Optimized production of lignolytic manganese peroxidase in immobilized cultures of Phanerochaete chrysosporium

Hyuk Sung Kwon, Eunyong Chung, Junse Oh, Chang Ha Lee, Ik Sung Ahn

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Manganese peroxidase (MnP) is a key enzyme involved in the lignolysis of white-rot fungi. The purpose of this study is to investigate the effect of immobilization and culture conditions on MnP production in cultures of Phanerochaete chrysosporium grown on polyurethane foam. Higher concentrations of foam and lower levels of spore inoculums resulted in the formation of scattered mycelial pellets, increased autolysis of chlamydospore-like cells (a reservoir of MnP), and a higher activity of MnP. Even though MnP was a secondary metabolite, the addition of 5 times more glucose and diammonium tartrate, as carbon and nitrogen sources, resulted in a 4 fold increase in the dry cell mass. However, MnP activity decreased under these conditions to less than half, due to the formation of increasingly dense pellets and the inhibited lysis of chlamydospore-like cells.

Original languageEnglish
Pages (from-to)108-114
Number of pages7
JournalBiotechnology and Bioprocess Engineering
Volume13
Issue number1
DOIs
Publication statusPublished - 2008 Jan 1

Fingerprint

manganese peroxidase
Phanerochaete
Manganese
Foams
Autolysis
Metabolites
Spores
Fungi
Immobilization
Polyurethanes
Glucose
Nitrogen
Carbon
Enzymes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering

Cite this

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abstract = "Manganese peroxidase (MnP) is a key enzyme involved in the lignolysis of white-rot fungi. The purpose of this study is to investigate the effect of immobilization and culture conditions on MnP production in cultures of Phanerochaete chrysosporium grown on polyurethane foam. Higher concentrations of foam and lower levels of spore inoculums resulted in the formation of scattered mycelial pellets, increased autolysis of chlamydospore-like cells (a reservoir of MnP), and a higher activity of MnP. Even though MnP was a secondary metabolite, the addition of 5 times more glucose and diammonium tartrate, as carbon and nitrogen sources, resulted in a 4 fold increase in the dry cell mass. However, MnP activity decreased under these conditions to less than half, due to the formation of increasingly dense pellets and the inhibited lysis of chlamydospore-like cells.",
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Optimized production of lignolytic manganese peroxidase in immobilized cultures of Phanerochaete chrysosporium. / Kwon, Hyuk Sung; Chung, Eunyong; Oh, Junse; Lee, Chang Ha; Ahn, Ik Sung.

In: Biotechnology and Bioprocess Engineering, Vol. 13, No. 1, 01.01.2008, p. 108-114.

Research output: Contribution to journalArticle

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