scholarly journals Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main α-galactosidase

1999 ◽  
Vol 339 (1) ◽  
pp. 43 ◽  
Author(s):  
Harry BRUMER III ◽  
Paul F.G. SIMS ◽  
Michael L. SINNOTT
1999 ◽  
Vol 25 (3-5) ◽  
pp. 392-399 ◽  
Author(s):  
Raziye Öztürk ◽  
L.Arzu Bozkaya ◽  
Esin Atav ◽  
Necdet Sağlam ◽  
Leman Tarhan

2004 ◽  
Vol 70 (10) ◽  
pp. 5794-5800 ◽  
Author(s):  
Theodorus H. de Koker ◽  
Michael D. Mozuch ◽  
Daniel Cullen ◽  
Jill Gaskell ◽  
Philip J. Kersten

ABSTRACT Pyranose 2-oxidase (POX) was recovered from Phanerochaete chrysosporium BKM-F-1767 solid substrate culture using mild extraction conditions and was purified. 13C-nuclear magnetic resonance confirmed production of d-arabino-hexos-2-ulose (glucosone) from d-glucose with the oxidase. Peptide fingerprints generated by liquid chromatography-tandem mass spectrometry of tryptic digests and analysis of the corresponding cDNA revealed a structurally unusual sequence for the P. chrysosporium POX. Relatively high levels of pox transcript were detected under carbon-starved culture conditions but not under nutrient sufficiency. This regulation pattern is similar to that observed for lignin peroxidases, manganese peroxidases, and glyoxal oxidase of P. chrysosporium, supporting evidence that POX has a role in lignocellulose degradation.


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