Scholarlink

<p>Phenol hydroxylase (PH) plays a central role in phenol biodegradation pathways. In this study, the enzymatic activity of PH in <i>Candida tropicalis</i> GY8 was evaluated following phenol-induced cultivation, and oxidation products were analyzed via high-performance liquid chromatography (HPLC). Two phenol hydroxylase genes, <i>CtPHE1</i> and <i>CtPHE2</i>, were identified, and their expression patterns were examined using RT-qPCR. Functional analysis of the corresponding proteins was conducted by cloning and expressing the genes in <i>Escherichia coli</i> BL21(DE3). Enzymatic activity reached its maximum after 15&#xa0;h of cultivation (<i>p</i> &lt; 0.01), and phenol conversion to catechol was verified by HPLC. RT-qPCR results indicated peak transcript levels at 10&#xa0;h, with <i>CtPHE2</i> showing consistently higher expression than <i>CtPHE1</i> at 5, 10, and 15&#xa0;h (<i>p</i> &lt; 0.01). Both recombinant proteins were capable of phenol degradation, with CtPHE2 exhibiting greater catalytic activity. These findings provide essential molecular information for advancing the understanding of phenol biodegradation mechanisms.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Gene cloning, phenol-responsive transcriptional profiling and recombinant protein characterization of phenol hydroxylase in Candida tropicalis GY8

  • 期刊论文

  • 发表日期：

    2025年6月2日

查看全文
  • Jianhua Lv,
  • Xiangnan Gu,
  • Minmin Hui,
  • Yingjie Luo,
  • Wenbo Luo,
  • Huiting Zhao,
  • Shuqin Yin,
  • Yan Feng,
  • Zhiquan Xue

摘要

Phenol hydroxylase (PH) plays a central role in phenol biodegradation pathways. In this study, the enzymatic activity of PH in Candida tropicalis GY8 was evaluated following phenol-induced cultivation, and oxidation products were analyzed via high-performance liquid chromatography (HPLC). Two phenol hydroxylase genes, CtPHE1 and CtPHE2, were identified, and their expression patterns were examined using RT-qPCR. Functional analysis of the corresponding proteins was conducted by cloning and expressing the genes in Escherichia coli BL21(DE3). Enzymatic activity reached its maximum after 15 h of cultivation (p < 0.01), and phenol conversion to catechol was verified by HPLC. RT-qPCR results indicated peak transcript levels at 10 h, with CtPHE2 showing consistently higher expression than CtPHE1 at 5, 10, and 15 h (p < 0.01). Both recombinant proteins were capable of phenol degradation, with CtPHE2 exhibiting greater catalytic activity. These findings provide essential molecular information for advancing the understanding of phenol biodegradation mechanisms.