Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , |
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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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 |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100213 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100213 |
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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1750318279645200384 |