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Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern

Salterns are hypersaline environments that are inhabited by diverse halophilic microorganisms, including fungi. In this study, we isolated a fungal strain SK1-1 from a saltern in the Republic of Korea, which was identified as Asperillus reticulatus. This is the first reported saline-environment-deri...

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Autores principales: Chung, Dawoon, Yu, Woon-Jong, Lim, Ji-Yeon, Kang, Nam-Seon, Kwon, Yong-Min, Choi, Grace, Bae, Seung-Sub, Cho, Kichul, Lee, Dae-Sung
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8781784/
https://www.ncbi.nlm.nih.gov/pubmed/35056479
http://dx.doi.org/10.3390/microorganisms10010029
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author Chung, Dawoon
Yu, Woon-Jong
Lim, Ji-Yeon
Kang, Nam-Seon
Kwon, Yong-Min
Choi, Grace
Bae, Seung-Sub
Cho, Kichul
Lee, Dae-Sung
author_facet Chung, Dawoon
Yu, Woon-Jong
Lim, Ji-Yeon
Kang, Nam-Seon
Kwon, Yong-Min
Choi, Grace
Bae, Seung-Sub
Cho, Kichul
Lee, Dae-Sung
author_sort Chung, Dawoon
collection PubMed
description Salterns are hypersaline environments that are inhabited by diverse halophilic microorganisms, including fungi. In this study, we isolated a fungal strain SK1-1 from a saltern in the Republic of Korea, which was identified as Asperillus reticulatus. This is the first reported saline-environment-derived A. reticulatus that belongs to the Aspergillus penicillioides clade and encompasses xerophilic fungi. SK1-1 was halophilic, obligately requiring NaCl for growth, with a maximum radial growth of 6%–9% (w/v) NaCl. To facilitate the biotechnological application of halophilic fungi, we screened the SK1-1 strain for proteolytic activity. Proteases have widespread applications in food processing, detergents, textiles, and waste treatment, and halophilic proteases can enable protein degradation in high salt environments. We assessed the proteolytic activity of the extracellular crude enzyme of SK1-1 using azocasein as a substrate. The crude protease exhibited maximum activity at 40–50 °C, pH 9.5–10.5, and in the absence of NaCl. It was also able to retain up to 69% of its maximum activity until 7% NaCl. Protease inhibitor assays showed complete inhibition of the proteolytic activity of crude enzymes by Pefabloc(®) SC. Our data suggest that the halophilic A. reticulatus strain SK1-1 produces an extracellular alkaline serine protease.
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spelling pubmed-87817842022-01-22 Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern Chung, Dawoon Yu, Woon-Jong Lim, Ji-Yeon Kang, Nam-Seon Kwon, Yong-Min Choi, Grace Bae, Seung-Sub Cho, Kichul Lee, Dae-Sung Microorganisms Article Salterns are hypersaline environments that are inhabited by diverse halophilic microorganisms, including fungi. In this study, we isolated a fungal strain SK1-1 from a saltern in the Republic of Korea, which was identified as Asperillus reticulatus. This is the first reported saline-environment-derived A. reticulatus that belongs to the Aspergillus penicillioides clade and encompasses xerophilic fungi. SK1-1 was halophilic, obligately requiring NaCl for growth, with a maximum radial growth of 6%–9% (w/v) NaCl. To facilitate the biotechnological application of halophilic fungi, we screened the SK1-1 strain for proteolytic activity. Proteases have widespread applications in food processing, detergents, textiles, and waste treatment, and halophilic proteases can enable protein degradation in high salt environments. We assessed the proteolytic activity of the extracellular crude enzyme of SK1-1 using azocasein as a substrate. The crude protease exhibited maximum activity at 40–50 °C, pH 9.5–10.5, and in the absence of NaCl. It was also able to retain up to 69% of its maximum activity until 7% NaCl. Protease inhibitor assays showed complete inhibition of the proteolytic activity of crude enzymes by Pefabloc(®) SC. Our data suggest that the halophilic A. reticulatus strain SK1-1 produces an extracellular alkaline serine protease. MDPI 2021-12-24 /pmc/articles/PMC8781784/ /pubmed/35056479 http://dx.doi.org/10.3390/microorganisms10010029 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Chung, Dawoon
Yu, Woon-Jong
Lim, Ji-Yeon
Kang, Nam-Seon
Kwon, Yong-Min
Choi, Grace
Bae, Seung-Sub
Cho, Kichul
Lee, Dae-Sung
Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern
title Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern
title_full Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern
title_fullStr Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern
title_full_unstemmed Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern
title_short Characterization of the Proteolytic Activity of a Halophilic Aspergillus reticulatus Strain SK1-1 Isolated from a Solar Saltern
title_sort characterization of the proteolytic activity of a halophilic aspergillus reticulatus strain sk1-1 isolated from a solar saltern
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8781784/
https://www.ncbi.nlm.nih.gov/pubmed/35056479
http://dx.doi.org/10.3390/microorganisms10010029
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