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Agroindustrial biomass for xylanase production by Penicillium chrysogenum: purification, biochemical properties and hydrolysis of hemicelluloses
Cabral Terrone, Cárol; Freitas, Caroline de; Fanchini Terrasan, César Rafael; Almeida, Alex Fernando de; Cano Carmona, Eleonora.
  • Cabral Terrone, Cárol; Universidade Estadual Paulista Júlio de Mesquita Filho. Instituto de Biociências. Rio Claro. BR
  • Freitas, Caroline de; Universidade Estadual Paulista Júlio de Mesquita Filho. Instituto de Biociências. Rio Claro. BR
  • Fanchini Terrasan, César Rafael; Universidade Estadual Paulista Júlio de Mesquita Filho. Instituto de Biociências. Rio Claro. BR
  • Almeida, Alex Fernando de; Universidade Federal do Tocantins - UFT. Departamento de Engenharia de Bioprocessos e Biotecnologia. Gurupi. BR
  • Cano Carmona, Eleonora; Universidade Estadual Paulista Júlio de Mesquita Filho. Instituto de Biociências. Rio Claro. BR
Electron. j. biotechnol ; 33: 39-45, May. 2018. tab, graf, ilus
Article in English | LILACS | ID: biblio-1022849
ABSTRACT

Background:

In this work, the xylanase production by Penicillium chrysogenum F-15 strain was investigated using agroindustrial biomass as substrate. The xylanase was purified, characterized and applied in hemicellulose hydrolysis.

Results:

The highest xylanase production was obtained when cultivation was carried out with sugar cane bagasse as carbon source, at pH 6.0 and 20°C, under static condition for 8 d. The enzyme was purified by a sequence of ion exchange and size exclusion chromatography, presenting final specific activity of 834.2 U·mg·prot-1. T he molecular mass of the purified enzyme estimated by SDS-PAGE was 22.1 kDa. The optimum activity was at pH 6.5 and 45°C. The enzyme was stable at 40°C with half-life of 35 min, and in the pH range from 4.5 to 10.0. The activity was increased in the presence of Mg+2 and Mn+2 and reducing agents such as DTT and ßmercaptoethanol, but it was reduced by Cu+2 and Pb+2 . The xylanase presented Km of 2.3 mM and Vmax of 731.8 U·mg·prot-1 with birchwood xylan as substrate. This xylanase presented differences in its properties when it was compared to the xylanases from other P. chrysogenum strains.

Conclusion:

The xylanase from P. chrysogenum F-15 showed lower enzymatic activity on commercial xylan than on hemicellulose from agroindustry biomass and its biochemistry characteristics, such as stability at 40°C and pH from 4.0 to 10.0, shows the potential of this enzyme for application in food, feed, pulp and paper industries and for bioethanol production.
Subject(s)


Full text: Available Index: LILACS (Americas) Main subject: Penicillium chrysogenum / Polysaccharides / Endo-1,4-beta Xylanases Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2018 Type: Article Affiliation country: Brazil Institution/Affiliation country: Universidade Estadual Paulista Júlio de Mesquita Filho/BR / Universidade Federal do Tocantins - UFT/BR

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Full text: Available Index: LILACS (Americas) Main subject: Penicillium chrysogenum / Polysaccharides / Endo-1,4-beta Xylanases Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2018 Type: Article Affiliation country: Brazil Institution/Affiliation country: Universidade Estadual Paulista Júlio de Mesquita Filho/BR / Universidade Federal do Tocantins - UFT/BR