Evaluation of strains of Geotrichum candidum for lipase production and fatty acid specificity

Baillargeon, Mary Welch; Bistline, R. G.; Sonnet, Philip E.

doi:10.1007/bf00256003

Cited by 76 publications

(36 citation statements)

References 14 publications

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“…Thus, it can be proposed that lipase release into culture medium is triggered by decrease of external lipid under a critical level. Early e nzyme release with an increase in stirring speed has also been observed with Penicillium restrictum (Freire et al, 1997a), and Geotrichum candidum (Baillargeon et al, 1989).…”

Section: Discussionmentioning

confidence: 79%

Improvement of lipase production at different stirring speeds and oxygen levels

Alonso

Oliveira

Dellamora-Ortiz

et al. 2005

Braz. J. Chem. Eng.

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-Lipase production by a Brazilian wild strain of Yarrowia lipolytica at different stirring speeds and air flow rates was studied. The relationship among lipid consumption, cell growth and lipase production by this microorganism is presented. The most pronounced effect of oxygen on lipase production was determined by stirring speed. Maximum lipase activity was detected in the late stationary phase at 200 rpm and an air flow rate of 1-2 dm 3 /min (0.8-1.7 vvm) when the lipid source had been fully consumed. Higher stirring speeds resulted in mechanical and/or oxidative stress, while lower stirring speeds seemed to limit oxygen levels. An increase in the availability of oxygen at higher air flow rates led to faster lipid uptake and anticipation of enzyme release into the culture medium. The highest lipase production was obtained at 200 rpm and 1 dm 3 /min (0.8 vvm).

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Section: Discussionmentioning

confidence: 79%

Improvement of lipase production at different stirring speeds and oxygen levels

Alonso

Oliveira

Dellamora-Ortiz

et al. 2005

Braz. J. Chem. Eng.

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“…For example, using methyl and butyl esters of oleic and palmitic acids to examine the specificity of crude enzyme preparations from a series of GC strains, strains ATCC 34614 and NRRL Y-552 were reported to produce lipases which did not discriminate between 1 8 : l and 16:O fatty acid esters. However, lipases from other strains (including NRRL Y-553) showed a preference for 18: 1 methyl ester (Baillargeon et al, 1989;Baillargeon and Sonnet, 1991). That GC produces multiple isozymes was realized early, but their separation proved to be difficult.…”

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confidence: 99%

Polymorphism in the lipase genes of Geotrichum candidum strains

Bertolini

Laramée

Thomas

et al. 1994

European Journal of Biochemistry

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The fungus Geotrichum candidum produces extracellular lipases. Purification and characterization of different lipase isoforms from various G. candidum strains is difficult due to the close physical and biochemical properties of the isoforms. Consequently, the characterization of these enzymes and their substrate specificities has been difficult. We have determined the lipase genes present in four strains of G. candidum (ATCC 34614, NRCC 205002, NRRL Y-552 and NRRL Y-553) by molecular cloning and DNA sequencing. Each strain contains two genes similar to the previously identified lipase I and lipase I1 cDNAs. Our data suggest that no other related lipase genes are present in these strains. Each lipase-gene family shows sequence variation (polymorphism) that is confirmed by Southern-blot analysis. This polymorphism and the sequence differences between lipase I and lipase I1 have been localized within the previously determined three-dimensional structure of lipase 11. Although most of the amino acid substitutions are located on the protein surface, some are present in structural features possibly involved in determining substrate specificity.Lipases (glycerol ester hydrolases) are rather unusual amongst soluble enzymes in that they exhibit increased activity at a waterdipid interface (Brockman, 1984), a phenomenon called interfacial activation. This activation process involves large movement of one surface loop (flap) which is sometimes associated with movements of other loops (Brzozowski et al., 1991;Grochulski et al., 1993: van Tilbeurgh et al., 1993. A great need to understand the molecular basis of lipase catalysis and substrate selectivity arises from their high industrial potential.The lipase produced by the fungus Geotrichum candidum (GC) was one of the first lipases investigated and many reports on its production, isolation, activity and selectivity appeared over the years (for review see Charton, 1991). Crude enzyme preparations from different GC strains exhibited varying degrees of specificity for the kind and position of the fatty acids hydrolyzed from triacylglycerols and fatty esters. For example, using methyl and butyl esters of oleic and palmitic acids to examine the specificity of crude enzyme preparations from a series of GC strains, strains ATCC 34614 and NRRL Y-552 were reported to produce lipases which did not discriminate between 1 8 : l and 16:O fatty acid esters. However, lipases from other strains (including NRRL Y-553) showed a preference for 18: 1 methyl ester (Baillargeon et al

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“…Bacterial lipases production needed adequate DOI: 10.9790/3008-120101105114 www.iosrjournals.org 109 | Page carbon source and sufficient incubation period which varied from a few hours to several days depending on the bacteria and environmental conditions (Vishnupriya et al, 2010). Similarly, the lipase from G. candidum (Baillargeon et al, 1989) showed the highest activity when the initial pH of the medium was adjusted to pH 7.0 while pH was 5.0 for Geotrichum (Macedo et al, 1997), 6.0 for Geotrichum-like R59 . The molecular weight of the purified lipase has 62 kDa and the same molecular weight was obtained by Abdul Hamid et al (2003).…”

Section: Discussionmentioning

confidence: 98%