Substrate specificity and kinetics of Candida rugosa lipase in organic media

Janssen, A.E.M.; Vaidya, A. M.; Halling, Peter J.

doi:10.1016/0141-0229(95)00075-5

Cited by 96 publications

(62 citation statements)

References 30 publications

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“…27 For Candida rugosa lipase, that has an aliphatic site positioned in a long tunnel inside the protein with a wide entrance involved in the binding of the scissile fatty acid chain, 29 previous studies showed a clear preference for short and medium chain fatty acids, mainly C 4 , C 8 and C 10 . 30 This could explain the poor molar conversion attained by this lipase source under the reaction conditions used here.…”

Section: Influence Of Lipase Sourcementioning

confidence: 83%

Enzymatic synthesis of glyceride esters in solvent-free system: influence of the molar ratio, lipase source and functional activating agent of the support

Freitas¹,

Pérez²,

Santos³

et al. 2007

J. Braz. Chem. Soc.

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Este trabalho avaliou a influência de fatores que afetam a síntese de ésteres glicéricos, tais como: razão molar entre os reagentes, fonte de lipase e tipo de agente de ativação do suporte obtido pela técnica sol-gel. Foram empregadas preparações comerciais de lipases imobilizadas em partículas de polissiloxano-álcool polivinílico (POS-PVA) previamente ativadas com diferentes agentes (glutaraldeído, metaperiodato de sódio e carbonildiimidazol). Esses resultados foram comparados com aqueles obtidos por preparações de lipase imobilizada disponíveis comercialmente (Lipozyme IM 20 , Novozym 435, Lipozyme RM IM e Lipozyme TL IM). O meio reacional contendo excesso de glicerol favoreceu a síntese de ésteres glicéricos e a Lipozyme IM 20 foi a preparação de lipase imobilizada mais adequada para a síntese, atingindo conversões molares maiores que 94%. O uso da lipase CALB L imobilizada em POS-PVA também alcançou resultados satisfatórios (cerca de 80% de conversão) possibilitando a formação de 36% de 2,3-diidroxipropil dodecanoato (monolaurina).This work assessed the influence of important factors that affect the synthesis of glyceride esters in solvent-free systems, such as: glycerol/fatty acid molar ratio, lipase source and activating agent of the support obtained by the sol-gel technique. Commercial lipase preparations were immobilized on polysiloxane-polyvinyl alcohol particles (POS-PVA) previously activated with different agents (glutaraldehyde, sodium metaperiodate and carbonyldiimidazole) and their performance on the esterification reaction was compared with commercial preparations of immobilized lipase (Lipozyme IM 20 , Novozym 435, Lipozyme RM IM and Lipozyme TL IM). The reaction medium containing excess glycerol favored the glyceride ester synthesis and the Lipozyme IM 20 was found to be the most suitable immobilized lipase preparation, attaining molar conversions higher than 94%. The use of CAL B Lipase immobilized on POS-PVA also provided satisfactory performance (conversion of about 80%) and allowed the formation of 36% wt of 2,3-dihydroxypropyl dodecanoate (monolaurin).Keywords: glycerides, lipase, esterification, hybrid support, immobilization IntroductionThe demand of the industries to operate their processes under sustained conditions such as green chemistry or clean technology systems is becoming an important issue nowadays and thus requests the availability of tailored biocatalysts to operate under these conditions. 1 Therefore, the need for developing active and stable immobilized biocatalysts for subsequent use in biotransformations has been highlighted. 2 Among the most important biocatalysts carrying out novel reactions in both aqueous and non aqueous media, lipases stand out due to their ability to utilize a wide spectrum of substrates, high stability towards extremes of temperature, pH and organic solvents, and chemo-, regio-and enantioselectivity. [3][4][5] Although most enzymatic syntheses are performed in presence of organic non-polar solvents, 6 the elimination of these compounds is technicall...

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Section: Influence Of Lipase Sourcementioning

confidence: 83%

Enzymatic synthesis of glyceride esters in solvent-free system: influence of the molar ratio, lipase source and functional activating agent of the support

Freitas¹,

Pérez²,

Santos³

et al. 2007

J. Braz. Chem. Soc.

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“…2, the nine lipases showed different optimal pH profiles. Except that the pH optima for J 8-2 Rhizopus oryzae lipase, MJ 2 Aspergillus oryzae lipase and MJ 1 Aspergillus niger lipase were in the acidic range (they were pH 6.0, 6.5, and 7.0, respectively), the other six lipases belong to the alkaline lipases: M 2 Mucor racemosus lipase, Y-11 Trichosporon capitatum lipase and S 11 Geotrichum candidum lipase showed their highest enzyme activity under weakly basic pH conditions (the optimal pH values for their activity were all pH 8.0), and the optimal pH for S 9 Candida lypolytica lipase was also weakly basic (pH 8.5), while the highest enzyme activities for Penicillum citrinum lipase and YM Bacillus coughing lipase were obtained under alkaline conditions (the pH optima were pH 9.0 and 10.0, respectively).…”

Section: Temperature Optima and Ph Optima Of Nine Lipasesmentioning

confidence: 98%

“…2 and Table 1, the pH stabilities of the nine lipases showed significant differences: Y-11 Trichosporon capitatum lipase was rather stable in the pH range of 8.0-10.5 (its activity at pH 10.5 was less than 15% of that at pH 8.0), whereas the activity of J Rhizopus oryzae lipase at pH 5.0 was less than 35% of that at pH 6.0, and the activity of MJ 2 Aspergillus oryzae lipase at pH 5.5 was less than 20% of that at pH 6.5 and compared with the activity of S 3 Penicillum citrinum lipase at pH 8.5, which at pH 7.5 was 33% less. For M 2 Mucor racemosus lipase, S 9 Geotrichum candidum lipase, S 11 …”

Section: Thermal Stability and Ph Stability Of Nine Lipasesmentioning

confidence: 99%

Studies of substrate specificities of lipases from different sources

Song

Hao

et al. 2008

Euro J Lipid Sci & Tech

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Although lipases are widely applied in a wide variety of reactions, available information on the factors that are responsible for the substrate specificities of lipases from different sources is scarce. In this paper, nine lipase-producing microorganism strains were isolated from oil-containing samples. The properties of these enzymes, including pH optima, temperature optima, thermal stability, and pH stability, vary significantly with the different sources from which these lipases were isolated. The substrate specificities of the nine lipases, including fatty acid and positional specificities, were also studied. The fatty acid specificities of the nine lipases were observably different toward 15 substrates with different carbon chain lengths, different saturation degrees and different side chains. The lipases from S 3 Penicillium citrinum (PCL), MJ 1 Aspergillus niger (ANL), MJ 2 Aspergillus oryzae (AOL), YM Bacillus coughing (BCL), S 9 Geotrichum candidum (GCL), and S 11 Candida lypolytica (CLL) showed the strongest specificities to short-chain esters, and the other lipases showed strong selectivity for medium-or long-chain and branched esters. The positional specificities were examined by analyzing the hydrolytic products of triolein catalyzed by the nine lipases, using TLC. The lipases can be mainly classified into two groups by their specificities for the ester bond at position 2 of triglycerides; one group can selectively hydrolyze the ester bond at position 2 of the triglycerides, the other group cannot. All these nine lipases were divided into four groups by hierarchical clustering analysis on the basis of the results of fatty acid and positional specificities.

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“…It may be because PKL have the higher percentage of shorter fatty acid chain compared to PKS. Janssen et al reported that binding of the short chain fatty acids is much better than for the long chain fatty acid (16). The V max for PKS are higher compared to PKL at the particular temperature, which may be due to the slow conversion of substrate to product.…”

Section: Synthesis Of Palm Kernel Oil Alkanolamide Using Lipasementioning

confidence: 97%