Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system

Elizabeth A. Pease; Steven D. Aust; Ming Tien

doi:10.1016/0006-291X(91)91903-P

Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system

Elizabeth A. Pease, Steven D. Aust, Ming Tien

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

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Abstract

The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H₂O₂.

Original language	English (US)
Pages (from-to)	897-903
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	179
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(91)91903-P
State	Published - Sep 16 1991

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(91)91903-P

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@article{2b048abf91344407829331d44c9c43e2,

title = "Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system",

abstract = "The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.",

author = "Pease, {Elizabeth A.} and Aust, {Steven D.} and Ming Tien",

note = "Funding Information: This work was supported in part by United States Department of Energy Grant DE-FGOZ 87ER136990 and National Institute of Environmental Health Sciences Grant l-P42ESO4922-01. Ming Tien is a recipient of a Presidential Young Investigator Award from the National Science Foundation (DCB-8657853). We thank Todd Johnson for his help in transfecting and purifying the recombinant virus.",

year = "1991",

month = sep,

day = "16",

doi = "10.1016/0006-291X(91)91903-P",

language = "English (US)",

volume = "179",

pages = "897--903",

journal = "Biochemical and Biophysical Research Communications",

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publisher = "Elsevier B.V.",

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T1 - Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system

AU - Pease, Elizabeth A.

AU - Aust, Steven D.

AU - Tien, Ming

N1 - Funding Information: This work was supported in part by United States Department of Energy Grant DE-FGOZ 87ER136990 and National Institute of Environmental Health Sciences Grant l-P42ESO4922-01. Ming Tien is a recipient of a Presidential Young Investigator Award from the National Science Foundation (DCB-8657853). We thank Todd Johnson for his help in transfecting and purifying the recombinant virus.

PY - 1991/9/16

Y1 - 1991/9/16

N2 - The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.

AB - The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.

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DO - 10.1016/0006-291X(91)91903-P

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JF - Biochemical and Biophysical Research Communications

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ER -

Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system

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