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Production of a sterol esterase from Ophiostoma piceae in batch and fed‐batch bioprocesses using different Pichia pastoris phenotypes as cell factory

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The potential biotechnological applications for the Ophiostoma piceae sterol esterase (OPE) are conditioned to the availability of high enzyme amounts at low prices. This enzyme is a versatile biocatalyst with different biotechnological applications. In this work a systematic study on its heterologous production in different Pichia pastoris strains and operational strategies is presented. The best results were obtained using an AOX1 defective yeast strain in a fed‐batch bioprocess using methanol as inducer substrate at a set point of 2.5 g L−1 and sorbitol as cosubstrate by means of a preprogramed exponential feeding rate at a μ = 0.02 h−1, reaching 30 U mL−1 of enzyme and a volumetric productivity of 403.5 U L−1 h−1. These values are twofold higher than those obtained with a Mut+ phenotype using methanol a sole carbon source. OPE was the main protein secreted by the yeast, 55% for Muts versus 25% for Mut+. © 2014 American Institute of Chemical Engineers Biotechnol. Prog., 30:1012–1020, 2014
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Keywords: ascomycete; esterase; lipase; recombinant protein

Document Type: Research Article

Publication date: September 1, 2014

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