purification and characterization of extracellular lipases from ophiostoma piliferum

Brush, T. S.; Chapman, Robert N.; Kurzman, Ricky; Williams, Daniel W.

doi:10.1016/s0968-0896(99)00142-x

Cited by 21 publications

(8 citation statements)

References 22 publications

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“…A different extracellular esterase with lowest M r (around 35 kDa) and different N-terminal sequence has been isolated from O. piceae and described as a lipase (Gao and Breuil, 1995). The enzyme studied in the present work shows similar M r and N-terminal sequence to that reported in Ophiostoma piliferum (Brush et al, 1999), although they showed different catalytic properties (as discussed below).…”

Section: Production and Characterisation Of O Piceae Sterol Esterasesupporting

confidence: 55%

“…The hydrolysis efficiency increased in parallel with the length of the fatty acid esterifying glycerol, and the presence of double bonds in the acyl chain affect k cat more than K m Brush et al, 1999). A low activity on cholesterol esters has been also reported for the other esterase isolated from O. piceae (Gao and Breuil, 1998).…”

Section: Production and Characterisation Of O Piceae Sterol Esterasementioning

confidence: 74%

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Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application to pitch control in pulping of Eucalyptus globulus wood

Calero-Rueda¹,

Gutiérrez²,

Rı́o³

et al. 2004

IJBT

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A sterol esterase purified from cultures of the sapstain fungus Ophiostoma piceae was able to hydrolyse sterol esters and glycerides. The kinetics of sterol esters and triglyceride hydrolysis by this new esterase, estimated using a pH-stat, showed a K m app and a k cat app in the range of 0.9-1.1 mM and 70-300 s -1 , respectively. Its ability to hydrolyse both pure sterol esters and natural mixtures of saponifiable lipids from eucalypt wood was compared with those of commercial sterol esterases from other microbial sources. Its specific activity on sterol esters was higher than that found with all the commercial esterases assayed, and the highest hydrolysis of eucalypt sterol esters was also attained using the O. piceae esterase. This sterol esterase could be of biotechnological interest for the hydrolysis of sterol esters that form pitch deposits in paper pulp manufacturing.

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Section: Production and Characterisation Of O Piceae Sterol Esterasesupporting

confidence: 55%

Section: Production and Characterisation Of O Piceae Sterol Esterasementioning

confidence: 74%

Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application to pitch control in pulping of Eucalyptus globulus wood

Calero-Rueda¹,

Gutiérrez²,

Rı́o³

et al. 2004

IJBT

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“…The native M. albomyces steryl esterase was also found to have high affinity to the fungal mycelium and Triton X-100 was used for recovery of the bound enzyme (Kontkanen et al, submitted). The high content of hydrophobic amino acid residues (41.1%) of STE1 might encourage binding, as well as aggregation, which is explained by the strong hydrophobic character of lipolytic enzymes (Brush et al, 1999;Rúa et al, 1997). This property of lipases/esterases provides possibilities to use these enzyme in immobilized systems, for example, in synthetic reactions, without the necessity for additional purification steps.…”

Section: Discussionmentioning

confidence: 99%

Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei

Kontkanen

Reinikainen

Saloheimo

2006

Biotech & Bioengineering

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The ste1 gene encoding a steryl esterase was isolated from the thermophilic fungus Melanocarpus albomyces. The gene has one intron, and it encodes a protein consisting of 576 amino acids. The deduced amino acid sequence of the steryl esterase was shown to be related to lipases and other esterases such as carboxylesterases. Formation of mature protein requires post-translational removal of a putative 18-amino-acid signal sequence and a 13-residue propeptide at the N-terminus. The intronless version of the Melanocarpus albomyces ste1 gene was expressed in Pichia pastoris under the inducible AOX1 promoter. The production level was low, and a large proportion of the total activity yield was found to be present intracellularly. However, the fact that steryl esterase activity was produced by P. pastoris cells carrying the expression cassette confirmed that the correct gene had been cloned. The ste1 gene was subsequently expressed in T. reesei under the inducible cbh1 promoter, and a clearly higher production level was obtained. About 60% of the total activity was bound to the fungal mycelium or to solid components of the culture medium, or existed as aggregates. Triton X-100 was successfully used to recover this activity. The heterologous production system in T. reesei provides a means of producing M. albomyces steryl esterase STE1 reliably in large scale for future studies.

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“…A major and minor lipase from the fungus O. piliferum were copurified by hydrophobic interaction chromatography on octyl sepharose FF, followed by ion exchange chromatography on Q sepharose FF (Brush et al, 1999). This protocol resulted in a 1000-fold purification of the lipase.…”

Section: Purification and Kinetic Characterization Of Lipasesmentioning

confidence: 99%

Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,269

712

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Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. Lipases occur widely in nature, but only microbial lipases are commercially significant. The many applications of lipases include speciality organic syntheses, hydrolysis of fats and oils, modification of fats, flavor enhancement in food processing, resolution of racemic mixtures, and chemical analyses. This article discusses the production, recovery, and use of microbial lipases. Issues of enzyme kinetics, thermostability, and bioactivity are addressed. Production of recombinant lipases is detailed. Immobilized preparations of lipases are discussed. In view of the increasing understanding of lipases and their many applications in high-value syntheses and as bulk enzymes, these enzymes are having an increasing impact on bioprocessing. D

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purification and characterization of extracellular lipases from ophiostoma piliferum

Cited by 21 publications

References 22 publications

Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application to pitch control in pulping of Eucalyptus globulus wood

Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application to pitch control in pulping of Eucalyptus globulus wood

Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei

Production, purification, characterization, and applications of lipases

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