Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/217142 |
Resumo: | Marine actinobacteria are viewed as a promising source of enzymes with potential technological applications. They contribute to the turnover of complex biopolymers, such as pectin, lignocellulose, chitin, and keratin, being able to secrete a wide variety of extracellular enzymes. Among these, keratinases are a valuable alternative for recycling keratin-rich waste, which is generated in large quantities by the poultry industry. In this work, we explored the biocatalytic potential of 75 marine-derived actinobacterial strains, focusing mainly on the search for keratinases. A major part of the strains secreted industrially important enzymes, such as proteases, lipases, cellulases, amylases, and keratinases. Among these, we identified two streptomycete strains that presented great potential for recycling keratin wastes—Streptomyces sp. CHA1 and Streptomyces sp. G11C. Substrate concentration, incubation temperature, and, to a lesser extent, inoculum size were found to be important parameters that influenced the production of keratinolytic enzymes in both strains. In addition, proteomic analysis of culture broths from Streptomyces sp. G11C on turkey feathers showed a high abundance and diversity of peptidases, belonging mainly to the serine and metallo-superfamilies. Two proteases from families S08 and M06 were highly expressed. These results contributed to elucidate the mechanism of keratin degradation mediated by streptomycetes. |
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González, ValentinaVargas Straube, María JoséSilva, Walter Orlando Beys daSanti, LucéliaValencia, PedroBeltrametti, FabrizioCámara, Beatriz2021-01-08T04:06:13Z20201660-3397http://hdl.handle.net/10183/217142001120556Marine actinobacteria are viewed as a promising source of enzymes with potential technological applications. They contribute to the turnover of complex biopolymers, such as pectin, lignocellulose, chitin, and keratin, being able to secrete a wide variety of extracellular enzymes. Among these, keratinases are a valuable alternative for recycling keratin-rich waste, which is generated in large quantities by the poultry industry. In this work, we explored the biocatalytic potential of 75 marine-derived actinobacterial strains, focusing mainly on the search for keratinases. A major part of the strains secreted industrially important enzymes, such as proteases, lipases, cellulases, amylases, and keratinases. Among these, we identified two streptomycete strains that presented great potential for recycling keratin wastes—Streptomyces sp. CHA1 and Streptomyces sp. G11C. Substrate concentration, incubation temperature, and, to a lesser extent, inoculum size were found to be important parameters that influenced the production of keratinolytic enzymes in both strains. In addition, proteomic analysis of culture broths from Streptomyces sp. G11C on turkey feathers showed a high abundance and diversity of peptidases, belonging mainly to the serine and metallo-superfamilies. Two proteases from families S08 and M06 were highly expressed. These results contributed to elucidate the mechanism of keratin degradation mediated by streptomycetes.application/pdfengMarine drugs. Basel. Vol. 18, no. 11 (2020), 537, 26 p.FarmáciaActinobacteriaStreptomycesQueratinasMarine actinobacteriaStreptomycesRare actinobacteriaHydrolytic enzymesKeratinolytic proteasesSecretomeEnzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11CEstrangeiroinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001120556.pdf.txt001120556.pdf.txtExtracted Texttext/plain93541http://www.lume.ufrgs.br/bitstream/10183/217142/2/001120556.pdf.txta642981bbb9dcaeb15f511bdbb106dedMD52ORIGINAL001120556.pdfTexto completo (inglês)application/pdf38958717http://www.lume.ufrgs.br/bitstream/10183/217142/1/001120556.pdf06a61dfa8e55c311caa52173f2a71cc8MD5110183/2171422021-03-09 04:39:57.630685oai:www.lume.ufrgs.br:10183/217142Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2021-03-09T07:39:57Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
title |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
spellingShingle |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C González, Valentina Farmácia Actinobacteria Streptomyces Queratinas Marine actinobacteria Streptomyces Rare actinobacteria Hydrolytic enzymes Keratinolytic proteases Secretome |
title_short |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
title_full |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
title_fullStr |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
title_full_unstemmed |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
title_sort |
Enzyme bioprospection of marine-derived actinobacteria from the Chilean Coast and New Insight in the aechanism of keratin degradation in Streptomyces sp. G11C |
author |
González, Valentina |
author_facet |
González, Valentina Vargas Straube, María José Silva, Walter Orlando Beys da Santi, Lucélia Valencia, Pedro Beltrametti, Fabrizio Cámara, Beatriz |
author_role |
author |
author2 |
Vargas Straube, María José Silva, Walter Orlando Beys da Santi, Lucélia Valencia, Pedro Beltrametti, Fabrizio Cámara, Beatriz |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
González, Valentina Vargas Straube, María José Silva, Walter Orlando Beys da Santi, Lucélia Valencia, Pedro Beltrametti, Fabrizio Cámara, Beatriz |
dc.subject.por.fl_str_mv |
Farmácia Actinobacteria Streptomyces Queratinas |
topic |
Farmácia Actinobacteria Streptomyces Queratinas Marine actinobacteria Streptomyces Rare actinobacteria Hydrolytic enzymes Keratinolytic proteases Secretome |
dc.subject.eng.fl_str_mv |
Marine actinobacteria Streptomyces Rare actinobacteria Hydrolytic enzymes Keratinolytic proteases Secretome |
description |
Marine actinobacteria are viewed as a promising source of enzymes with potential technological applications. They contribute to the turnover of complex biopolymers, such as pectin, lignocellulose, chitin, and keratin, being able to secrete a wide variety of extracellular enzymes. Among these, keratinases are a valuable alternative for recycling keratin-rich waste, which is generated in large quantities by the poultry industry. In this work, we explored the biocatalytic potential of 75 marine-derived actinobacterial strains, focusing mainly on the search for keratinases. A major part of the strains secreted industrially important enzymes, such as proteases, lipases, cellulases, amylases, and keratinases. Among these, we identified two streptomycete strains that presented great potential for recycling keratin wastes—Streptomyces sp. CHA1 and Streptomyces sp. G11C. Substrate concentration, incubation temperature, and, to a lesser extent, inoculum size were found to be important parameters that influenced the production of keratinolytic enzymes in both strains. In addition, proteomic analysis of culture broths from Streptomyces sp. G11C on turkey feathers showed a high abundance and diversity of peptidases, belonging mainly to the serine and metallo-superfamilies. Two proteases from families S08 and M06 were highly expressed. These results contributed to elucidate the mechanism of keratin degradation mediated by streptomycetes. |
publishDate |
2020 |
dc.date.issued.fl_str_mv |
2020 |
dc.date.accessioned.fl_str_mv |
2021-01-08T04:06:13Z |
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http://hdl.handle.net/10183/217142 |
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1660-3397 |
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001120556 |
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1660-3397 001120556 |
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http://hdl.handle.net/10183/217142 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Marine drugs. Basel. Vol. 18, no. 11 (2020), 537, 26 p. |
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info:eu-repo/semantics/openAccess |
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openAccess |
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