Physical adsorption used to the immobilization of Burkholderia cepacia lipase into powder polymeric supports

Corrêa, Wellington Moreira; Bortolozo, Ausdinir D.; Osório, Wislei R.; Padilha, Giovana da Silva

doi:10.1007/s10973-021-10714-5

Cited by 4 publications

(4 citation statements)

References 34 publications

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“…To provide further evidence for BCL incorporation into ZIFs, we measured FTIR spectroscopy and used fluorescein isothiocyanate (FITC) to label BCL. A distinctive peak around 1650 cm −1 of the internal C�O vibration (amide I band), indicating the presence of BCL, 47 was observed in the spectra of BCL@MAF-6, BCL@ MAF-6-X, and BCL@ZIF-8 compared to original ZIFs (Figure S22). Confocal laser scanning microscopy (CLSM) images showed FITC-labeled BCL uniformly distributed within crystals, confirming its presence inside rather than just on crystal surfaces (Figure S23).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Highly Enantioselective Catalysis by Enzyme Encapsulated in Metal Azolate Frameworks with Micelle-Controlled Pore Sizes

Ren,

Yuan,

et al. 2024

ACS Cent. Sci.

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Encapsulating enzymes within metal−organic frameworks has enhanced their structural stability and interface tunability for catalysis. However, the small apertures of the frameworks restrict their effectiveness to small organic molecules. Herein, we present a green strategy directed by visible linker micelles for the aqueous synthesis of MAF-6 that enables enzymes for the catalytic asymmetric synthesis of chiral molecules. Due to the large pore aperture (7.6 Å), double the aperture size of benchmark ZIF-8 (3.4 Å), MAF-6 allows encapsulated enzyme BCL to access larger substrates and do so faster. Through the optimization of surfactants' effect during synthesis, BCL@MAF-6-SDS (SDS = sodium dodecyl sulfate) displayed a catalytic efficiency (K cat /K m ) that was 420 times greater than that of BCL@ZIF-8. This biocomposite efficiently catalyzed the synthesis of drug precursor molecules with 94−99% enantioselectivity and nearly quantitative yields. These findings represent a deeper understanding of de novo synthetic encapsulation of enzyme in MOFs, thereby unfolding the great potential of enzyme@MAF catalysts for asymmetric synthesis of organics and pharmaceuticals.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Highly Enantioselective Catalysis by Enzyme Encapsulated in Metal Azolate Frameworks with Micelle-Controlled Pore Sizes

Ren,

Yuan,

et al. 2024

ACS Cent. Sci.

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“…[15][16][17] Since PHB is insoluble in organic solvents such as ethanol, methanol, and n-hexane, it is suitable for use in synthesis reactions catalyzed by lipases, for example, the production of ethyl linoleate and ethyl oleate. [18][19][20][21][22] However, PHB is commercialized as a mesoporous powder (particle diameter 75-90 μm) and most authors to date have used this commercial powder directly. [18][19][20][21][22] Unfortunately, this powder is not suitable for application in packed-bed bioreactors, which are often used at large scale.…”

Section: Introductionmentioning

confidence: 99%

“…[18][19][20][21][22] However, PHB is commercialized as a mesoporous powder (particle diameter 75-90 μm) and most authors to date have used this commercial powder directly. [18][19][20][21][22] Unfortunately, this powder is not suitable for application in packed-bed bioreactors, which are often used at large scale. 7 An alternative strategy would be to use the double emulsion solvent evaporation technique (DESE) to produce PHB pellets with controlled size and porosity.…”

Section: Introductionmentioning

confidence: 99%

“…One hydrophobic support that has been used to immobilize lipases by adsorption is poly‐hydroxybutyrate (PHB), a biopolymer produced by microorganisms such as Ralstonia eutropha , Cupriavidus necator , and Bacillus spp 15–17 . Since PHB is insoluble in organic solvents such as ethanol, methanol, and n ‐hexane, it is suitable for use in synthesis reactions catalyzed by lipases, for example, the production of ethyl linoleate and ethyl oleate 18–22 . However, PHB is commercialized as a mesoporous powder (particle diameter 75–90 μm) and most authors to date have used this commercial powder directly 18–22 .…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of the metagenomic lipase, LipG9, on porous pellets of poly‐hydroxybutyrate produced by the double emulsion solvent evaporation technique

Richter

Zawadzki

Santos

et al. 2023

Biotech and App Biochem

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This work aimed to produce porous poly‐hydroxybutyrate (PHB) pellets in order to evaluate the pellets as a support for immobilization of the metagenomic lipase, LipG9. Four types of pelletized PHB particles with different morphological characteristics were obtained using the double emulsion and solvent evaporation technique (DESE). The micropores of these PHB pellets had similar average diameters (about 3 nm), but the pellets had different specific surface areas: 11.7 m2 g−1 for the PHB powder, 8.4 m2 g−1 for the control pellets (Ø < 0.5 mm, produced without the pore forming agent), 10.0 m2 g−1 for the small pellets (Ø < 0.5 mm), 9.5 m2 g−1 for the medium pellets (0.5 < Ø < 0.8 mm) and 8.4 m2 g−1 for the large pellets (Ø > 1.4 mm). Purified LipG9 was immobilized by adsorption on these pellets, and the results were compared with those obtained with PHB powder. The highest immobilization yield (83%) was obtained for the medium PHB pellets, followed by large (76%) and small (55%) PHB pellets. The activity of LipG9 immobilized on the pellets, for the synthesis of ethyl oleate in n‐hexane, was highest for the medium pellets (22 U g−1). The immobilization yield was high for PHB powder (99%) but the esterification activity was slightly lower (20 U g−1). These results show that pelletized PHB beads can be used for the immobilization of lipases, with the advantage that pelletized PHB will perform better than PHB powder in large‐scale enzyme bioreactors.

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Graphene Oxide Enabled Colorimetric Detection of Triglyceride

Iyer,

Baradia,

Chattopadhyay

2024

BioNanoSci.

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Physical adsorption used to the immobilization of Burkholderia cepacia lipase into powder polymeric supports

Cited by 4 publications

References 34 publications

Highly Enantioselective Catalysis by Enzyme Encapsulated in Metal Azolate Frameworks with Micelle-Controlled Pore Sizes

Highly Enantioselective Catalysis by Enzyme Encapsulated in Metal Azolate Frameworks with Micelle-Controlled Pore Sizes

Immobilization of the metagenomic lipase, LipG9, on porous pellets of poly‐hydroxybutyrate produced by the double emulsion solvent evaporation technique

Graphene Oxide Enabled Colorimetric Detection of Triglyceride

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