Phanerochaete chrysosporium and its natural substrate

P. Broda; P. Birch; P. Brooks; J. L. Copa-Patino; M. L. Sinnott; C. Tempelaars; Q. Wang; A. Wyatt; P. Sims

doi:10.1111/j.1574-6976.1994.tb00042.x

Phanerochaete chrysosporium and its natural substrate

P. Broda, P. Birch, P. Brooks, J. L. Copa-Patino, M. L. Sinnott, C. Tempelaars, Q. Wang, A. Wyatt, P. Sims

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

Abstract

We seek to define more fully how Phanerochaete chrysosporium degrades its natural substrate, lignocellulose. This contribution concerns several relevant topics. Mineralisation of [ 14C]DHP, as a model for lignin degradation, showed that a set of genetically defined meiotically derived products of strain ME446 differed in their degradative ability and also that, under optimum conditions for mineralisation, extracellular lignin peroxidase activity was absent. Xylanolytic and xylosidase/β(1 → 3) glucanase activities are also described. The complexity of the CBHI gene family is described and differential splicing of a CBHI gene transcript is proposed. In contrast to the multiplicity of CHBI genes there is a single CBHII gene. PCR methods were developed to analyse differential gene expression on different substrates. We have also developed a transformation system involving a reporter construct for the analysis of CBHI promoter function.

Original language	English
Pages (from-to)	189-195
Number of pages	6
Journal	FEMS microbiology reviews
Volume	13
Issue number	2-3
DOIs	https://doi.org/10.1111/j.1574-6976.1994.tb00042.x
Publication status	Published - 1994

Keywords

β(1 → )-glucanase
cellobiohydrolase
lignin
lignocellulose
Phanerochaete chrysosporium
transformation
xylanolytic system

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10.1111/j.1574-6976.1994.tb00042.x

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title = "Phanerochaete chrysosporium and its natural substrate",

abstract = "We seek to define more fully how Phanerochaete chrysosporium degrades its natural substrate, lignocellulose. This contribution concerns several relevant topics. Mineralisation of [ 14C]DHP, as a model for lignin degradation, showed that a set of genetically defined meiotically derived products of strain ME446 differed in their degradative ability and also that, under optimum conditions for mineralisation, extracellular lignin peroxidase activity was absent. Xylanolytic and xylosidase/β(1 → 3) glucanase activities are also described. The complexity of the CBHI gene family is described and differential splicing of a CBHI gene transcript is proposed. In contrast to the multiplicity of CHBI genes there is a single CBHII gene. PCR methods were developed to analyse differential gene expression on different substrates. We have also developed a transformation system involving a reporter construct for the analysis of CBHI promoter function.",

keywords = "β(1 → )-glucanase, cellobiohydrolase, lignin, lignocellulose, Phanerochaete chrysosporium, transformation, xylanolytic system",

author = "P. Broda and P. Birch and P. Brooks and Copa-Patino, {J. L.} and Sinnott, {M. L.} and C. Tempelaars and Q. Wang and A. Wyatt and P. Sims",

year = "1994",

doi = "10.1111/j.1574-6976.1994.tb00042.x",

language = "English",

volume = "13",

pages = "189--195",

journal = "FEMS microbiology reviews",

issn = "0168-6445",

publisher = "Oxford University Press",

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TY - JOUR

T1 - Phanerochaete chrysosporium and its natural substrate

AU - Broda, P.

AU - Birch, P.

AU - Brooks, P.

AU - Copa-Patino, J. L.

AU - Sinnott, M. L.

AU - Tempelaars, C.

AU - Wang, Q.

AU - Wyatt, A.

AU - Sims, P.

PY - 1994

Y1 - 1994

N2 - We seek to define more fully how Phanerochaete chrysosporium degrades its natural substrate, lignocellulose. This contribution concerns several relevant topics. Mineralisation of [ 14C]DHP, as a model for lignin degradation, showed that a set of genetically defined meiotically derived products of strain ME446 differed in their degradative ability and also that, under optimum conditions for mineralisation, extracellular lignin peroxidase activity was absent. Xylanolytic and xylosidase/β(1 → 3) glucanase activities are also described. The complexity of the CBHI gene family is described and differential splicing of a CBHI gene transcript is proposed. In contrast to the multiplicity of CHBI genes there is a single CBHII gene. PCR methods were developed to analyse differential gene expression on different substrates. We have also developed a transformation system involving a reporter construct for the analysis of CBHI promoter function.

AB - We seek to define more fully how Phanerochaete chrysosporium degrades its natural substrate, lignocellulose. This contribution concerns several relevant topics. Mineralisation of [ 14C]DHP, as a model for lignin degradation, showed that a set of genetically defined meiotically derived products of strain ME446 differed in their degradative ability and also that, under optimum conditions for mineralisation, extracellular lignin peroxidase activity was absent. Xylanolytic and xylosidase/β(1 → 3) glucanase activities are also described. The complexity of the CBHI gene family is described and differential splicing of a CBHI gene transcript is proposed. In contrast to the multiplicity of CHBI genes there is a single CBHII gene. PCR methods were developed to analyse differential gene expression on different substrates. We have also developed a transformation system involving a reporter construct for the analysis of CBHI promoter function.

KW - β(1 → )-glucanase

KW - cellobiohydrolase

KW - lignin

KW - lignocellulose

KW - Phanerochaete chrysosporium

KW - transformation

KW - xylanolytic system

U2 - 10.1111/j.1574-6976.1994.tb00042.x

DO - 10.1111/j.1574-6976.1994.tb00042.x

M3 - Article

SN - 0168-6445

VL - 13

SP - 189

EP - 195

JO - FEMS microbiology reviews

JF - FEMS microbiology reviews

IS - 2-3

ER -

Phanerochaete chrysosporium and its natural substrate

Abstract

Keywords

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