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Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1

The production of xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by Aspergillus awamori 2B.361 U2/1, a hyper producer of glucoamylase and pectinase, was evaluated using selected conditions regarding nitrogen nutrition. Submerged cultivations were carried out at 30 °C and 200 rpm in...

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Autores principales: Gottschalk, Leda Maria Fortes, de Sousa Paredes, Raquel, Teixeira, Ricardo Sposina Sobral, da Silva, Ayla Sant’Ana, da Silva Bon, Elba Pinto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Brazilian Society of Microbiology 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3833162/
https://www.ncbi.nlm.nih.gov/pubmed/24294256
http://dx.doi.org/10.1590/S1517-83822013000200037
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author Gottschalk, Leda Maria Fortes
de Sousa Paredes, Raquel
Teixeira, Ricardo Sposina Sobral
da Silva, Ayla Sant’Ana
da Silva Bon, Elba Pinto
author_facet Gottschalk, Leda Maria Fortes
de Sousa Paredes, Raquel
Teixeira, Ricardo Sposina Sobral
da Silva, Ayla Sant’Ana
da Silva Bon, Elba Pinto
author_sort Gottschalk, Leda Maria Fortes
collection PubMed
description The production of xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by Aspergillus awamori 2B.361 U2/1, a hyper producer of glucoamylase and pectinase, was evaluated using selected conditions regarding nitrogen nutrition. Submerged cultivations were carried out at 30 °C and 200 rpm in growth media containing 30 g wheat bran/L as main carbon source and either yeast extract, ammonium sulfate, sodium nitrate or urea, as nitrogen sources; in all cases it was used a fixed molar carbon to molar nitrogen concentration of 10.3. The use of poor nitrogen sources favored the accumulation of xylanase, β-xylosidase and ferulic acid esterase to a peak concentrations of 44,880; 640 and 118 U/L, respectively, for sodium nitrate and of 34,580, 685 and 170 U/L, respectively, for urea. However, the highest β-glucosidase accumulation of 10,470 U/L was observed when the rich organic nitrogen source yeast extract was used. The maxima accumulation of filter paper activity, xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by A. awamori 2B.361 U2/1 was compared to that produced by Trichoderma reesei Rut-C30. The level of β-glucosidase was over 17-fold higher for the Aspergillus strain, whereas the levels of xylanase and β-xylosidase were over 2-fold higher. This strain also produced ferulic acid esterase (170 U/L), which was not detected in the T. reesei culture.
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spelling pubmed-38331622013-11-30 Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1 Gottschalk, Leda Maria Fortes de Sousa Paredes, Raquel Teixeira, Ricardo Sposina Sobral da Silva, Ayla Sant’Ana da Silva Bon, Elba Pinto Braz J Microbiol Research Paper The production of xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by Aspergillus awamori 2B.361 U2/1, a hyper producer of glucoamylase and pectinase, was evaluated using selected conditions regarding nitrogen nutrition. Submerged cultivations were carried out at 30 °C and 200 rpm in growth media containing 30 g wheat bran/L as main carbon source and either yeast extract, ammonium sulfate, sodium nitrate or urea, as nitrogen sources; in all cases it was used a fixed molar carbon to molar nitrogen concentration of 10.3. The use of poor nitrogen sources favored the accumulation of xylanase, β-xylosidase and ferulic acid esterase to a peak concentrations of 44,880; 640 and 118 U/L, respectively, for sodium nitrate and of 34,580, 685 and 170 U/L, respectively, for urea. However, the highest β-glucosidase accumulation of 10,470 U/L was observed when the rich organic nitrogen source yeast extract was used. The maxima accumulation of filter paper activity, xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by A. awamori 2B.361 U2/1 was compared to that produced by Trichoderma reesei Rut-C30. The level of β-glucosidase was over 17-fold higher for the Aspergillus strain, whereas the levels of xylanase and β-xylosidase were over 2-fold higher. This strain also produced ferulic acid esterase (170 U/L), which was not detected in the T. reesei culture. Brazilian Society of Microbiology 2013-10-30 /pmc/articles/PMC3833162/ /pubmed/24294256 http://dx.doi.org/10.1590/S1517-83822013000200037 Text en Copyright © 2013, Sociedade Brasileira de Microbiologia All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License CC BY-NC.
spellingShingle Research Paper
Gottschalk, Leda Maria Fortes
de Sousa Paredes, Raquel
Teixeira, Ricardo Sposina Sobral
da Silva, Ayla Sant’Ana
da Silva Bon, Elba Pinto
Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
title Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
title_full Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
title_fullStr Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
title_full_unstemmed Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
title_short Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
title_sort efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain aspergillus awamori 2b.361 u2/1
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3833162/
https://www.ncbi.nlm.nih.gov/pubmed/24294256
http://dx.doi.org/10.1590/S1517-83822013000200037
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