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Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader
Huge quantities of keratinaceous waste are a substantial and almost totally unexploited protein resource which could be upgraded for use as high value-added products by efficient keratinolytic enzymes. In this study, we found that Bacillus sp. 8A6 can efficiently degrade chicken feather after 24 h g...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7308268/ https://www.ncbi.nlm.nih.gov/pubmed/32572051 http://dx.doi.org/10.1038/s41598-020-66792-2 |
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author | Huang, Yuhong Łężyk, Mateusz Herbst, Florian-Alexander Busk, Peter Kamp Lange, Lene |
author_facet | Huang, Yuhong Łężyk, Mateusz Herbst, Florian-Alexander Busk, Peter Kamp Lange, Lene |
author_sort | Huang, Yuhong |
collection | PubMed |
description | Huge quantities of keratinaceous waste are a substantial and almost totally unexploited protein resource which could be upgraded for use as high value-added products by efficient keratinolytic enzymes. In this study, we found that Bacillus sp. 8A6 can efficiently degrade chicken feather after 24 h growth. According to phylogenetic analysis, the strain (formerly identified as Bacillus pumilus 8A6) belongs to the B. pumilus species clade but it is more closely related to B. safensis. Hotpep predicted 233 putative proteases from Bacillus sp. 8A6 genome. Proteomic analysis of culture broths from Bacillus sp. 8A6 cultured on chicken feathers or on a mixture of bristles and hooves showed high abundance of proteins with functions related to peptidase activity. Five proteases (one from family M12, one from family S01A, two from family S08A and one from family T3) and four oligopeptide and dipeptide binding proteins were highly expressed when Bacillus sp. 8A6 was grown in keratin media compared to LB medium. This study is the first to report that bacterial proteases in families M12, S01A and T3 are involved in keratin degradation together with proteases from family S08. |
format | Online Article Text |
id | pubmed-7308268 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73082682020-06-23 Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader Huang, Yuhong Łężyk, Mateusz Herbst, Florian-Alexander Busk, Peter Kamp Lange, Lene Sci Rep Article Huge quantities of keratinaceous waste are a substantial and almost totally unexploited protein resource which could be upgraded for use as high value-added products by efficient keratinolytic enzymes. In this study, we found that Bacillus sp. 8A6 can efficiently degrade chicken feather after 24 h growth. According to phylogenetic analysis, the strain (formerly identified as Bacillus pumilus 8A6) belongs to the B. pumilus species clade but it is more closely related to B. safensis. Hotpep predicted 233 putative proteases from Bacillus sp. 8A6 genome. Proteomic analysis of culture broths from Bacillus sp. 8A6 cultured on chicken feathers or on a mixture of bristles and hooves showed high abundance of proteins with functions related to peptidase activity. Five proteases (one from family M12, one from family S01A, two from family S08A and one from family T3) and four oligopeptide and dipeptide binding proteins were highly expressed when Bacillus sp. 8A6 was grown in keratin media compared to LB medium. This study is the first to report that bacterial proteases in families M12, S01A and T3 are involved in keratin degradation together with proteases from family S08. Nature Publishing Group UK 2020-06-22 /pmc/articles/PMC7308268/ /pubmed/32572051 http://dx.doi.org/10.1038/s41598-020-66792-2 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Huang, Yuhong Łężyk, Mateusz Herbst, Florian-Alexander Busk, Peter Kamp Lange, Lene Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
title | Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
title_full | Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
title_fullStr | Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
title_full_unstemmed | Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
title_short | Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
title_sort | novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7308268/ https://www.ncbi.nlm.nih.gov/pubmed/32572051 http://dx.doi.org/10.1038/s41598-020-66792-2 |
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