Specificities of immobilized Geotrichum candidum CMICC 335426 lipases A and B in hydrolysis and ester synthesis reactions in organic solvents

Charton, Emmanuelle; Macrae, Alasdair R.

doi:10.1016/0141-0229(93)90081-c

Cited by 24 publications

(13 citation statements)

References 12 publications

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“…Such results have also been reported whereby the lipases from G. candidum NRRL Y-553 and 26557 RP strain showed highest relative specificity constants for the competitive hydrolysis of oleic and palmitic methyl or butyl esters (Baillargeon et al 1989). Charton and Macrae (1993) reported that lipase from G. candidum CMICC 335426 showed no activity on tristearin, no significant activity on trilaurin, trimyristin, tripalmitin and low activity on tricaprylin and tricaprin in relative to triolein; while Sonnet et al (1993) observed a 1:10 relative reactivity of stearic versus oleic acid in esterification with 1-butanol catalysed by lipase of GC-4. Similar selectivity have been observed in commercial preparation of G. candidum lipase GC-20 (Amano International Enzyme) which showed relative activity of oleic and palmitic acid of 1.5:1 in hydrolysis of umbelliferate esters (Baillargeon 1990); while crude but free lipases from NRRL Y-553 showed a relative reactivity of oleic to palmitic acid of 20:1 (Baillargeon and McCarthy 1991).…”

Section: Composition Of Extracted Lipid Materialsmentioning

confidence: 95%

“…The lipase from G. candidum has been shown to possess unique specificity for fatty acids with cis-9 monounsaturated double bond, and these esters are hydrolysed more rapidly than other fatty acids (Baillargeon et al 1989;Baillargeon and McCarthy 1991;Charton and Macrae 1993). In a previous study (Loo et al 2006), it was shown that G. candidum produced a bound lipase that was able to hydrolyse 70% of palm olein during growth.…”

Section: Introductionmentioning

confidence: 96%

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Fatty acid preference of mycelium-bound lipase from a locally isolated strain of Geotrichum candidum

Loo

Lai

Long

et al. 2007

World J Microbiol Biotechnol

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Mycelium-bound lipase (MBL) was prepared using a strain of Geotrichum candidum isolated from local soil. At the time of maximum lipase activity (54 h), the mycelia to which the lipase was bound were harvested by filtration and centrifugation. Dry MBL was prepared by lyophilizing the mycelia obtained. The yield of MBL was 3.66 g/l with a protein content of 44.11 mg/g. The lipase activity and specific lipase activity were 22.59 and 510 U/g protein, respectively. The moisture content of the MBL was 3.85%. The activity of free (extracellular) lipase in the culture supernatant (after removal of mycelia) was less than 0.2 U/ml. The MBL showed selectivity for oleic acid over palmitic acid during hydrolysis of palm olein, indicating that the lipase from G. candidum displayed high substrate selectivity for unsaturated fatty acid containing a cis-9 double bond, even in crude form. This unique specificity of MBL could be a direct, simple and inexpensive way in the fats and oil industry for the selective hydrolysis or transesterification of cis-9 fatty acid residues in natural triacylglycerols.

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Section: Composition Of Extracted Lipid Materialsmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 96%

Fatty acid preference of mycelium-bound lipase from a locally isolated strain of Geotrichum candidum

Loo

Lai

Long

et al. 2007

World J Microbiol Biotechnol

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show abstract

“…on NKA resin and applied the resulting biocatalyst to the hydrolysis of fish oil, keeping 80% of relative activity after five cycles of reaction. In other work, Charton and Macrae (1993) using a porous polypropylene support pre-coated with ovalbumin, were able to immobilized lipase from G. candidum and to increase its enzymatic stability in organic solvent at high temperature.…”

Section: Introductionmentioning

confidence: 97%

Evaluation of partial purification and immobilization of lipase from Geotrichum candidum

Maldonado

Aguiar‐Oliveira

Fogaça

et al. 2015

Biocatalysis and Agricultural Biotechnology

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“…The lipase of Geotrichum canddidum has been described as one of the few known fatty acidspecific lipases (Jacobsen et al, 1990;Charton et Macrae, 1993;Jensen et al, 1972;Stránský et al, 2007;Hlavsová et al, 2009). It was shown that lipases of different strains of G. candidum have different substrate specificities.…”

Section: Introductionmentioning

confidence: 99%

Differences in hydrolytic abilities of two crude lipases from Geotrichum candidum 4013

Brabcová

Zarevúcká

Macková

2010

Yeast

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The fungus Geotrichum candidum 4013 produces two types of lipases (extracellular and cell-bound). Both enzymes were tested for their hydrolytic ability to pnitrophenyl esters and compounds having a structure similar to the original substrate (triacylglycerols). Higher lipolytic activity of extracellular lipase was observed when triacylglycerols of medium-(C12) and long-(C18) chain fatty acids were used as substrates. Cell-bound lipase preferentially hydrolysed trimyristate (C14). The differences in the abilities of these two enzymes to hydrolyse p-nitrophenyl esters were observed as well. The order of extracellular lipase hydrolysis relation velocity was as follows: p-nitrophenyl decanoate > p-nitrophenyl caprylate > p-nitrophenyl laurate > p-nitrophenyl palmitate > p-nitrophenyl stearate. The cell-bound lipase indicates preference for p-nitrophenyl palmitate. The most striking differences in the ratios between the activity of both lipases (extracellular : cell-bound) towards different fatty acid methyl esters were 2.2 towards methyl hexanoate and 0.46 towards methyl stearate (C18). The Michaelis constant (K m ) and maximum reaction rate (V max ) for p-nitrophenyl palmitate hydrolysis of cell-bound lipase were significantly higher (K m 2.462 mM and V max 0.210 U/g/min) than those of extracellular lipase (K m 0.406 mM and V max 0.006 U/g/min).

show abstract

Specificities of immobilized Geotrichum candidum CMICC 335426 lipases A and B in hydrolysis and ester synthesis reactions in organic solvents

Cited by 24 publications

References 12 publications

Fatty acid preference of mycelium-bound lipase from a locally isolated strain of Geotrichum candidum

Fatty acid preference of mycelium-bound lipase from a locally isolated strain of Geotrichum candidum

Evaluation of partial purification and immobilization of lipase from Geotrichum candidum

Differences in hydrolytic abilities of two crude lipases from Geotrichum candidum 4013

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