Influence of the nature of the support on the catalytic performance of CALB: experimental and theoretical evidence

José, Carla; Toledo, María Victoria; Nicolás, Paula; Lasalle, Verónica; Ferreira, Marı́a Luján; Briand, Laura E.

doi:10.1039/c7cy02466e

Cited by 17 publications

(9 citation statements)

References 46 publications

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“…In the same way as for physical adsorption, both hydrophilic and hydrophobic supports can be used for covalent immobilization. 97 Jose et al 97 reported the use of functionalized chitosan, epoxy acrylic resin, and functionalized magnetite as supports for Candida antarctica lipase B covalent immobilization with subsequent application in the esterification of R/S-ibuprofen with ethanol. Another technique of immobilization was employed as well as other supports, but some decrease in the specific activity was observed in those immobilized by covalent bonding.…”

Section: Industrial and Engineering Chemistry Researchmentioning

confidence: 99%

Driving Immobilized Lipases as Biocatalysts: 10 Years State of the Art and Future Prospects

Facin¹,

Melchiors²,

Valério³

et al. 2019

Ind. Eng. Chem. Res.

116

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Immobilized lipase is a cost-effective biocatalyst for a wide variety of industrial applications, mainly in food, cosmetics, and pharmaceutics due to the huge number of so-called chemically catalyzed reactions of industrial interest that can be replaced by immobilized-enzyme catalysis. In this scenario, there is a growing demand to develop new products, supports, and immobilization protocols, as well as to elucidate the reaction mechanism aiming to cross the barrier imposed by the cost of immobilized lipases. As a large number of researchers have focused their efforts in order to find new applications taking into account new products emerging continuously, it is important to clarify the traditional and alternative process routes using immobilized lipases. In the past decade, almost 5000 research endeavors were reported, and this number continues to rise. This review reports the past 10 years of research work on the techniques used for lipase immobilization proposing a brief introduction about traditional immobilization techniques and an overview of the reactions catalyzed by immobilized lipases with a focus on applications and some products obtained by each pathway.

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Section: Industrial and Engineering Chemistry Researchmentioning

confidence: 99%

Driving Immobilized Lipases as Biocatalysts: 10 Years State of the Art and Future Prospects

Facin¹,

Melchiors²,

Valério³

et al. 2019

Ind. Eng. Chem. Res.

116

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“…5,6 The supporting materials should meet the demands for biocompatibility, stability, and high enzyme loadings. 7,8 Recently, graphene oxide (GO) has attracted wide attention due to its incredibly large specific surface area (single-layered and unique double-sided material), abundant oxygen-containing functional groups (such as hydroxyl, carbonyl, carboxyl, and epoxy groups), and high biocompatibility. 9,10 These unique physical and chemical properties make GO an outstanding supporting matrix for enzyme immobilization.…”

Section: Introductionmentioning

confidence: 99%

Construction of Novel Enzyme–Graphene Oxide Catalytic Interface with Improved Enzymatic Performance and Its Assembly Mechanism

Chen

Luo

2019

ACS Appl. Mater. Interfaces

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In the present study, a novel bioinorganic catalytic interface, combining the in situ radical polymerization technique with the noncovalent adsorption method, was successfully fabricated, and its assembly mechanism was explored. The in situ radical polymerization technique was applied to construct a polymer shell around the enzyme surface to form the protein nanocapsule. Then, protein nanocapsules assembled on the surface of graphene oxide (GO) through noncovalent interactions to fabricate the dual-immobilized enzyme system. Here, native organophosphorus hydrolase (OPH) and OPH nanocapsule (nOPH10) were immobilized on GO to form the traditional immobilized OPH (OPH@GO) and dual-immobilized OPH (nOPH10@GO), respectively. The introduced polymer shell could protect the enzyme from various denaturation factors and provide abundant functional groups to interact with supports to strengthen the interactions between them. Compared to native OPH and OPH@GO, the resulting nOPH10@GO exhibited enhanced catalytic activity, stability, and reusability. The nOPH10@GO was further used to construct the biosensor, which exhibited better detection performance compared with that of OPH@GO. These features indicated that the introduced enzyme immobilization system could enhance the enzymatic performance and broaden its application prospect.

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“…In the case of CALB, there is an immobilized commercial preparation supplied by Novozymes, Novozym ® 435, immobilized on a macroporous acrylic polymer resin (Lewatit VP OC 1600) [33]. This biocatalyst has been successfully used in diverse reactions, but it has been described to possess some limitations, like enzyme release in certain media, polymer dissolution in organic media, or the capture of hydrophilic compounds in the enzyme environment [33,34,35,36,37,38,39]. Thus, an alternative support may further increase the implementation of these interesting enzymes.…”

Section: Introductionmentioning

confidence: 99%

Ethyl Butyrate Synthesis Catalyzed by Lipases A and B from Candida antarctica Immobilized onto Magnetic Nanoparticles. Improvement of Biocatalysts’ Performance under Ultrasonic Irradiation

Monteiro

Neto

Fechine

et al. 2019

IJMS

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The synthesis of ethyl butyrate catalyzed by lipases A (CALA) or B (CALB) from Candida antarctica immobilized onto magnetic nanoparticles (MNP), CALA-MNP and CALB-MNP, respectively, is hereby reported. MNPs were prepared by co-precipitation, functionalized with 3-aminopropyltriethoxysilane, activated with glutaraldehyde, and then used as support to immobilize either CALA or CALB (immobilization yield: 100 ± 1.2% and 57.6 ± 3.8%; biocatalysts activities: 198.3 ± 2.7 Up-NPB/g and 52.9 ± 1.7 Up-NPB/g for CALA-MNP and CALB-MNP, respectively). X-ray diffraction and Raman spectroscopy analysis indicated the production of a magnetic nanomaterial with a diameter of 13.0 nm, whereas Fourier-transform infrared spectroscopy indicated functionalization, activation and enzyme immobilization. To determine the optimum conditions for the synthesis, a four-variable Central Composite Design (CCD) (biocatalyst content, molar ratio, temperature and time) was performed. Under optimized conditions (1:1, 45 °C and 6 h), it was possible to achieve 99.2 ± 0.3% of conversion for CALA-MNP (10 mg) and 97.5 ± 0.8% for CALB-MNP (12.5 mg), which retained approximately 80% of their activity after 10 consecutive cycles of esterification. Under ultrasonic irradiation, similar conversions were achieved but at 4 h of incubation, demonstrating the efficiency of ultrasound technology in the enzymatic synthesis of esters.

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Influence of the nature of the support on the catalytic performance of CALB: experimental and theoretical evidence

Abstract: CALB immobilized on hydrophobic supports exhibits higher conversion of ibuprofen and enantiomeric excess towards the S-enantiomer.

Cited by 17 publications

References 46 publications

Driving Immobilized Lipases as Biocatalysts: 10 Years State of the Art and Future Prospects

Driving Immobilized Lipases as Biocatalysts: 10 Years State of the Art and Future Prospects

Construction of Novel Enzyme–Graphene Oxide Catalytic Interface with Improved Enzymatic Performance and Its Assembly Mechanism

Ethyl Butyrate Synthesis Catalyzed by Lipases A and B from Candida antarctica Immobilized onto Magnetic Nanoparticles. Improvement of Biocatalysts’ Performance under Ultrasonic Irradiation

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