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Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
Umsza-Guez, Marcelo A; Díaz, Ana B; Ory, Ignacio de; Blandino, Ana; Gomes, Eleni; Caro, Ildefonso.
  • Umsza-Guez, Marcelo A; Universidade Estadual Paulista. Instituto de Biociências, Letras e Ciências Exatas. São José do Rio Preto. BR
  • Díaz, Ana B; Universidad de Cádiz. Facultad de Ciencias. Departamento de Ingeniería Química y Tecnología de Alimentos. ES
  • Ory, Ignacio de; Universidad de Cádiz. Facultad de Ciencias. Departamento de Ingeniería Química y Tecnología de Alimentos. ES
  • Blandino, Ana; Universidad de Cádiz. Facultad de Ciencias. Departamento de Ingeniería Química y Tecnología de Alimentos. ES
  • Gomes, Eleni; Universidade Estadual Paulista. Instituto de Biociências, Letras e Ciências Exatas. São José do Rio Preto. BR
  • Caro, Ildefonso; Universidad de Cádiz. Facultad de Ciencias. Departamento de Ingeniería Química y Tecnología de Alimentos. ES
Braz. j. microbiol ; 42(4): 1585-1597, Oct.-Dec. 2011. ilus, graf, tab
Artículo en Inglés | LILACS | ID: lil-614625
ABSTRACT
In this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and ¥á-amylase. The principal step of the process is the solid state fermentation (SSF) of this residue by Aspergillus awamori. In several laboratory experiments, maximum xylanase and exo-PG activities were measured during the first days of culture, reaching values around 100 and 80 IU/gds (international units of enzyme activity per gram of dried solid), respectively. For CMCase and ¥á-amylase production remained almost constant along fermentation, with average values of 19 and 21.5 IU/gds, respectively. Experiments carried out in a plate-type bioreactor at lab scale showed a clear positive effect of aeration on xylanase and CMCase, while the opposite was observed for exo-PG and ¥á-amylase. In general, xylanase was the enzyme produced in higher levels, thus the optimum conditions for the determination of the enzyme activity was characterized. The xylanase activity shows an optimum pH of 5 and an optimum temperature of 50 ¨¬C. The enzyme is activated by Mg2+, but strongly inhibited by Hg2+ and Cu2+. The enzymatic activity remains quite high if the extract is preserved in a range of pH from 3 to 10 and a temperature between 30 ¨¬C to 40 ¨¬C.
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Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Aspergillus / Xilanos / Estructuras de las Plantas / Activadores de Enzimas Idioma: Inglés Revista: Braz. j. microbiol Asunto de la revista: Microbiologia Año: 2011 Tipo del documento: Artículo País de afiliación: Brasil / España Institución/País de afiliación: Universidad de Cádiz/ES / Universidade Estadual Paulista/BR

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Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Aspergillus / Xilanos / Estructuras de las Plantas / Activadores de Enzimas Idioma: Inglés Revista: Braz. j. microbiol Asunto de la revista: Microbiologia Año: 2011 Tipo del documento: Artículo País de afiliación: Brasil / España Institución/País de afiliación: Universidad de Cádiz/ES / Universidade Estadual Paulista/BR