scholarly journals Structure-Based Engineering of Phanerochaete chrysosporium Alcohol Oxidase for Enhanced Oxidative Power toward Glycerol

Biochemistry ◽  
2018 ◽  
Vol 57 (43) ◽  
pp. 6209-6218 ◽  
Author(s):  
Quoc-Thai Nguyen ◽  
Elvira Romero ◽  
Willem P. Dijkman ◽  
Suzan Pantaroto de Vasconcellos ◽  
Claudia Binda ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Alcohol Oxidase

scholarly journals Differential Expression in Phanerochaete chrysosporium of Membrane-Associated Proteins Relevant to Lignin Degradation

2008 ◽  
Vol 74 (23) ◽  
pp. 7252-7257 ◽  
Author(s):  
Semarjit Shary ◽  
Alexander N. Kapich ◽  
Ellen A. Panisko ◽  
Jon K. Magnuson ◽  
Daniel Cullen ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Protein Identification ◽  
Plasma Membranes ◽  
Alcohol Oxidase ◽  
White Rot ◽  
Rna Transcripts ◽  
Reverse Transcription Pcr ◽  
Liquid Chromatography Tandem Mass ◽  
Associated Proteins ◽  
Comparison Of The Results

ABSTRACT Fungal lignin-degrading systems likely include membrane-associated proteins that participate in diverse processes such as uptake and oxidation of lignin fragments, production of ligninolytic secondary metabolites, and defense of the mycelium against ligninolytic oxidants. Little is known about the nature or regulation of these membrane-associated components. We grew the white rot basidiomycete Phanerochaete chrysosporium on cellulose or glucose as the carbon source and monitored the mineralization of a 14C-labeled synthetic lignin by these cultures to assess their ligninolytic competence. The results showed that the cellulose-grown cultures were ligninolytic, whereas the glucose-grown ones were not. We isolated microsomal membrane fractions from both types of culture and analyzed tryptic digests of their proteins by shotgun liquid chromatography-tandem mass spectrometry. Comparison of the results against the predicted P. chrysosporium proteome showed that a catalase (Joint Genome Institute P. chrysosporium protein identification number [I.D.] 124398), an alcohol oxidase (126879), two transporters (137220 and 132234), and two cytochrome P450s (5011 and 8912) were upregulated under ligninolytic conditions. Quantitative reverse transcription-PCR assays showed that RNA transcripts encoding all of these proteins were also more abundant in ligninolytic cultures. Catalase 124398, alcohol oxidase 126879, and transporter 137220 were found in a proteomic analysis of partially purified plasma membranes from ligninolytic P. chrysosporium and are therefore most likely associated with the outer envelope of the fungus.

An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity

2014 ◽  
Vol 61-62 ◽  
pp. 7-12 ◽  
Author(s):  
Diana Linke ◽  
Nicole Lehnert ◽  
Manfred Nimtz ◽  
Ralf G. Berger
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Oxidase Activity ◽  
Alcohol Oxidase

Decolorisation of natural organic matter by Phanerochaete chrysosporium: the effect of environmental conditions

2004 ◽  
Vol 4 (4) ◽  
pp. 175-182 ◽  
Author(s):  
K. Rojek ◽  
F.A. Roddick ◽  
A. Parkinson
Keyword(s):  
Organic Matter ◽  
Ionic Strength ◽  
Natural Organic Matter ◽  
Phanerochaete Chrysosporium ◽  
Fungal Growth ◽  
Low Ph ◽  
Colour Removal ◽  
Humic Material ◽  
Carbon And Nitrogen ◽  
Carbon And Nitrogen Content

Phanerochaete chrysosporium was shown to rapidly decolorise a solution of natural organic matter (NOM). The effect of various parameters such as carbon and nitrogen content, pH, ionic strength, NOM concentration and addition of Mn2+ on the colour removal process was investigated. The rapid decolorisation was related to fungal growth and biosorption rather than biodegradation as neither carbon nor nitrogen limitation, nor Mn2+ addition, triggered the decolorisation process. Low pH (pH 3) and increased ionic strength (up to 50 g L‒1 added NaCl) led to greater specific removal (NOM/unit biomass), probably due to increased electrostatic bonding between the humic material and the biomass. Adsorption of NOM with viable and inactivated (autoclaved or by sodium azide) fungal pellets occurred within 24 hours and the colour removal depended on the viability, method of inactivation and pH. Colour removal by viable pellets was higher under the same conditions, and this, combined with desorption data, confirmed that fungal metabolic activity was important in the decolorisation process. Overall, removals of up to 40–50% NOM from solution were obtained. Of this, removal by adsorption was estimated as 60–70%, half of which was physicochemical, the other half metabolically-dependent biosorption and bioaccumulation. The remainder was considered to be removed by biodegradation, although some of this may be ascribed to bioaccumulation and metabolically-dependent biosorption.

scholarly journals Positive Selection of Novel Peroxisome Biogenesis-Defective Mutants of the Yeast Pichia pastoris

Genetics ◽  
1999 ◽  
Vol 151 (4) ◽  
pp. 1379-1391
Author(s):  
Monique A Johnson ◽  
Hans R Waterham ◽  
Galyna P Ksheminska ◽  
Liubov R Fayura ◽  
Joan Lin Cereghino ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Allyl Alcohol ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeast ◽  
Direct Selection ◽  
Toxic Exposure ◽  
Peroxisome Biogenesis ◽  
Yeast Pichia Pastoris ◽  
Methylotrophic Yeast Pichia Pastoris ◽  
Selection Of

Abstract We have developed two novel schemes for the direct selection of peroxisome-biogenesis-defective (pex) mutants of the methylotrophic yeast Pichia pastoris. Both schemes take advantage of our observation that methanol-induced pex mutants contain little or no alcohol oxidase (AOX) activity. AOX is a peroxisomal matrix enzyme that catalyzes the first step in the methanol-utilization pathway. One scheme utilizes allyl alcohol, a compound that is not toxic to cells but is oxidized by AOX to acrolein, a compound that is toxic. Exposure of mutagenized populations of AOX-induced cells to allyl alcohol selectively kills AOX-containing cells. However, pex mutants without AOX are able to grow. The second scheme utilizes a P. pastoris strain that is defective in formaldehyde dehydrogenase (FLD), a methanol pathway enzyme required to metabolize formaldehyde, the product of AOX. AOX-induced cells of fld1 strains are sensitive to methanol because of the accumulation of formaldehyde. However, fld1 pex mutants, with little active AOX, do not efficiently oxidize methanol to formaldehyde and therefore are not sensitive to methanol. Using these selections, new pex mutant alleles in previously identified PEX genes have been isolated along with mutants in three previously unidentified PEX groups.

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