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Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
In this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and α-amylase. The pri...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Sociedade Brasileira de Microbiologia
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768745/ https://www.ncbi.nlm.nih.gov/pubmed/24031793 http://dx.doi.org/10.1590/S1517-838220110004000046 |
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author | Umsza-Guez, Marcelo A. Díaz, Ana B. de Ory, Ignacio Blandino, Ana Gomes, Eleni Caro, Ildefonso |
author_facet | Umsza-Guez, Marcelo A. Díaz, Ana B. de Ory, Ignacio Blandino, Ana Gomes, Eleni Caro, Ildefonso |
author_sort | Umsza-Guez, Marcelo A. |
collection | PubMed |
description | In this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and α-amylase. The principal step of the process is the solid state fermentation (SSF) of this residue by Aspergillus awamori. In several laboratory experiments, maximum xylanase and exo-PG activities were measured during the first days of culture, reaching values around 100 and 80 IU/gds (international units of enzyme activity per gram of dried solid), respectively. For CMCase and α-amylase production remained almost constant along fermentation, with average values of 19 and 21.5 IU/gds, respectively. Experiments carried out in a plate-type bioreactor at lab scale showed a clear positive effect of aeration on xylanase and CMCase, while the opposite was observed for exo-PG and α-amylase. In general, xylanase was the enzyme produced in higher levels, thus the optimum conditions for the determination of the enzyme activity was characterized. The xylanase activity shows an optimum pH of 5 and an optimum temperature of 50 ºC. The enzyme is activated by Mg(2+), but strongly inhibited by Hg(2+) and Cu(2+). The enzymatic activity remains quite high if the extract is preserved in a range of pH from 3 to 10 and a temperature between 30 ºC to 40 ºC. |
format | Online Article Text |
id | pubmed-3768745 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Sociedade Brasileira de Microbiologia |
record_format | MEDLINE/PubMed |
spelling | pubmed-37687452013-09-12 Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace Umsza-Guez, Marcelo A. Díaz, Ana B. de Ory, Ignacio Blandino, Ana Gomes, Eleni Caro, Ildefonso Braz J Microbiol Microbial Physiology In this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and α-amylase. The principal step of the process is the solid state fermentation (SSF) of this residue by Aspergillus awamori. In several laboratory experiments, maximum xylanase and exo-PG activities were measured during the first days of culture, reaching values around 100 and 80 IU/gds (international units of enzyme activity per gram of dried solid), respectively. For CMCase and α-amylase production remained almost constant along fermentation, with average values of 19 and 21.5 IU/gds, respectively. Experiments carried out in a plate-type bioreactor at lab scale showed a clear positive effect of aeration on xylanase and CMCase, while the opposite was observed for exo-PG and α-amylase. In general, xylanase was the enzyme produced in higher levels, thus the optimum conditions for the determination of the enzyme activity was characterized. The xylanase activity shows an optimum pH of 5 and an optimum temperature of 50 ºC. The enzyme is activated by Mg(2+), but strongly inhibited by Hg(2+) and Cu(2+). The enzymatic activity remains quite high if the extract is preserved in a range of pH from 3 to 10 and a temperature between 30 ºC to 40 ºC. Sociedade Brasileira de Microbiologia 2011 2011-12-01 /pmc/articles/PMC3768745/ /pubmed/24031793 http://dx.doi.org/10.1590/S1517-838220110004000046 Text en © Sociedade Brasileira de Microbiologia http://creativecommons.org/licenses/by-nc/3.0/ All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License |
spellingShingle | Microbial Physiology Umsza-Guez, Marcelo A. Díaz, Ana B. de Ory, Ignacio Blandino, Ana Gomes, Eleni Caro, Ildefonso Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace |
title | Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace |
title_full | Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace |
title_fullStr | Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace |
title_full_unstemmed | Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace |
title_short | Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace |
title_sort | xylanase production by aspergillus awamori under solid state fermentation conditions on tomato pomace |
topic | Microbial Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768745/ https://www.ncbi.nlm.nih.gov/pubmed/24031793 http://dx.doi.org/10.1590/S1517-838220110004000046 |
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