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...
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| Veröffentlicht in: | Scientific reports 2020-06, Vol.10 (1), p.10033-10033, Article 10033 |
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| creator | Huang, Yuhong Łężyk, Mateusz Herbst, Florian-Alexander Busk, Peter Kamp Lange, Lene |
| 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. |
| doi_str_mv | 10.1038/s41598-020-66792-2 |
| format | Article |
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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
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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. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Yuhong</au><au>Łężyk, Mateusz</au><au>Herbst, Florian-Alexander</au><au>Busk, Peter Kamp</au><au>Lange, Lene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2020-06-22</date><risdate>2020</risdate><volume>10</volume><issue>1</issue><spage>10033</spage><epage>10033</epage><pages>10033-10033</pages><artnum>10033</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>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.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32572051</pmid><doi>10.1038/s41598-020-66792-2</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/114 631/1647 631/326 631/337 631/61 Animals Bacillus Bacillus - enzymology Bacillus - genetics Bacillus - metabolism Bacillus pumilus - enzymology Bacillus pumilus - genetics Bacillus pumilus - metabolism Biodegradation Bristles Chickens Cysteine Proteases - genetics Cysteine Proteases - metabolism Enzymes Feathers Feathers - metabolism Genomes Humanities and Social Sciences Keratin Keratinocytes Keratins - metabolism Metalloproteases - genetics Metalloproteases - metabolism multidisciplinary Peptidase Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Phylogeny Proteomics Science Science (multidisciplinary) Serine Proteases - genetics Serine Proteases - metabolism |
| title | Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader |
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