Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost

Detalhes bibliográficos
Autor(a) principal: Marco, Evilin Giordana de
Data de Publicação: 2017
Outros Autores: Silva, Karina Heck da, Martos, Emerson Tokuda, Van der Sand, Sueli Terezinha
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFRGS
Texto Completo: http://hdl.handle.net/10183/188805
Resumo: During composting processes, the degradation of organic waste is accomplished and driven by a succession of microbial populations exhibiting a broad range of functional competencies. A total of 183 bacteria, isolated from a composting process, were evaluated for cellulase activity at different temperatures (37, 50, 60, and 70°C) and pH values. Out of the 22 isolates that showed activity, isolate 380 showed the highest cellulase activity. Its ability to produce cellulase was evaluated in culture medium supplemented with carboxymethyl cellulose, microcrystalline cellulose, wheat straw, and rice husk. The culture medium supplemented with carboxymethyl cellulose induced higher enzyme activity after 6 hours of incubation (0.12 UEA mL-1 min-1). For wheat straw and rice husk, the results were 0.08 UEA mL-1 min-1 for both, while for microcrystalline cellulose, 0.04 UEA mL-1 min-1 were observed. The highest carboxymethyl cellulase activity was observed at 60°C (0.14 UEA mL-1 min-1) for both crude and partially purified enzyme after 30 and 120 min of incubation, respectively. Alkalinization of the medium was observed during cultivation in all substrates. The cellulase had a molecular mass of 20 kDa determined by SDS-Page. Isolate 380 was identified as Bacillus licheniformis. This work provides a basis for further studies on composting optimization.
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spelling Marco, Evilin Giordana deSilva, Karina Heck daMartos, Emerson TokudaVan der Sand, Sueli Terezinha2019-02-15T02:33:34Z20170001-3765http://hdl.handle.net/10183/188805001086972During composting processes, the degradation of organic waste is accomplished and driven by a succession of microbial populations exhibiting a broad range of functional competencies. A total of 183 bacteria, isolated from a composting process, were evaluated for cellulase activity at different temperatures (37, 50, 60, and 70°C) and pH values. Out of the 22 isolates that showed activity, isolate 380 showed the highest cellulase activity. Its ability to produce cellulase was evaluated in culture medium supplemented with carboxymethyl cellulose, microcrystalline cellulose, wheat straw, and rice husk. The culture medium supplemented with carboxymethyl cellulose induced higher enzyme activity after 6 hours of incubation (0.12 UEA mL-1 min-1). For wheat straw and rice husk, the results were 0.08 UEA mL-1 min-1 for both, while for microcrystalline cellulose, 0.04 UEA mL-1 min-1 were observed. The highest carboxymethyl cellulase activity was observed at 60°C (0.14 UEA mL-1 min-1) for both crude and partially purified enzyme after 30 and 120 min of incubation, respectively. Alkalinization of the medium was observed during cultivation in all substrates. The cellulase had a molecular mass of 20 kDa determined by SDS-Page. Isolate 380 was identified as Bacillus licheniformis. This work provides a basis for further studies on composting optimization.application/pdfengAnais da Academia Brasileira de Ciências. Rio de Janeiro, RJ. Vol. 89, no. 3 supl (2017), p. 2359-2370Carboximetilcelulose sódicaCeluloseEnzimasBactériasBacillus liqueniformisAlkalophilic enzymeCarboxymethyl celullaseCompostHigh temperaturePurification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compostEstrangeiroinfo: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:UFRGSTEXT001086972.pdf.txt001086972.pdf.txtExtracted Texttext/plain40661http://www.lume.ufrgs.br/bitstream/10183/188805/2/001086972.pdf.txt9524bffdbfcb6fcc682892abae406a2dMD52ORIGINAL001086972.pdfTexto completo (inglês)application/pdf632204http://www.lume.ufrgs.br/bitstream/10183/188805/1/001086972.pdfe8f7976244d8fc85ee26d9482fd796dbMD5110183/1888052019-02-16 02:34:25.355452oai:www.lume.ufrgs.br:10183/188805Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2019-02-16T04:34:25Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false
dc.title.pt_BR.fl_str_mv Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
title Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
spellingShingle Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
Marco, Evilin Giordana de
Carboximetilcelulose sódica
Celulose
Enzimas
Bactérias
Bacillus liqueniformis
Alkalophilic enzyme
Carboxymethyl celullase
Compost
High temperature
title_short Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
title_full Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
title_fullStr Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
title_full_unstemmed Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
title_sort Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
author Marco, Evilin Giordana de
author_facet Marco, Evilin Giordana de
Silva, Karina Heck da
Martos, Emerson Tokuda
Van der Sand, Sueli Terezinha
author_role author
author2 Silva, Karina Heck da
Martos, Emerson Tokuda
Van der Sand, Sueli Terezinha
author2_role author
author
author
dc.contributor.author.fl_str_mv Marco, Evilin Giordana de
Silva, Karina Heck da
Martos, Emerson Tokuda
Van der Sand, Sueli Terezinha
dc.subject.por.fl_str_mv Carboximetilcelulose sódica
Celulose
Enzimas
Bactérias
Bacillus liqueniformis
topic Carboximetilcelulose sódica
Celulose
Enzimas
Bactérias
Bacillus liqueniformis
Alkalophilic enzyme
Carboxymethyl celullase
Compost
High temperature
dc.subject.eng.fl_str_mv Alkalophilic enzyme
Carboxymethyl celullase
Compost
High temperature
description During composting processes, the degradation of organic waste is accomplished and driven by a succession of microbial populations exhibiting a broad range of functional competencies. A total of 183 bacteria, isolated from a composting process, were evaluated for cellulase activity at different temperatures (37, 50, 60, and 70°C) and pH values. Out of the 22 isolates that showed activity, isolate 380 showed the highest cellulase activity. Its ability to produce cellulase was evaluated in culture medium supplemented with carboxymethyl cellulose, microcrystalline cellulose, wheat straw, and rice husk. The culture medium supplemented with carboxymethyl cellulose induced higher enzyme activity after 6 hours of incubation (0.12 UEA mL-1 min-1). For wheat straw and rice husk, the results were 0.08 UEA mL-1 min-1 for both, while for microcrystalline cellulose, 0.04 UEA mL-1 min-1 were observed. The highest carboxymethyl cellulase activity was observed at 60°C (0.14 UEA mL-1 min-1) for both crude and partially purified enzyme after 30 and 120 min of incubation, respectively. Alkalinization of the medium was observed during cultivation in all substrates. The cellulase had a molecular mass of 20 kDa determined by SDS-Page. Isolate 380 was identified as Bacillus licheniformis. This work provides a basis for further studies on composting optimization.
publishDate 2017
dc.date.issued.fl_str_mv 2017
dc.date.accessioned.fl_str_mv 2019-02-15T02:33:34Z
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dc.relation.ispartof.pt_BR.fl_str_mv Anais da Academia Brasileira de Ciências. Rio de Janeiro, RJ. Vol. 89, no. 3 supl (2017), p. 2359-2370
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