1988
DOI: 10.1007/bf02542388
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Polyethylene glycol modification ofCandida rugosa lipase

Abstract: Polyethylene glycol (PEG) was covalently attached to lipase (EC 3.1.1.3) fromCandida rugosa yielding a modified lipase of higher specific activity in hydrolytic and synthetic reactions in organic solvents. PEG of molecular weights 5000 and 1900 solubilized the lipase in selected organic solvents, but PEG of molecular weight 750 was too small to accomplish this completely. The modified lipase was 10 times more stable in water than native lipase, but was less stable in benzene. The selectivity of the modified li… Show more

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Cited by 49 publications
(12 citation statements)
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References 17 publications
(6 reference statements)
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“…Similar results have been reported by Ampon et al (1991) using alkyl-lipase as biocatalyst in the esterification of oleic acid in benzene, and this is in agreement with observations made by Klibanov (Volkin et al, 1991;Zaks and Klibanov, 1984) and Baillergeou and Sonnet (1988). We can observe that stability increases with the modification degree, and thus CRSL-pNPCF-1/30 is the most stable derivative.…”
Section: Thermal Deactivation In Organic Solventsupporting
confidence: 95%
See 1 more Smart Citation
“…Similar results have been reported by Ampon et al (1991) using alkyl-lipase as biocatalyst in the esterification of oleic acid in benzene, and this is in agreement with observations made by Klibanov (Volkin et al, 1991;Zaks and Klibanov, 1984) and Baillergeou and Sonnet (1988). We can observe that stability increases with the modification degree, and thus CRSL-pNPCF-1/30 is the most stable derivative.…”
Section: Thermal Deactivation In Organic Solventsupporting
confidence: 95%
“…In the case of CRSL-pNPCF this value is higher than the modification degree obtained by Basri et al (1995) (55%), who worked with a different kind of enzyme (C. rugosa Type IV, M w 120,000) and under other experimental conditions. In the case of CRSL-CC, Baillergeou and Sonnet (1988) described a 10-fold molar excess of the activated PEG to free amino groups of the commercial lipase and obtained 36% modification. The small chemical modification percentage obtained by these authors can be explained by the presence of many impurities (glycopeptides, lactose) in the commercial powder (Rúa et al, 1993).…”
Section: Chemical Modification Of the Lipasesmentioning
confidence: 99%
“…In addition, organic reaction media improves substrate solubility and stability and aids facile product recovery (Dordick, 1989;Klibanov, 1990). However, crude lipases typically show little or no activity in organic solvents, hence methods to irnprove both the activity and stability are of particular importance (Baillargeon & Sonnet, 1988;Basri et al, 1992).…”
mentioning
confidence: 99%
“…Hydrolysis [mmol FFA/(g·h)] and interesterification activities [mmol PPS/(g ⋅ h)] using SA IML after 4 h with continuous batch reactions(1)(2)(3)(4). For reaction 5 no water was added to the reaction media.…”
mentioning
confidence: 99%
“…Recent attention has focused on using lipases for the conversion of fats and oils to produce high-value products (1,2). Lipases typically show little or no activity in organic solvents, hence, methods to improve both activity and stability are of particular importance (3,4). Enzyme coating by oil-soluble surfactants and lipids has greatly enhanced activity in organic media (5)(6)(7)(8)(9).…”
mentioning
confidence: 99%