Phanerochaete chrysosporium and its natural substrate

• Published in: FEMS microbiology reviews Vol. 13; no. 2/3; pp. 189 - 196
• Main Authors: Broda, P, Birch, P, Brooks, P, Copa-Patino, J.L, Sinnott, M.L, Tempelaars, C, Wang, Q, Wyatt, A, Sims, P
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.03.1994; Blackwell
• Subjects: Basidiomycota - enzymology; Basidiomycota - genetics; Biodegradation, Environmental; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Cellobiohydrolase; Cellulose - metabolism; Cellulose 1,4-beta-Cellobiosidase; enzymes; Fundamental and applied biological sciences. Psychology; gene expression; Genes, Fungal - genetics; genetic regulation; genetic transformation; Genetics; Glycoside Hydrolases - genetics; Glycoside Hydrolases - metabolism; Lignin; Lignin - metabolism; Lignocellulose; Mission oriented research; multigene family; Phanerochaete chrysosporium; Polymerase Chain Reaction - methods; promoter regions; reporter genes; RNA, Fungal - analysis; RNA, Messenger - analysis; Transformation; Transformation, Genetic; Xylanolytic system; β(1→3)‐glucanase; Biodegradation; Lignin; Genetic transformation; Enzyme; Basidiomycetes; Lignocellulosics; Review; Ligninolytic enzyme; Xylan 1,4-β-xylosidase; Fungi; Regulation(control); β-Glucosidase; Glycosidases; Phanerochaete chrysosporium; Wood destroying fungi; Hydrolases; Xylan endo-1,3-β-xylosidase; O-Glycosidases; Thallophyta
• ISSN: 0168-6445; 1574-6976
• DOI: 10.1111/j.1574-6976.1994.tb00042.x

We seek to define more fully how Phanerochaete chrysosporium degrades its natural substrate, lignocellulose. This contribution concerns several relevant topics. Mineralization of [(14)C]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 mineralization, extracellular lignin peroxidase activity was absent. Xylanolytic and xylosidase/ beta(1 leads to 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.