ArticleMicrobial cell factories2012
Recombinant sterol esterase from Ophiostoma piceae: an improved biocatalyst expressed in Pichia pastoris.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- Living Microbial Drugs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Unraveling the regioselectivity of Ophiostoma piceae sterol esterase as a case study for lipases with wide acyl-binding tunnel entrances.The Journal of biological chemistry · 2026Article
- Article
- Fungal-Lactobacteria Consortia and Enzymatic Catalysis for Polylactic Acid Production.Journal of fungi (Basel, Switzerland) · 2023Article
- Design of an improved universal signal peptide based on the α-factor mating secretion signal for enzyme production in yeast.Cellular and molecular life sciences : CMLS · 2021Article
- Versatile Lipases from theJournal of chemical information and modeling · 2021Article
- Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase fromMolecules (Basel, Switzerland) · 2019Article
- Improvement of the Activity of a Fungal Versatile-Lipase Toward Triglycerides: AnFrontiers in bioengineering and biotechnology · 2019Article
- Article
- Identification of lipolytic enzymes isolated from bacteria indigenous toBiotechnology reports (Amsterdam, Netherlands) · 2017Article
- Directed evolution and secretory expression of a pyrethroid-hydrolyzing esterase with enhanced catalytic activity and thermostability.Microbial cell factories · 2017Article
- Potential of Ophiostoma piceae sterol esterase for biotechnologically relevant hydrolysis reactions.BioengineeredArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe ascomycete Ophiostoma piceae produces a sterol esterase (OPE) with high affinity towards p-nitrophenol, glycerol and sterol esters. Its hydrolytic activity on natural mixtures of triglycerides and sterol esters has been proposed for pitch biocontrol in paper industry since these compounds produce important economic losses during paper pulp manufacture.
resultsRecently, this enzyme has been heterologously expressed in the methylotrophic yeast Pichia pastoris, and the hydrolytic activity of the recombinant protein (OPE*) studied. After the initial screening of different clones expressing the enzyme, only one was selected for showing the highest production rate. Different culture conditions were tested to improve the expression of the recombinant enzyme. Complex media were better than minimal media for production, but in any case the levels of enzymatic activity were higher (7-fold in the best case) than those obtained from O. piceae. The purified enzyme had a molecular mass of 76 kDa, higher than that reported for the native enzyme under SDS-PAGE (60 kDa). Steady-state kinetic characterization of the recombinant protein showed improved catalytic efficiency for this enzyme as compared to the native one, for all the assayed substrates (p-nitrophenol, glycerol, and cholesterol esters). Different causes for this were studied, as the increased glycosylation degree of the recombinant enzyme, their secondary structures or the oxidation of methionine residues. However, none of these could explain the improvements found in the recombinant protein. N-terminal sequencing of OPE* showed that two populations of this enzyme were expressed, having either 6 or 8 amino acid residues more than the native one. This fact affected the aggregation behaviour of the recombinant protein, as was corroborated by analytical ultracentrifugation, thus improving the catalytic efficiency of this enzyme.
conclusionP. pastoris resulted to be an optimum biofactory for the heterologous production of recombinant sterol esterase from O. piceae, yielding higher activity levels than those obtained with the saprophytic fungus. The enzyme showed improved kinetic parameters because of its modified N-terminus, which allowed changes in its aggregation behaviour, suggesting that its hydrophobicity has been modified.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.