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Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions

The ascomycete Ophiostoma piceae produces a sterol esterase (OPE) with high affinity toward p-nitrophenol, glycerol, and sterol esters. Recently, this enzyme has been heterologously expressed in the methylotrophic yeast Pichia pastoris under the AOX1 methanol-inducible promoter (P(AOX1)) using sorbi...

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Autores principales: Barba Cedillo, Víctor, Prieto, Alicia, Martínez, María Jesús
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728196/
https://www.ncbi.nlm.nih.gov/pubmed/23138020
http://dx.doi.org/10.4161/bioe.22818
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author Barba Cedillo, Víctor
Prieto, Alicia
Martínez, María Jesús
author_facet Barba Cedillo, Víctor
Prieto, Alicia
Martínez, María Jesús
author_sort Barba Cedillo, Víctor
collection PubMed
description The ascomycete Ophiostoma piceae produces a sterol esterase (OPE) with high affinity toward p-nitrophenol, glycerol, and sterol esters. Recently, this enzyme has been heterologously expressed in the methylotrophic yeast Pichia pastoris under the AOX1 methanol-inducible promoter (P(AOX1)) using sorbitol as co-susbtrate, and the hydrolytic activity of the recombinant protein (OPE*) turned out to be improved from a kinetic point of view. In this study, we analyze the effects of sorbitol during the expression of OPE*, at first added as an additional carbon source, and methanol as inducer. The O. piceae enzyme was successfully used for PVAc hydrolysis, suggesting its potential applicability in recycled paper production to decrease stickies problems.
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spelling pubmed-37281962013-08-02 Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions Barba Cedillo, Víctor Prieto, Alicia Martínez, María Jesús Bioengineered Addendum The ascomycete Ophiostoma piceae produces a sterol esterase (OPE) with high affinity toward p-nitrophenol, glycerol, and sterol esters. Recently, this enzyme has been heterologously expressed in the methylotrophic yeast Pichia pastoris under the AOX1 methanol-inducible promoter (P(AOX1)) using sorbitol as co-susbtrate, and the hydrolytic activity of the recombinant protein (OPE*) turned out to be improved from a kinetic point of view. In this study, we analyze the effects of sorbitol during the expression of OPE*, at first added as an additional carbon source, and methanol as inducer. The O. piceae enzyme was successfully used for PVAc hydrolysis, suggesting its potential applicability in recycled paper production to decrease stickies problems. Landes Bioscience 2013-07-01 2012-11-08 /pmc/articles/PMC3728196/ /pubmed/23138020 http://dx.doi.org/10.4161/bioe.22818 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Addendum
Barba Cedillo, Víctor
Prieto, Alicia
Martínez, María Jesús
Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
title Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
title_full Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
title_fullStr Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
title_full_unstemmed Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
title_short Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
title_sort potential of ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions
topic Addendum
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728196/
https://www.ncbi.nlm.nih.gov/pubmed/23138020
http://dx.doi.org/10.4161/bioe.22818
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