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Studies on the production of fungal peroxidases in Aspergillus niger

A Conesa1, C A van den Hondel, P J Punt

  • 1Department of Molecular Genetics and Gene Technology, TNO Nutrition and Food Research Institute, 3704 HE Zeist, The Netherlands.

Applied and Environmental Microbiology
|July 6, 2000
PubMed

Insights

Researchers explored fungal peroxidase production in Aspergillus niger, finding that manganese peroxidase (MnP) can be efficiently produced and secreted as an active enzyme. Lignin peroxidase (LiP) expression, however, resulted in inactive protein, highlighting processing challenges.

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Enzyme Engineering

Background:

  • Filamentous fungi are crucial for producing enzymes like fungal peroxidases.
  • Understanding limitations in enzyme production is key for industrial applications.
  • Phanerochaete chrysosporium peroxidases (lignin peroxidase and manganese peroxidase) are of significant interest.

Purpose of the Study:

  • To investigate the expression of Phanerochaete chrysosporium lignin peroxidase (lipA) and manganese peroxidase (mnp1) genes in Aspergillus niger.
  • To identify limiting factors for efficient fungal peroxidase production.
  • To optimize the production of active fungal peroxidases.

Main Methods:

  • Utilized a protease-deficient Aspergillus niger strain for gene expression studies.
  • Employed different expression cassettes for recombinant gene integration.
  • Analyzed gene expression using Northern blotting.
  • Assessed enzyme activity, N-terminal processing, and SDS-PAGE for secreted proteins.
  • Investigated the effect of hemoglobin supplementation and gene fusion strategies.

Main Results:

  • High steady-state mRNA levels were observed for both lipA and mnp1 genes.
  • Active manganese peroxidase (MnP) was successfully secreted into the culture medium with properties similar to the native enzyme.
  • Recombinant MnP production reached up to 100 mg/liter with hemoglobin supplementation.
  • Secreted lignin peroxidase (LiP) was not active, suggesting incorrect processing.
  • Fusion of genes to the Aspergillus niger glucoamylase gene did not improve production yields.

Conclusions:

  • Aspergillus niger can efficiently produce active manganese peroxidase (MnP).
  • Challenges in protein processing limit the production of active lignin peroxidase (LiP) in this system.
  • Hemoglobin supplementation is a viable strategy to enhance MnP yields.
  • Further research is needed to overcome processing issues for LiP production.

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