Conformation and activity of lipase B from Candida antarctica in bicontinuous microemulsions

Subinya, Mireia; Steudle, Anne K.; Jurkowski, Tomasz P.

doi:10.1016/j.colsurfb.2015.04.041

Cited by 14 publications

(3 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The tested buffer may have a stabilizing effect on the active site of the CALB immobilized on octyl-agarose beads. The high activity in an organic solvent (medium) could be related to the effect of the buffer on the ionization state of the catalytic triad and the interaction between the CALB and the support [36,37]. Additionally, the lipase loading could also have a significant impact on its activity.…”

Section: Effect Of Buffer Phmentioning

confidence: 99%

A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives

Siódmiak,

Dulęba,

Kocot

et al. 2024

IJMS

View full text Add to dashboard Cite

The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers of chiral drugs in reactions carried out in organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it is extremely important to develop optimal procedures to achieve a high enantioselectivity of the biocatalysts in the organic medium. Our paper describes a new approach to biocatalysis performed in an organic solvent with the use of CALB-octyl-agarose support including the application of a polypropylene reactor, an appropriate buffer for immobilization (Tris base—pH 9, 100 mM), a drying step, and then the storage of immobilized lipases in a climatic chamber or a refrigerator. An immobilized lipase B from Candida antarctica (CALB) was used in the kinetic resolution of (R,S)-flurbiprofen by enantioselective esterification with methanol, reaching a high enantiomeric excess (eep = 89.6% ± 2.0%). As part of the immobilization optimization, the influence of different buffers was investigated. The effect of the reactor material and the reaction medium on the lipase activity was also studied. Moreover, the stability of the immobilized lipases: lipase from Candida rugosa (CRL) and CALB during storage in various temperature and humidity conditions (climatic chamber and refrigerator) was tested. The application of the immobilized CALB in a polypropylene reactor allowed for receiving over 9-fold higher conversion values compared to the results achieved when conducting the reaction in a glass reactor, as well as approximately 30-fold higher conversion values in comparison with free lipase. The good stability of the CALB-octyl-agarose support was demonstrated. After 7 days of storage in a climatic chamber or refrigerator (with protection from humidity) approximately 60% higher conversion values were obtained compared to the results observed for the immobilized form that had not been stored. The new approach involving the application of the CALB-octyl-agarose support for reactions performed in organic solvents indicates a significant role of the polymer reactor material being used in achieving high catalytic activity.

show abstract

Section: Effect Of Buffer Phmentioning

confidence: 99%

A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives

Siódmiak,

Dulęba,

Kocot

et al. 2024

IJMS

View full text Add to dashboard Cite

show abstract

“…Notably, Aac SHC activity toward its natural substrate squalene has also been demonstrated in bicontinuous microemulsions . In collaboration with the groups of Engelskirchen and Stubenrauch from the University of Stuttgart, with whom studies on lipase B from Candida antarctica in bicontinuous microemulsions − were previously performed, Aac SHC was tested in a microemulsion consisting of buffer– n -octane–nonionic surfactant. The studies showed that Aac SHC in the bicontinuous microemulsions exhibited significantly increased selectivity toward hopene formation and that the conformation of Aac SHC was not affected in an environment of surfactant and organic solvent.…”

Section: To New Beginningsbernhard′s Time In Stuttgartmentioning

confidence: 99%

A Career in Catalysis: Bernhard Hauer

Nebel¹,

Breuer

Schneider

et al. 2023

ACS Catal.

View full text Add to dashboard Cite

On the occasion of Professor Bernhard Hauer′s (partial) retirement, we reflect on and highlight his distinguished career in biocatalysis. Bernhard, a biologist by training, has greatly influenced biocatalysis with his vision and ideas throughout his four-decade career. The development of his career went hand in hand with the evolution of biocatalysis and the application and development of enzymes for chemical processes. In this Account, we present selected examples of his early work on the development of enzymes and their application in an industrial setting, with a focus on his specific contributions to harnessing the catalytic power of enzymes for novel reactions and the understanding and engineering of flexible loops and channels on catalysis.

show abstract

“…Bicontinuous microemulsion is often called ''optimal microemulsion'' due to its ultra-low interfacial tension. [13][14][15] Therefore, it is important to formulate new types of bicontinuous microemulsions and evaluate the catalytic performance of an enzyme hosted in these media. Hellweg et al reported that in the two sugar surfactant-stabilized bicontinuous microemulsions (consisting of cyclohexane/water/ C 8/10 G 1.3 /n-pentanol and Lanol 99/water/Simulsol SL55/n-pentanol), diisopropyl fluorophosphatase (DFPase) showed high stability and activity.…”

Section: Introductionmentioning

confidence: 99%

Study on the catalytic performance of laccase in the hydrophobic ionic liquid-based bicontinuous microemulsion stabilized by polyoxyethylene-type nonionic surfactants

Wang

et al. 2016

Soft Matter

View full text Add to dashboard Cite

To formulate a compatible green medium for the conversion of a hydrophobic substrate by a hydrophilic enzyme, we investigated the phase behavior of pseudo ternary hydrophobic ionic liquid (HIL)/buffer/polyoxyethylene-type nonionic surfactant (CnEm)/n-alcohol system and the effects of the components on the formulation of the HIL-based bicontinuous microemulsion. It is found that small head group of the surfactant, high concentration of n-alcohol (medium/long alkyl chain) and low cohesive energy density of the HIL result in low phase transition temperature. In the CnEm stabilized compatible bicontinuous microemulsion, the kinetics of laccase catalyzed oxidation of 2,6-dimethoxyphenol were also investigated. It is found that in addition to temperature, n-alcohol is the key parameter affecting the catalytic performance of laccase, and the optimum n-alcohol depends on the type of HIL as an oil phase. All the kinetic parameters, such as Km, kcat, kcat/Km, and Ea (apparent activation energy), indicate that the bicontinuous microemulsion consisting of [Omim]NTf2/buffer/CnEm/n-hexanol is a suitable medium for the laccase-catalyzed reaction. To the best of our knowledge, this is the first report on the formulation of HIL-based bicontinuous microemulsion for enzyme catalysis.

show abstract

Conformation and activity of lipase B from Candida antarctica in bicontinuous microemulsions

Cited by 14 publications

References 30 publications

A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives

A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives

A Career in Catalysis: Bernhard Hauer

Study on the catalytic performance of laccase in the hydrophobic ionic liquid-based bicontinuous microemulsion stabilized by polyoxyethylene-type nonionic surfactants

Contact Info

Product

Resources

About