisciplinary collaborations among biologists, biotechnologists and engineers for quantitative understanding and holistic engineering (design-built-test) of biological parts and processes in the different application areas.
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