Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

The filamentous fungus A. phoenicis produced high levels of ?-D-fructofuranosidase (FFase) when grown for 72 hrs under Solid-State Fermentation (SSF), using soy bran moistened with tap water (1:0.5 w/v) as substrate/carbon source. Two isoforms (I and II) were obtained, and FFase II was purified 18-f...

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Autores principales: Rustiguel,Cynthia Barbosa, Oliveira,Arthur Henrique Cavalcanti de, Terenzi,Héctor Francisco, Jorge,João Atílio, Guimarães,Luis Henrique Souza
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2011
Materias:
agroindustrial substrate
Aspergillus
?-D-fructofuranosidase
solid state fermentation
sucrose
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000200002
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spelling oai:scielo:S0717-345820110002000022011-05-26Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrateRustiguel,Cynthia BarbosaOliveira,Arthur Henrique Cavalcanti deTerenzi,Héctor FranciscoJorge,João AtílioGuimarães,Luis Henrique Souza agroindustrial substrate Aspergillus ?-D-fructofuranosidase solid state fermentation sucrose The filamentous fungus A. phoenicis produced high levels of ?-D-fructofuranosidase (FFase) when grown for 72 hrs under Solid-State Fermentation (SSF), using soy bran moistened with tap water (1:0.5 w/v) as substrate/carbon source. Two isoforms (I and II) were obtained, and FFase II was purified 18-fold to apparent homogeneity with 14% recovery. The native molecular mass of the glycoprotein (12% of carbohydrate content) was 158.5 kDa with two subunits of 85 kDa estimated by SDS-PAGE. Optima of temperature and pH were 55�C and 4.5. The enzyme was stable for more than 1 hr at 50�C and was also stable in a pH range from 7.0 to 8.0. FFase II retained 80% of activity after storage at 4�C by 200 hrs. Dichroism analysis showed the presence of random and ?-sheet structure. A. phoenicis FFase II was activated by Mn2+, Mg2+ and Co2+, and inhibited by Cu2+, Hg2+ and EDTA. The enzyme hydrolyzed sucrose, inulin and raffinose. Kd and Vmax values were 18 mM and 189 U/mg protein using sucrose as substrate.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.14 n.2 20112011-03-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000200002en
institution Scielo Chile
collection Scielo Chile
language English
topic agroindustrial substrate
Aspergillus
?-D-fructofuranosidase
solid state fermentation
sucrose
spellingShingle agroindustrial substrate
Aspergillus
?-D-fructofuranosidase
solid state fermentation
sucrose
Rustiguel,Cynthia Barbosa
Oliveira,Arthur Henrique Cavalcanti de
Terenzi,Héctor Francisco
Jorge,João Atílio
Guimarães,Luis Henrique Souza
Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
description The filamentous fungus A. phoenicis produced high levels of ?-D-fructofuranosidase (FFase) when grown for 72 hrs under Solid-State Fermentation (SSF), using soy bran moistened with tap water (1:0.5 w/v) as substrate/carbon source. Two isoforms (I and II) were obtained, and FFase II was purified 18-fold to apparent homogeneity with 14% recovery. The native molecular mass of the glycoprotein (12% of carbohydrate content) was 158.5 kDa with two subunits of 85 kDa estimated by SDS-PAGE. Optima of temperature and pH were 55�C and 4.5. The enzyme was stable for more than 1 hr at 50�C and was also stable in a pH range from 7.0 to 8.0. FFase II retained 80% of activity after storage at 4�C by 200 hrs. Dichroism analysis showed the presence of random and ?-sheet structure. A. phoenicis FFase II was activated by Mn2+, Mg2+ and Co2+, and inhibited by Cu2+, Hg2+ and EDTA. The enzyme hydrolyzed sucrose, inulin and raffinose. Kd and Vmax values were 18 mM and 189 U/mg protein using sucrose as substrate.
author Rustiguel,Cynthia Barbosa
Oliveira,Arthur Henrique Cavalcanti de
Terenzi,Héctor Francisco
Jorge,João Atílio
Guimarães,Luis Henrique Souza
author_facet Rustiguel,Cynthia Barbosa
Oliveira,Arthur Henrique Cavalcanti de
Terenzi,Héctor Francisco
Jorge,João Atílio
Guimarães,Luis Henrique Souza
author_sort Rustiguel,Cynthia Barbosa
title Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
title_short Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
title_full Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
title_fullStr Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
title_full_unstemmed Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
title_sort biochemical properties of an extracellular β-d-fructofuranosidase ii produced by aspergillus phoenicis under solid-sate fermentation using soy bran as substrate
publisher Pontificia Universidad Católica de Valparaíso
publishDate 2011
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000200002
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