scholarly journals Cloning, expression and characterization of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium strain BKM-F-1767

2012 ◽  
Vol 12 (1) ◽  
pp. 126 ◽  
Author(s):  
Dong-Dong Yang ◽  
Jean François ◽  
Gustavo M de Billerbeck
Keyword(s):  
Alcohol Dehydrogenase ◽  
Phanerochaete Chrysosporium ◽  
White Rot ◽  
White Rot Fungus

scholarly journals Characterization of Carbohydrate-Binding Cytochrome b562 from the White-Rot Fungus Phanerochaete chrysosporium

2005 ◽  
Vol 71 (8) ◽  
pp. 4548-4555 ◽  
Author(s):  
Makoto Yoshida ◽  
Kiyohiko Igarashi ◽  
Masahisa Wada ◽  
Satoshi Kaneko ◽  
Norio Suzuki ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Carbon Catabolite Repression ◽  
White Rot ◽  
White Rot Fungus ◽  
Carbohydrate Binding ◽  
Resonance Raman Spectrum ◽  
High Affinity ◽  
Gene Transcripts

ABSTRACT cDNA encoding a hemoprotein similar to the cytochrome domain of extracellular flavocytochrome cellobiose dehydrogenase (CDH) was cloned from the white-rot fungus Phanerochaete chrysosporium. The deduced amino acid sequence implies that there is a two-domain structure consisting of an N-terminal cytochrome domain and a C-terminal family 1 carbohydrate-binding module (CBM1) but that the flavin-containing domain of CDH is not present. The gene transcripts were observed in cultures in cellulose medium but not in cultures in glucose medium, suggesting that there is regulation by carbon catabolite repression. The gene was successfully overexpressed in Pichia pastoris, and the recombinant protein was designated carbohydrate-binding cytochrome b 562 (CBCyt. b 562). The resonance Raman spectrum suggested that the heme of CBCyt. b 562 is 6-coordinated in both the ferric and ferrous states. Moreover, the redox potential measured by cyclic voltammetry was similar to that of the cytochrome domain of CDH. These results suggest that the redox characteristics may be similar to those of the cytochrome domain of CDH, and so CBCyt. b 562 may have an electron transfer function. In a binding study with various carbohydrates, CBCyt. b 562 was adsorbed with high affinity on both cellulose and chitin. As far as we know, this is the first example of a CBM1 connected to a domain without apparent catalytic activity for carbohydrate; this CBM1 may play a role in localization of the redox protein on the surface of cellulose or on the fungal sheath in vivo.

scholarly journals Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium

1991 ◽  
Vol 195 (2) ◽  
pp. 369-375 ◽  
Author(s):  
Andreas MUHEIM ◽  
Roland WALDNER ◽  
Dominique SANGLARD ◽  
Jakob REISER ◽  
Hans E. SCHOEMAKER ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Phanerochaete Chrysosporium ◽  
White Rot ◽  
White Rot Fungus ◽  
Purification And Properties
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