Scholarlink

<p>This study reported the optimization, purification and characterization of a novel L-lysine α-oxidase (LLO) from marine-derived&#xa0;<i>Streptomyces griseobrunneus</i>&#xa0;strain S15. Among the twenty-two Streptomyces isolates, S15 showed the highest production of LLO (8 U/mg) after 96&#xa0;h of cultivation. Molecular identification via 16S rRNA sequencing confirmed its phylogenetic relationship to&#xa0;<i>S. griseobrunneus</i>&#xa0;(GenBank PQ416578). Optimization of LLO production using response surface methodology enhanced the enzyme production by about five-fold compared to the control. Purification of LLO resulted in a yield of 49.99% and 2.356-fold purification through a single-step Sephacryl S-300 column. The purified homodimeric enzyme (115&#xa0;kDa native, 58&#xa0;kDa subunit) exhibited optimal activity at pH 6.4 and 50&#xa0;°C, with exceptional thermal stability at physiological temperatures. According to kinetic studies, the enzyme has a high substrate affinity (<Emphasis Type="BoldItalic">K</Emphasis><sub><Emphasis Type="BoldItalic">m</Emphasis></sub> 0.050&#xa0;mM for L-lysine) and a broad specificity for basic and hydrophobic amino acids. Moreover, the enzyme showed potent antibacterial effects against multidrug-resistant pathogens (MIC 1.99–5.33 U/mL), demonstrated comparable or enhanced antibacterial activity relative to tested antibiotics. The unique combination of catalytic efficiency, stability, and antimicrobial activity makes this LLO a promising candidate for therapeutic and industrial applications.</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

Novel L-lysine α-oxidase from marine streptomyces: production, optimization and potent antibacterial activity against drug-resistant pathogens

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月13日

查看全文
  • Mohamed Abdelraof,
  • Amany A. Hassabo,
  • Doaa Darwich,
  • Mohamed M. Abdel-Monsef

摘要

This study reported the optimization, purification and characterization of a novel L-lysine α-oxidase (LLO) from marine-derived Streptomyces griseobrunneus strain S15. Among the twenty-two Streptomyces isolates, S15 showed the highest production of LLO (8 U/mg) after 96 h of cultivation. Molecular identification via 16S rRNA sequencing confirmed its phylogenetic relationship to S. griseobrunneus (GenBank PQ416578). Optimization of LLO production using response surface methodology enhanced the enzyme production by about five-fold compared to the control. Purification of LLO resulted in a yield of 49.99% and 2.356-fold purification through a single-step Sephacryl S-300 column. The purified homodimeric enzyme (115 kDa native, 58 kDa subunit) exhibited optimal activity at pH 6.4 and 50 °C, with exceptional thermal stability at physiological temperatures. According to kinetic studies, the enzyme has a high substrate affinity (Km 0.050 mM for L-lysine) and a broad specificity for basic and hydrophobic amino acids. Moreover, the enzyme showed potent antibacterial effects against multidrug-resistant pathogens (MIC 1.99–5.33 U/mL), demonstrated comparable or enhanced antibacterial activity relative to tested antibiotics. The unique combination of catalytic efficiency, stability, and antimicrobial activity makes this LLO a promising candidate for therapeutic and industrial applications.