Abstract:Alcohol oxidase from Candida methanosorbosa was purified about sixfold with a yield of 37.6% from the culture broth of Candida methanosorbosa M-2003. The enzyme preparation was homogeneous on slab gel electrophoresis. The purified enzyme had an optimal pH from 6.0 to 9.0 and was stable in the range 6.0-8.5. Its optimal temperature of reaction was 50 degrees C, and it was stable below 50 degrees C. In the presence of NaN3, the enzyme retained its initial activity at 30 degrees C for 35 days, indicating stabilit… Show more
“…Este tipo de compuesto volátil y otros aldehídos grasos conforman el grupo de VOC's del aroma y fragancia; los cuales además son una herramienta para la diferenciación de especies de hongos comestibles y/o permiten identificar el estado de conservación/almacenamiento de las setas, pues derivan de productos de degradación u oxidación de lípidos (249). No hay claridad del rol biológico en hongos, pero se ha observado su influencia junto con los alcoholes para, estimular el crecimiento cuando se manifiesta en la interacción entre diferentes especies fúngicas (250), facilitar la infección en plantas (251), en insectos (252), como intermediarios del metabolismo de ácidos grasos (231), del metabolismo de alcoholes primarios o de piruvato para posteriormente poder reducirlo a etanol en procesos fermentativos (253)(254)(255).…”
“…Este tipo de compuesto volátil y otros aldehídos grasos conforman el grupo de VOC's del aroma y fragancia; los cuales además son una herramienta para la diferenciación de especies de hongos comestibles y/o permiten identificar el estado de conservación/almacenamiento de las setas, pues derivan de productos de degradación u oxidación de lípidos (249). No hay claridad del rol biológico en hongos, pero se ha observado su influencia junto con los alcoholes para, estimular el crecimiento cuando se manifiesta en la interacción entre diferentes especies fúngicas (250), facilitar la infección en plantas (251), en insectos (252), como intermediarios del metabolismo de ácidos grasos (231), del metabolismo de alcoholes primarios o de piruvato para posteriormente poder reducirlo a etanol en procesos fermentativos (253)(254)(255).…”
“…5a) with the NAT embedded in the ST. GL25583 encoded a candidate alcohol oxidase (Supplementary File 3a). Alcohol oxidase catalyzed the reaction that converts a primary alcohol and O 2 to an aldehyde and H 2 O 2
41 . Both GL25583 and AT22678 appeared to have introns.…”
Ganoderma lucidum is a white-rot fungus best-known for its medicinal and ligninolytic activities. To discover the underlying genes responsible for these activities, we identified and characterized the natural antisense transcripts (NATs) using strand-specific (ss) RNA-seq data obtained from the mycelia, primordia and fruiting bodies. NATs were identified using a custom pipeline and then subjected to functional enrichment and differential expression analyses. A total of 1613 cis- and 244 trans- sense and antisense transcripts were identified. Mapping to GO terms and KEGG pathways revealed that NATs were frequently associated with genes of particular functional categories in particular stages. ssRT-qPCR experiments showed that the expression profiles of 30 of 50 (60%) transcripts were highly correlated with those of the RNA-seq results (r ≥ 0.9). Expression profiles of 22 of 25 (88%) pairs of NATs and STs were highly correlated (p ≤ 0.01), with 15 having r ≥ 0.8 and 4 having r ≤ -0.8. Six lignin-modifying genes and their NATs were analyzed in detail. Diverse patterns of differential expression among different stages and positive and negative correlations were observed. These results suggested that NATs were implicated in gene expression regulation in a function-group and developmental-stage specific manner through complex mechanisms.
Short chain alcohol oxidase (SCAO), long chain alcohol oxidase (LCAO), secondary alcohol oxidase (SAO), and aryl alcohol oxidase (AAO) activities were localized in the microsome of Aspergillus terreus during growth of the fungi on n-hexadecane. Zymogram analysis of the microsomes of n-hexadecane-grown cells in polyacrylamide gel electrophoresis showed distinct bands, H4, H3, H2, and H1, in a sequence of their molecular weight (Mr) from high to low. The Mr of the isozymes corresponding to the bands H4, H3, and H2 were close to each other and were higher than 272 kDa. While, the Mr of the isozyme H1 was found to be approximately 48 kDa. H1 gave activity only as SCAO. Although the substrates for other bands were varied, strong (S), medium (M), and weak (W) activity for the bands were as follows: H2: SAO (S), AAO (S), LCAO (M), SCAO (S); H3: LCAO (S), SCAO (S); H4: SCAO (S), LCAO (W), SAO (W). The pH and temperature optima of these isozymes were found to be 8.5+/-0.5 and 30+/-1 degrees C, respectively. The stability of the isozymes was drastically decreased beyond 30 degrees C. The SAO showed 33% enantiomeric excess for the R(-)2-octanol over S(+)2-octanol, which may be correlated with the lower Michaelis-Menten constant (K (M)) values of the enzyme for the R(-)2-octanol than the S(+)2-octanol. The fluorescence emission spectra of the chromatographically purified SCAO at 443 nm excitation were similar to that obtained with authentic flavin adenine dinucleotide.
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