Cellulose and xylan degrading enzymes in Thecotheus pelletieri
The ability to produce cellulose and xylan degrading enzymes by different strains of Thecotheus pelletieri, in liquid synthetic media with cellulose and xylan as inducers, was compared. All the strains tested were able to grow and produce cellulases and xylanases, being the strain BAFC 2077 the best...
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2000
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03257541_v32_n4_p190_Pardo http://hdl.handle.net/20.500.12110/paper_03257541_v32_n4_p190_Pardo |
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paper:paper_03257541_v32_n4_p190_Pardo2023-06-08T15:32:49Z Cellulose and xylan degrading enzymes in Thecotheus pelletieri Cellulases Fungi Thecotheus pelletieri Xylanases asparagine cellulase cellulose cycloheximide ethidium bromide glucose nitrogen surfactant xylan xylan endo 1,3 beta xylosidase xylose article culture medium degradation enzyme induction enzyme synthesis fungus fungus growth nitrogen fixation nonhuman protein synthesis inhibition Thecotheus pelletieri Ascomycota Cellulase Cellulose Fungal Proteins Manure Xylan Endo-1,3-beta-Xylosidase Xylans Xylosidases The ability to produce cellulose and xylan degrading enzymes by different strains of Thecotheus pelletieri, in liquid synthetic media with cellulose and xylan as inducers, was compared. All the strains tested were able to grow and produce cellulases and xylanases, being the strain BAFC 2077 the best producer. Several cultural conditions were analysed in order to optimise enzyme production by strain 2077. Shaking cultures gave higher yields of cellulases and xylanases compared with stationary ones. Asparagine at 0.75 g N/L was the best nitrogen source in promoting enzyme production. The influence of different surfactants on enzyme production was studied. Tween 80 exhibited no effect on growth and enzyme production, whereas Tween 20 and Triton X-100 were inhibitory. By means of studies of variation of cellulose/xylan ratio in the culture medium we determined that cellulose and xylan induced cellulase and xylanase synthesis, being the specific substrates the most effective. The inducible behavior of cellulases and xylanases in T. pelletieri was determined by means of inhibition of protein synthesis by cycloheximide and ethidium bromide. Moreover, we found that glucose as well as xylose repressed cellulase and xylanase synthesis in T. pelletieri. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03257541_v32_n4_p190_Pardo http://hdl.handle.net/20.500.12110/paper_03257541_v32_n4_p190_Pardo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Cellulases Fungi Thecotheus pelletieri Xylanases asparagine cellulase cellulose cycloheximide ethidium bromide glucose nitrogen surfactant xylan xylan endo 1,3 beta xylosidase xylose article culture medium degradation enzyme induction enzyme synthesis fungus fungus growth nitrogen fixation nonhuman protein synthesis inhibition Thecotheus pelletieri Ascomycota Cellulase Cellulose Fungal Proteins Manure Xylan Endo-1,3-beta-Xylosidase Xylans Xylosidases |
| spellingShingle |
Cellulases Fungi Thecotheus pelletieri Xylanases asparagine cellulase cellulose cycloheximide ethidium bromide glucose nitrogen surfactant xylan xylan endo 1,3 beta xylosidase xylose article culture medium degradation enzyme induction enzyme synthesis fungus fungus growth nitrogen fixation nonhuman protein synthesis inhibition Thecotheus pelletieri Ascomycota Cellulase Cellulose Fungal Proteins Manure Xylan Endo-1,3-beta-Xylosidase Xylans Xylosidases Cellulose and xylan degrading enzymes in Thecotheus pelletieri |
| topic_facet |
Cellulases Fungi Thecotheus pelletieri Xylanases asparagine cellulase cellulose cycloheximide ethidium bromide glucose nitrogen surfactant xylan xylan endo 1,3 beta xylosidase xylose article culture medium degradation enzyme induction enzyme synthesis fungus fungus growth nitrogen fixation nonhuman protein synthesis inhibition Thecotheus pelletieri Ascomycota Cellulase Cellulose Fungal Proteins Manure Xylan Endo-1,3-beta-Xylosidase Xylans Xylosidases |
| description |
The ability to produce cellulose and xylan degrading enzymes by different strains of Thecotheus pelletieri, in liquid synthetic media with cellulose and xylan as inducers, was compared. All the strains tested were able to grow and produce cellulases and xylanases, being the strain BAFC 2077 the best producer. Several cultural conditions were analysed in order to optimise enzyme production by strain 2077. Shaking cultures gave higher yields of cellulases and xylanases compared with stationary ones. Asparagine at 0.75 g N/L was the best nitrogen source in promoting enzyme production. The influence of different surfactants on enzyme production was studied. Tween 80 exhibited no effect on growth and enzyme production, whereas Tween 20 and Triton X-100 were inhibitory. By means of studies of variation of cellulose/xylan ratio in the culture medium we determined that cellulose and xylan induced cellulase and xylanase synthesis, being the specific substrates the most effective. The inducible behavior of cellulases and xylanases in T. pelletieri was determined by means of inhibition of protein synthesis by cycloheximide and ethidium bromide. Moreover, we found that glucose as well as xylose repressed cellulase and xylanase synthesis in T. pelletieri. |
| title |
Cellulose and xylan degrading enzymes in Thecotheus pelletieri |
| title_short |
Cellulose and xylan degrading enzymes in Thecotheus pelletieri |
| title_full |
Cellulose and xylan degrading enzymes in Thecotheus pelletieri |
| title_fullStr |
Cellulose and xylan degrading enzymes in Thecotheus pelletieri |
| title_full_unstemmed |
Cellulose and xylan degrading enzymes in Thecotheus pelletieri |
| title_sort |
cellulose and xylan degrading enzymes in thecotheus pelletieri |
| publishDate |
2000 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03257541_v32_n4_p190_Pardo http://hdl.handle.net/20.500.12110/paper_03257541_v32_n4_p190_Pardo |
| _version_ |
1768543182270758912 |