Substrate specificities of lipases A and B from Geotrichumcandidum CMICC 335426

Charton, Emmanuelle; Macrae, Alasdair R.

doi:10.1016/0005-2760(92)90171-q

Cited by 48 publications

(28 citation statements)

References 15 publications

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“…G. candidum lipases A and B were immobilized on Accurel EP 100 porous polypropylene supports, precoated with ovalbumin to increase stability in organic solvents and at elevated temperatures (Charton and Macrae, 1992). Bosley and Clayton (1994) used hydrophobic controlled pore glasses to immobilize R. miehei lipase.…”

Section: Immobilization Of Lipasesmentioning

confidence: 99%

Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,284

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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Section: Immobilization Of Lipasesmentioning

confidence: 99%

Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,284

712

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“…This fungus produces multiple extracellular lipases: lipases A and B from G. candidum CMICC 335426, and lipases I (major), II, III, and IV from G. candidum ATCC 34614 (Sidebottom et al, 1991;Sugihara et al, 1991). Among these G. candidum lipases (GCLs), GCL B and GCL I have shown a preference for cis-9 unsaturated FAs and discrimination against trans-9-containing structures and EA, although the structural basis is still obscure (Holmquist et al, 1997;Sidebottom et al, 1991;Charton and Macrae, 1992). Residues within GCL I sequence positions of 349-406 were considered to be essential in recognizing cis-9 fatty acyls (Holmquist et al, 1997;Holmquist, 1998).…”

Section: Lipase Specificities For Ea Enrichmentmentioning

confidence: 99%

Enzymatic Isolation and Enrichment of Erucic Acid From Hea Seed Oils: Current Status

Tao¹,

He²

2005

Transactions of the ASAE

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“…This fungus expresses two closely related lipases (Shimada et al 1989(Shimada et al , 1990) with 86% amino acid identity. Despite such high similarity these lipase isoforms display different specificity profiles (Charton and Macrae 1992) and present an excellent system for the identification of key residues involved in the differentiation between fatty acyl chains. We cloned both isoforms in yeast (Vernet et al 1993;Bertolini et al 1994) and characterized their activity profiles with a wide variety of triglyceride substrates (Bertolini et al 1995).…”

Section: Fatty Acyl Chain Preferencesmentioning

confidence: 99%

Structural determinants defining common stereoselectivity of lipases toward secondary alcohols

Cygler

Grochulski²,

Schrag³

1995

Can. J. Microbiol.

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/npsi/ctrl?action=rtdoc&an=3538624&lang=en http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/ctrl?action=rtdoc&an=3538624&lang=frAccess and use of this website and the material on it are subject to the Terms and Conditions set forth at http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/jsp/nparc_cp.jsp?lang=en NRC Publications Archive Archives des publications du CNRCThis publication could be one of several versions: author's original, accepted manuscript or the publisher's version. / La version de cette publication peut être l'une des suivantes : la version prépublication de l'auteur, la version acceptée du manuscrit ou la version de l'éditeur. For the publisher's version, please access the DOI link below./ Pour consulter la version de l'éditeur, utilisez le lien DOI ci-dessous.http://dx.doi.org/10.1139/m95-199Canadian Journal of Microbiology, 41, 13, pp. 289-296, 1995 Structural determinants defining common stereoselectivity of lipases toward secondary alcohols Cygler, Miroslaw; Grochulski, Pawel; Schrag, Joseph D. Abstract: In this review we summarize some aspects of the enantiopreference of the lipase from Candida rugosa following structural analysis of complexes of this lipase with two enantiomers of an analog of a tetrahedral intermediate in the hydrolysis of simple esters. The analysis of the molecular basis of the enantiomeric differentiation suggests that these results can be generalized to a large class of lipases and esterases. We also summarize our experiments on identification of the key regions in the lipases from Geotrichum candidum lipase responsible for differentiation between fatty acyl chains. Structural determinants defining

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Substrate specificities of lipases A and B from Geotrichumcandidum CMICC 335426

Cited by 48 publications

References 15 publications

Production, purification, characterization, and applications of lipases

Production, purification, characterization, and applications of lipases

Enzymatic Isolation and Enrichment of Erucic Acid From Hea Seed Oils: Current Status

Structural determinants defining common stereoselectivity of lipases toward secondary alcohols

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