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Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue
Salazar, Ludmila Noskoski; Astolfi, Viviane; Ogimbosvski, Tailan Antonio; Daronch, Naionara Ariete; Zeni, Jamile; Junges, Alexander; Cansian, Rogério Luis; Backes, Geciane Toniazzo.
Afiliação
  • Salazar, Ludmila Noskoski; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Astolfi, Viviane; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Ogimbosvski, Tailan Antonio; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Daronch, Naionara Ariete; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Zeni, Jamile; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Junges, Alexander; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Cansian, Rogério Luis; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
  • Backes, Geciane Toniazzo; Regional Integrated University of Alto Uruguay and the Missions. Department of Food Engineering. Erechim. BR
Braz. arch. biol. technol ; Braz. arch. biol. technol;63: e20170710, 2020. tab, graf
Article em En | LILACS | ID: biblio-1132254
Biblioteca responsável: BR1.1
ABSTRACT
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.
Assuntos
Palavras-chave

Texto completo: 1 Índice: LILACS Assunto principal: Penicillium / Glycine max / Xilosidases / Celulases Idioma: En Revista: Braz. arch. biol. technol Assunto da revista: BIOLOGIA Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Índice: LILACS Assunto principal: Penicillium / Glycine max / Xilosidases / Celulases Idioma: En Revista: Braz. arch. biol. technol Assunto da revista: BIOLOGIA Ano de publicação: 2020 Tipo de documento: Article