Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue

Detalhes bibliográficos
Autor(a) principal: Salazar,Ludmila Noskoski
Data de Publicação: 2020
Outros Autores: Astolfi,Viviane, Ogimbosvski,Tailan Antonio, Daronch,Naionara Ariete, Zeni,Jamile, Junges,Alexander, Cansian,Rogério Luis, Backes,Geciane Toniazzo
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100213
Resumo: Abstract (1) Background: The aim of this study was to evaluate the production and partial characterization of xylanase and avicelase by a newly isolated Penicillium sp. in solid-state fermentation, using soybean hulls as substrate. (2) Methods: Temperature, time, number of spores, and substrate moisture on xylanase and avicelase bioproduction were evaluated, maximizing activity with 30°C, 1x106 spores/g substrate, 14 and 7 days of fermentation with 70 and 76% substrate moisture contents, for xylanase and avicelase, respectively. (3) Results: Different solvents, temperatures, and agitation in the enzymatic extraction were evaluated, obtaining higher activities, 430.77 and 26.77 U/g for xylanase and avicelase using 30 min extraction and 0.05 M citrate buffer solution (pH 4.5 ), respectively at 60°C and 175 rpm and 50°C and 125 rpm. The optimum pH and temperature for enzymatic activity determination were 5.3 and 50°C. Enzyme extract stability was evaluated, obtaining higher stability with pH between 4.5 and 5.5, higher temperature of up to 40°C. The kinetic thermal denaturation (Kd), half-life time, D-value, and Z-value were similar for both enzymes. The xylanase Ed value (89.1 kJ/mol) was slightly lower than the avicelase one (96.7 kJ/mol), indicating higher thermostability for avicelase. (4) Conclusion: In this way, the production of cellulases using alternative substrates is a way to reduce production costs, since they represent about 10% of the world demand of enzymes, with application in animal feed processing, food production and breweries, textile processing, detergent and laundry production, pulp manufacturing and the production of biofuels.
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spelling Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull ResidueXylanaseavicelasesolid-state fermentationpartial characterizationenzymatic thermostabilityAbstract (1) Background: The aim of this study was to evaluate the production and partial characterization of xylanase and avicelase by a newly isolated Penicillium sp. in solid-state fermentation, using soybean hulls as substrate. (2) Methods: Temperature, time, number of spores, and substrate moisture on xylanase and avicelase bioproduction were evaluated, maximizing activity with 30°C, 1x106 spores/g substrate, 14 and 7 days of fermentation with 70 and 76% substrate moisture contents, for xylanase and avicelase, respectively. (3) Results: Different solvents, temperatures, and agitation in the enzymatic extraction were evaluated, obtaining higher activities, 430.77 and 26.77 U/g for xylanase and avicelase using 30 min extraction and 0.05 M citrate buffer solution (pH 4.5 ), respectively at 60°C and 175 rpm and 50°C and 125 rpm. The optimum pH and temperature for enzymatic activity determination were 5.3 and 50°C. Enzyme extract stability was evaluated, obtaining higher stability with pH between 4.5 and 5.5, higher temperature of up to 40°C. The kinetic thermal denaturation (Kd), half-life time, D-value, and Z-value were similar for both enzymes. The xylanase Ed value (89.1 kJ/mol) was slightly lower than the avicelase one (96.7 kJ/mol), indicating higher thermostability for avicelase. (4) Conclusion: In this way, the production of cellulases using alternative substrates is a way to reduce production costs, since they represent about 10% of the world demand of enzymes, with application in animal feed processing, food production and breweries, textile processing, detergent and laundry production, pulp manufacturing and the production of biofuels.Instituto de Tecnologia do Paraná - Tecpar2020-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100213Brazilian Archives of Biology and Technology v.63 2020reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/1678-4324-2020170710info:eu-repo/semantics/openAccessSalazar,Ludmila NoskoskiAstolfi,VivianeOgimbosvski,Tailan AntonioDaronch,Naionara ArieteZeni,JamileJunges,AlexanderCansian,Rogério LuisBackes,Geciane Toniazzoeng2020-08-27T00:00:00Zoai:scielo:S1516-89132020000100213Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2020-08-27T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
title Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
spellingShingle Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
Salazar,Ludmila Noskoski
Xylanase
avicelase
solid-state fermentation
partial characterization
enzymatic thermostability
title_short Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
title_full Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
title_fullStr Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
title_full_unstemmed Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
title_sort Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
author Salazar,Ludmila Noskoski
author_facet Salazar,Ludmila Noskoski
Astolfi,Viviane
Ogimbosvski,Tailan Antonio
Daronch,Naionara Ariete
Zeni,Jamile
Junges,Alexander
Cansian,Rogério Luis
Backes,Geciane Toniazzo
author_role author
author2 Astolfi,Viviane
Ogimbosvski,Tailan Antonio
Daronch,Naionara Ariete
Zeni,Jamile
Junges,Alexander
Cansian,Rogério Luis
Backes,Geciane Toniazzo
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Salazar,Ludmila Noskoski
Astolfi,Viviane
Ogimbosvski,Tailan Antonio
Daronch,Naionara Ariete
Zeni,Jamile
Junges,Alexander
Cansian,Rogério Luis
Backes,Geciane Toniazzo
dc.subject.por.fl_str_mv Xylanase
avicelase
solid-state fermentation
partial characterization
enzymatic thermostability
topic Xylanase
avicelase
solid-state fermentation
partial characterization
enzymatic thermostability
description Abstract (1) Background: The aim of this study was to evaluate the production and partial characterization of xylanase and avicelase by a newly isolated Penicillium sp. in solid-state fermentation, using soybean hulls as substrate. (2) Methods: Temperature, time, number of spores, and substrate moisture on xylanase and avicelase bioproduction were evaluated, maximizing activity with 30°C, 1x106 spores/g substrate, 14 and 7 days of fermentation with 70 and 76% substrate moisture contents, for xylanase and avicelase, respectively. (3) Results: Different solvents, temperatures, and agitation in the enzymatic extraction were evaluated, obtaining higher activities, 430.77 and 26.77 U/g for xylanase and avicelase using 30 min extraction and 0.05 M citrate buffer solution (pH 4.5 ), respectively at 60°C and 175 rpm and 50°C and 125 rpm. The optimum pH and temperature for enzymatic activity determination were 5.3 and 50°C. Enzyme extract stability was evaluated, obtaining higher stability with pH between 4.5 and 5.5, higher temperature of up to 40°C. The kinetic thermal denaturation (Kd), half-life time, D-value, and Z-value were similar for both enzymes. The xylanase Ed value (89.1 kJ/mol) was slightly lower than the avicelase one (96.7 kJ/mol), indicating higher thermostability for avicelase. (4) Conclusion: In this way, the production of cellulases using alternative substrates is a way to reduce production costs, since they represent about 10% of the world demand of enzymes, with application in animal feed processing, food production and breweries, textile processing, detergent and laundry production, pulp manufacturing and the production of biofuels.
publishDate 2020
dc.date.none.fl_str_mv 2020-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100213
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dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-4324-2020170710
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.63 2020
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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