Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation

An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50–55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturoni...

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Autores principales: Gomes, Eleni, Leite, Rodrigo Simões Ribeiro, da Silva, Roberto, Silva, Dênis
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2009
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2817892/
https://www.ncbi.nlm.nih.gov/pubmed/20148174
http://dx.doi.org/10.1155/2009/631942
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author Gomes, Eleni
Leite, Rodrigo Simões Ribeiro
da Silva, Roberto
Silva, Dênis
author_facet Gomes, Eleni
Leite, Rodrigo Simões Ribeiro
da Silva, Roberto
Silva, Dênis
author_sort Gomes, Eleni
collection PubMed
description An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50–55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). Ions Ca(2+) enhanced the stability of enzyme and its activity by 30%. The K (m) was 1.30 in absence of Ca(2+) and 1.16 mg mL(−1) in presence of this ion. In relation to the V (max) the presence of this ion increased from 1.76 to 2.07 μmol min(−1)mg(−1).
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spelling pubmed-28178922010-02-10 Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation Gomes, Eleni Leite, Rodrigo Simões Ribeiro da Silva, Roberto Silva, Dênis Int J Microbiol Research Article An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50–55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). Ions Ca(2+) enhanced the stability of enzyme and its activity by 30%. The K (m) was 1.30 in absence of Ca(2+) and 1.16 mg mL(−1) in presence of this ion. In relation to the V (max) the presence of this ion increased from 1.76 to 2.07 μmol min(−1)mg(−1). Hindawi Publishing Corporation 2009 2010-02-03 /pmc/articles/PMC2817892/ /pubmed/20148174 http://dx.doi.org/10.1155/2009/631942 Text en Copyright © 2009 Eleni Gomes et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Gomes, Eleni
Leite, Rodrigo Simões Ribeiro
da Silva, Roberto
Silva, Dênis
Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
title Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
title_full Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
title_fullStr Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
title_full_unstemmed Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
title_short Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
title_sort purification of an exopolygalacturonase from penicillium viridicatum rfc3 produced in submerged fermentation
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2817892/
https://www.ncbi.nlm.nih.gov/pubmed/20148174
http://dx.doi.org/10.1155/2009/631942
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