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Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

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The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
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A Putative Lignin Copper Oxidase from Trichoderma reesei.

Mariane Daou1, Alexandra Bisotto1, Mireille Haon1

  • 1BBF, INRAE, Aix Marseille University, 13288 Marseille, France.

Journal of Fungi (Basel, Switzerland)
|August 26, 2021
PubMed
Summary

Trichoderma reesei fungus grows on lignin, enzymatically modifying its structure. A novel lignin copper oxidase (TrLOx) enzyme was identified, showing potential for lignin breakdown and polymerization.

Keywords:
Trichoderma reeseicopper radical oxidasetechnical lignin

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Area of Science:

  • Biotechnology
  • Mycology
  • Biochemistry

Background:

  • Trichoderma reesei is a fungus utilized for industrial enzyme production.
  • Lignin, a complex biopolymer, presents challenges for biodegradation and valorization.
  • Understanding fungal interactions with lignin is crucial for biorefining applications.

Purpose of the Study:

  • To investigate the ability of Trichoderma reesei to grow on and modify technical soda lignin.
  • To identify and characterize key enzymes involved in lignin degradation and modification by T. reesei.
  • To explore the potential of T. reesei secretome for lignin valorization.

Main Methods:

  • Cultivation of T. reesei on lignin-containing media.
  • Quantification of fungal growth and sporulation.
  • Analysis of soluble and insoluble lignin fractions.
  • Proteomic analysis of secreted enzymes.
  • Heterologous production and characterization of a novel copper oxidase (TrLOx).
  • Enzymatic assays on lignin-derived molecules and dimers.
  • High-performance size-exclusion chromatography (HPSEC) and liquid chromatography-mass spectrometry (LC-MS).

Main Results:

  • T. reesei demonstrated growth and sporulation on lignin as a sole carbon source.
  • Enzymatic modification of lignin involved oxidative conversion of side chains and cleavage of β-O-4 linkages.
  • Polymerization reactions of lignin were observed.
  • Five auxiliary activity (AA) enzymes, including a unique copper radical oxidase (TrLOx), were identified in the secretome.
  • TrLOx exhibited high stability at alkaline pH, oxidized alcohols and aldehydes, and acted on lignin-derived phenolic molecules and carbohydrates.
  • TrLOx displayed polymerizing activity on lignin dimers, forming polymers up to 10 units.
  • Synergistic action of TrLOx with other secreted oxidoreductases is suggested for lignin breakdown.

Conclusions:

  • Trichoderma reesei possesses the capability to utilize and modify technical soda lignin.
  • A novel lignin copper oxidase (TrLOx) from T. reesei plays a significant role in lignin modification and polymerization.
  • The identified enzymes and their synergistic interactions offer potential for lignin valorization and biorefining strategies.