Candida Rugosa

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Simonetta Soro - One of the best experts on this subject based on the ideXlab platform.

  • Monoclonal antibodies against Candida Rugosa lipase
    Journal of Molecular Catalysis B-enzymatic, 2004
    Co-Authors: Hassan Rahimi, Simonetta Soro, Aurelia Rughetti, Cleofe Palocci, Mauro Biffoni, Serena Barachini, Federica Taurino, Enrico Cernia, Luigi Frati, Marianna Nuti
    Abstract:

    Abstract We generated monoclonal antibodies (MoAbs) BF11 and VNH9 against Candida Rugosa lipase (CRL), one of the most widely used lipolytic enzymes. The antibodies, both of the IgG1 isotype recognize specie specific and distinct antigenic determinants shared by different CRL isoforms present both in the native and in the denaturated form of the enzyme. The CRL enzyme maintained its enzymatic activity even when immunocomplexed with MoAb BF11 and VNH9. These novel reagents are of interest for their possible application as immobilization and purification systems, and during fermentation processes.

  • High yield and optical purity in biocatalysed acylation of trans-2-phenyl- 1-cyclohexanol with Candida Rugosa lipase in non-conventional media
    Journal of Molecular Catalysis B: Enzymatic, 1999
    Co-Authors: Elena C Celia, Enrico Cernia, Cleofe Palocci, Ilaria D'acquarica, Simonetta Soro
    Abstract:

    Abstract Candida Rugosa lipase (CRL) shows high enantioselectivity toward (1 R ,2 S )-(−)- trans -2-phenyl-1-cyclohexanol enantiomer in acetylation reaction employing vinyl acetate as acyl donor. Attempts to improve reaction yields have pointed out that supercritical CO 2 is the best reaction medium in the studied biocatalytic process. In these conditions an immobilised lipase from Candida Rugosa is able to quantitatively resolve racemate with e.e. p 100%.

Carles Solà - One of the best experts on this subject based on the ideXlab platform.

  • Improving lipase production from Candida Rugosa by a biochemical engineering approach
    Chemistry and Physics of Lipids, 1998
    Co-Authors: M. A. Gordillo, Francisco Valero, Javier Lafuente, J. L. Montesinos, C. Casas, Carles Solà
    Abstract:

    It has been tested that the use of oleic acid as sole carbon source and as inducer of the production has an important effect in the lipase production by Candida Rugosa under aerobic conditions. A simple structured mathematical model coupled with a methodology to estimate biomass, specific growth rate and substrate was developed and applied to the production of Candida Rugosa lipase in batch, fed-batch and continuous operation to obtain a reproducible product. The best operation mode tested was a controlled specific growth rate fed-batch with a 10-fold increase in productivity related to batch operation. Downstream of the culture broth has demonstrated that the ratio between the different isoenzymes presented can be modulated by the selection of the operational strategy and this ratio is quite different comparing with commercial lipases. Thus, their catalytic properties in front of chiral reactions could be different.

  • Enantioselective esterification of 2-arylpropionic acids and trans-2-phenyl-1-cyclohexanol: Comparison between immobilised lipases from Candida Rugosa and Rhizomucor miehei
    Biotechnology Letters, 1998
    Co-Authors: Antoni Sánchez, Francisco Valero, Javier Lafuente, Carles Solà
    Abstract:

    2-Phenyl propionic acid, ibuprofen and trans-2-phenyl-1-cyclohexanol were resolved using commercial Rhizomucor miehei lipase (Lipozyme IM20) and Candida Rugosa lipase produced in our laboratory immobilised on EP100 polypropylene powder. Important differences were found on the enantioselectivity of both lipases in esterification reactions. Candida Rugosa lipase was more enantioselective in the resolution of the tested substrates, especially with trans-2-phenyl-1-cyclohexanol, whereas the lipase from Rhizomucor miehei did not show catalytic activity with this substrate. © Rapid Science Ltd. 1998

  • Effects of different fatty acids in lipase production by Candida Rugosa
    Biotechnology Letters, 1993
    Co-Authors: Nuria Obradors, Francisco Valero, J. L. Montesinos, F J Lafuente, Carles Solà
    Abstract:

    Oleic acid has been reported as a good inducer of lipase production by Candida Rugosa. In order to know if this enzyme is induced by oleic acid itself or by a metabolite, different short chain fatty acids were tested. Butyric acid was the best carbon source to growth microorganism but it did not induce lipase production. Although caprylic and capric acid were the best inducers of lipase production, at concentrations up 1 g/l they have toxic effect in Candida Rugosa growth. Thus, from the point of view of industrial production oleic acid could be considered as the best substrate tested.

  • A model for lipase production by Candida Rugosa
    Bioprocess Engineering, 1992
    Co-Authors: Pau Serra, Carles Solà, J. L. Del Rio, J. Robusté, Manel Poch, A. Cheruy
    Abstract:

    A model adequately describing the lipase production by Candida Rugosa has been developed, calibrated and validated using new experimental data. Process modelling has been done using CAMBIO software (Computer Aided Modelling of BIOprocesses), allowing to easy and interactively test various hypothesis and reaction schemes.

  • Lipase production by immobilized Candida Rugosa cells
    Applied Microbiology and Biotechnology, 1992
    Co-Authors: Pau Ferrer, Carles Solà
    Abstract:

    Immobilization of Candida Rugosa cells on a solid support for extracellular lipase production has been explored. The use of Ca-alginate beads and of mixed matrix of polyurethane foam/Ca-alginate beads enabled us to operate a batch and a continuous four-phase fluidized bed bioreactor. Cells co-entrapped together with polyurethane into Ca-alginate did not show higher lipase production levels than the cells entrapped in Ca-alginate gels. The addition of gum arabic to the medium greatly enhanced lipase production without affecting the hydrodynamic operating conditions significantly. This fact demonstrates that the reactor system is limited in terms of organic substrate dispersion and direct contact with cells.

Shi-chang Wang - One of the best experts on this subject based on the ideXlab platform.

  • Esterification reactions catalyzed by surfactant-coated Candida Rugosa lipase in organic solvents
    Process Biochemistry, 2002
    Co-Authors: Bao-dong Song, Ai-hua Xing, Yoshishige Hayashi, Mahabubur Rahman Talukder, Shi-chang Wang
    Abstract:

    Abstract Lipase from Candida Rugosa was coated with glutamic acid didodecyl ester ribitol amide as catalyst in organic solvents. The surfactant-coated lipase showed considerable activity for the esterification of lauryl alcohol and lauric acid in iso-octane, while almost no activity was observed when the native powder lipase was used. The optimal pH of the buffer used for preparation of the coated lipase was around 7. The optimum reaction temperature was around 30 °C and the best solvent was iso-octane. The half-life of the coated lipase at 30 °C was ≈10 h. The surfactant-coated Candida Rugosa lipase was most suitable for catalyzing esterification reactions of fatty acid and fatty alcohol both with a medium chain length.

Cleofe Palocci - One of the best experts on this subject based on the ideXlab platform.

  • Monoclonal antibodies against Candida Rugosa lipase
    Journal of Molecular Catalysis B-enzymatic, 2004
    Co-Authors: Hassan Rahimi, Simonetta Soro, Aurelia Rughetti, Cleofe Palocci, Mauro Biffoni, Serena Barachini, Federica Taurino, Enrico Cernia, Luigi Frati, Marianna Nuti
    Abstract:

    Abstract We generated monoclonal antibodies (MoAbs) BF11 and VNH9 against Candida Rugosa lipase (CRL), one of the most widely used lipolytic enzymes. The antibodies, both of the IgG1 isotype recognize specie specific and distinct antigenic determinants shared by different CRL isoforms present both in the native and in the denaturated form of the enzyme. The CRL enzyme maintained its enzymatic activity even when immunocomplexed with MoAb BF11 and VNH9. These novel reagents are of interest for their possible application as immobilization and purification systems, and during fermentation processes.

  • High yield and optical purity in biocatalysed acylation of trans-2-phenyl- 1-cyclohexanol with Candida Rugosa lipase in non-conventional media
    Journal of Molecular Catalysis B: Enzymatic, 1999
    Co-Authors: Elena C Celia, Enrico Cernia, Cleofe Palocci, Ilaria D'acquarica, Simonetta Soro
    Abstract:

    Abstract Candida Rugosa lipase (CRL) shows high enantioselectivity toward (1 R ,2 S )-(−)- trans -2-phenyl-1-cyclohexanol enantiomer in acetylation reaction employing vinyl acetate as acyl donor. Attempts to improve reaction yields have pointed out that supercritical CO 2 is the best reaction medium in the studied biocatalytic process. In these conditions an immobilised lipase from Candida Rugosa is able to quantitatively resolve racemate with e.e. p 100%.

Enrico Cernia - One of the best experts on this subject based on the ideXlab platform.

  • Monoclonal antibodies against Candida Rugosa lipase
    Journal of Molecular Catalysis B-enzymatic, 2004
    Co-Authors: Hassan Rahimi, Simonetta Soro, Aurelia Rughetti, Cleofe Palocci, Mauro Biffoni, Serena Barachini, Federica Taurino, Enrico Cernia, Luigi Frati, Marianna Nuti
    Abstract:

    Abstract We generated monoclonal antibodies (MoAbs) BF11 and VNH9 against Candida Rugosa lipase (CRL), one of the most widely used lipolytic enzymes. The antibodies, both of the IgG1 isotype recognize specie specific and distinct antigenic determinants shared by different CRL isoforms present both in the native and in the denaturated form of the enzyme. The CRL enzyme maintained its enzymatic activity even when immunocomplexed with MoAb BF11 and VNH9. These novel reagents are of interest for their possible application as immobilization and purification systems, and during fermentation processes.

  • High yield and optical purity in biocatalysed acylation of trans-2-phenyl- 1-cyclohexanol with Candida Rugosa lipase in non-conventional media
    Journal of Molecular Catalysis B: Enzymatic, 1999
    Co-Authors: Elena C Celia, Enrico Cernia, Cleofe Palocci, Ilaria D'acquarica, Simonetta Soro
    Abstract:

    Abstract Candida Rugosa lipase (CRL) shows high enantioselectivity toward (1 R ,2 S )-(−)- trans -2-phenyl-1-cyclohexanol enantiomer in acetylation reaction employing vinyl acetate as acyl donor. Attempts to improve reaction yields have pointed out that supercritical CO 2 is the best reaction medium in the studied biocatalytic process. In these conditions an immobilised lipase from Candida Rugosa is able to quantitatively resolve racemate with e.e. p 100%.