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Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges
BACKGROUND: Pectinase enzymes catalyze the breakdown of pectin, a key component of the plant cell wall. At industrial level, pectinases are used in diverse applications, especially in food-processing industry. Currently, most of the industrial pectinases have optimal activity at mesophilic temperatu...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6109986/ https://www.ncbi.nlm.nih.gov/pubmed/30149803 http://dx.doi.org/10.1186/s40659-018-0177-4 |
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author | Poveda, Gabriela Gil-Durán, Carlos Vaca, Inmaculada Levicán, Gloria Chávez, Renato |
author_facet | Poveda, Gabriela Gil-Durán, Carlos Vaca, Inmaculada Levicán, Gloria Chávez, Renato |
author_sort | Poveda, Gabriela |
collection | PubMed |
description | BACKGROUND: Pectinase enzymes catalyze the breakdown of pectin, a key component of the plant cell wall. At industrial level, pectinases are used in diverse applications, especially in food-processing industry. Currently, most of the industrial pectinases have optimal activity at mesophilic temperatures. On the contrary, very little is known about the pectinolytic activities from organisms from cold climates such as Antarctica. In this work, 27 filamentous fungi isolated from marine sponges collected in King George Island, Antarctica, were screened as new source of cold-active pectinases. RESULTS: In semi-quantitative plate assays, 8 out 27 of these isolates showed pectinolytic activities at 15 °C and one of them, Geomyces sp. strain F09-T3-2, showed the highest production of pectinases in liquid medium containing pectin as sole carbon source. More interesting, Geomyces sp. F09-T3-2 showed optimal pectinolytic activity at 30 °C, 10 °C under the temperature of currently available commercial mesophilic pectinases. CONCLUSION: Filamentous fungi associated with Antarctic marine sponges are a promising source of pectinolytic activity. In particular, pectinases from Geomyces sp. F09-T3-2 may be potentially suitable for biotechnological applications needing cold-active pectinases. To the best of our knowledge, this is the first report describing the production of pectinolytic activity from filamentous fungi from any environment in Antarctica. |
format | Online Article Text |
id | pubmed-6109986 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-61099862018-08-28 Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges Poveda, Gabriela Gil-Durán, Carlos Vaca, Inmaculada Levicán, Gloria Chávez, Renato Biol Res Research Article BACKGROUND: Pectinase enzymes catalyze the breakdown of pectin, a key component of the plant cell wall. At industrial level, pectinases are used in diverse applications, especially in food-processing industry. Currently, most of the industrial pectinases have optimal activity at mesophilic temperatures. On the contrary, very little is known about the pectinolytic activities from organisms from cold climates such as Antarctica. In this work, 27 filamentous fungi isolated from marine sponges collected in King George Island, Antarctica, were screened as new source of cold-active pectinases. RESULTS: In semi-quantitative plate assays, 8 out 27 of these isolates showed pectinolytic activities at 15 °C and one of them, Geomyces sp. strain F09-T3-2, showed the highest production of pectinases in liquid medium containing pectin as sole carbon source. More interesting, Geomyces sp. F09-T3-2 showed optimal pectinolytic activity at 30 °C, 10 °C under the temperature of currently available commercial mesophilic pectinases. CONCLUSION: Filamentous fungi associated with Antarctic marine sponges are a promising source of pectinolytic activity. In particular, pectinases from Geomyces sp. F09-T3-2 may be potentially suitable for biotechnological applications needing cold-active pectinases. To the best of our knowledge, this is the first report describing the production of pectinolytic activity from filamentous fungi from any environment in Antarctica. BioMed Central 2018-08-27 /pmc/articles/PMC6109986/ /pubmed/30149803 http://dx.doi.org/10.1186/s40659-018-0177-4 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Poveda, Gabriela Gil-Durán, Carlos Vaca, Inmaculada Levicán, Gloria Chávez, Renato Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges |
title | Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges |
title_full | Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges |
title_fullStr | Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges |
title_full_unstemmed | Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges |
title_short | Cold-active pectinolytic activity produced by filamentous fungi associated with Antarctic marine sponges |
title_sort | cold-active pectinolytic activity produced by filamentous fungi associated with antarctic marine sponges |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6109986/ https://www.ncbi.nlm.nih.gov/pubmed/30149803 http://dx.doi.org/10.1186/s40659-018-0177-4 |
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