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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.
  • 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 ; 63: e20170710, 2020. tab, graf
Article in English | LILACS | ID: biblio-1132254
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.
Subject(s)


Full text: Available Index: LILACS (Americas) Main subject: Penicillium / Soybeans / Xylosidases / Cellulases Language: English Journal: Braz. arch. biol. technol Journal subject: Biology Year: 2020 Type: Article Affiliation country: Brazil Institution/Affiliation country: Regional Integrated University of Alto Uruguay and the Missions/BR

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Full text: Available Index: LILACS (Americas) Main subject: Penicillium / Soybeans / Xylosidases / Cellulases Language: English Journal: Braz. arch. biol. technol Journal subject: Biology Year: 2020 Type: Article Affiliation country: Brazil Institution/Affiliation country: Regional Integrated University of Alto Uruguay and the Missions/BR