Study of a sterol esterase secreted by Ophiostoma piceae: Sequence, model and biochemical properties

Calero-Rueda, Olga; Barba, Víctor; Rodríguez, Enrique; Plou, Francisco J.; Martı́nez, Ángel T.; Martı́nez, Marı́a Jesús

doi:10.1016/j.bbapap.2009.02.012

Cited by 21 publications

(27 citation statements)

References 43 publications

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“…The 820-bp sequence from tup1 and the 363-bp sequence from cyr1 lacked introns. The absence of introns has in the gene for the O. piceae sterol esterase also been reported (32). The sequences obtained had nucleotide identities of 76% for tup1 and 87% for cyr1 with the genes from the Canadian strain of O. piceae (29).…”

Section: Resultsmentioning

confidence: 74%

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Quorum-Sensing Mechanisms Mediated by Farnesol in Ophiostoma piceae: Effect on Secretion of Sterol Esterase

Salas

Martı́nez

Barriuso

2015

Appl Environ Microbiol

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Ophiostoma piceae CECT 20416 is a dimorphic wood-staining fungus able to produce an extracellular sterol-esterase/lipase (OPE) that is of great biotechnological interest. In this work, we have studied the morphological change of this fungus from yeast to hyphae, which is associated with the cell density-related mechanism known as quorum sensing (QS), and how this affects the secretion of OPE. The data presented here confirm that the molecule E,E-farnesol accumulates as the cell number is growing within the population. The exogenous addition of this molecule or spent medium to the cultures increased the extracellular activity of OPE 2.5 times. This fact was related not to an increase in microbial biomass or in the expression of the gene coding for OPE but to a marked morphological transition in the cultures. Moreover, the morphological transition also occurred when a high cell density was inoculated into the medium. The results suggest that E,E-farnesol regulates through QS mechanisms the morphological transition in the dimorphic fungus O. piceae and that it is associated with a higher extracellular esterase activity. Furthermore, identification and transcriptional analysis of genes tup1 and cyr1, which are involved in the response, was carried out. Here we report enhanced production of a sterol-esterase/lipase of biotechnological interest by means of QS mechanisms. These results may be useful in increasing the production of secreted enzymes of other dimorphic fungi of biotechnological interest.T riacylglycerol esterases, also known as lipases, have acylglycerols as their natural substrates, while sterol esterases hydrolyze fatty acid esters of sterols. In addition, both kinds of enzymes are able to carry out synthesis reactions in the presence of organic solvents (1, 2). They are widespread in nature, but those from microorganisms, especially fungi, have gained special interest due to their broad substrate specificity and their potential application for biotechnological applications (2).Ophiostoma piceae is a wood-staining fungus and is a causal agent of pine and spruce discoloration. Although it is not a pathogenic species and associates with nonaggressive bark beetles, the infection results in substantial economic losses in the forestry industry (3). Its ability to produce a morphological transition from yeast to hyphal forms, depending on fungal culture conditions, probably contributes to its adaptation to different environmental conditions (3). The effect of inoculum size on culture morphology of fungi from the genera Ophiostoma has been recently reported, suggesting that yeast-or hypha-like growth could be associated with quorum-sensing (QS) activity (4).The fungus O. piceae CECT 20416 produces an extracellular sterol esterase (OPE) with activity on triglycerides, esters of p-nitrophenol, and cholesterol (5). This is the only esterase secreted by this strain, and it represents a major protein in the crude enzyme obtained using a basal medium supplemented with olive oil. The enzyme is a glycosylated protein,...

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Section: Resultsmentioning

confidence: 74%

“…The ascomycete O. piceae causes important losses in the wood sector (3) but also secretes a sterol-esterase/lipase of high biotechnological interest (1,32). In this work, the effects of several putative QS molecules on fungal growth and morphology, extracellular protein production, and, particularly, sterol esterase secretion were studied.…”

Section: Resultsmentioning

confidence: 99%

Quorum-Sensing Mechanisms Mediated by Farnesol in Ophiostoma piceae: Effect on Secretion of Sterol Esterase

Salas

Martı́nez

Barriuso

2015

Appl Environ Microbiol

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“…Fungal sterol esterases from Melanocarpus albomyces (Kontkanen et al 2006a, c) and Ophiostoma piceae (Calero-Rueda et al 2002) have recently been characterized from the biochemical and molecular points of view. The ability to hydrolyze sterol esters is considered to be a particular characteristic of this group of enzymes, together with the lack of the above-mentioned mobile lid in their molecular structure, as found in typical lipases (Calero-Rueda et al 2009). These fungal esterases were tested for treating a model pitch preparation simulating the TMP (Kontkanen et al 2006c) and eucalypt pulp resin (Calero-Rueda et al 2004).…”

Section: A Hydrolytic Enzymesmentioning

confidence: 99%

“…Fungal sterol esterases can be produced by heterologous expression in industrial hosts and the recombinant enzymes have been characterized (Calero-Rueda et al 2009;Kontkanen et al 2006a) and immobilized to increase their enzyme stability (Torres et al 2008). The effects of a recombinant sterol esterase from M. albomyces on the extractives of TMP water (Table 17.3) as well as on the properties of derived paper sheets were evaluated and compared with Resinase A2X (Kontkanen et al 2006b).…”

Section: A Hydrolytic Enzymesmentioning

confidence: 99%

Fungi and Their Enzymes for Pitch Control in the Pulp and Paper Industry

Gutiérrez

Rı́o

Martı́nez

2010

Industrial Applications

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“…These enzymes are commonly categorized according to their corresponding substrates and are known as carboxylesterase, sulfatase, and phosphatase (Tirawongsaroj et al 2008;Calero-Rueda et al 2009;Chimtong et al 2014). There are many reports on esterases that discuss distribution, quantitation, targeted synthesis, production, purification, and molecular biology.…”

Section: Introductionmentioning

confidence: 99%

Accurately Determining Esterase Activity via the Isosbestic Point of p-Nitrophenol

Peng¹,

Fu²,

Líu³

et al. 2016

BioResources

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Esterase is an important enzyme for ester hydrolysis or synthesis. Its activity, however, has not been accurately ascertained due to a lack of accurate protocols. In this study, the isosbestic point of p-nitrophenol was found and used as the marker for its activity. The methodology avoided decomposition of the substrate, chromophore agents, and pH changes. The esterase activity was determined accurately and rapidly in a complex solution. In this protocol system, organic solvents were used for dissolving substrates, which influenced activity determination to some extent. Among the solvents tested, methanol exerted the least inhibitory influence. The results indicated that this modified method has potential to be applied for esterase activity determination on a large scale and in real time.

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Study of a sterol esterase secreted by Ophiostoma piceae: Sequence, model and biochemical properties

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Cited by 21 publications

References 43 publications

Quorum-Sensing Mechanisms Mediated by Farnesol in Ophiostoma piceae: Effect on Secretion of Sterol Esterase

Quorum-Sensing Mechanisms Mediated by Farnesol in Ophiostoma piceae: Effect on Secretion of Sterol Esterase

Fungi and Their Enzymes for Pitch Control in the Pulp and Paper Industry

Accurately Determining Esterase Activity via the Isosbestic Point of p-Nitrophenol

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