Frozen Microemulsions for MAPLE Immobilization of Lipase

Califano, Valeria; Bloisi, F.; Perretta, Gemma; Aronne, Antonio; Ausanio, G.; Costantini, A.; Vicari, L.

doi:10.3390/molecules22122153

Cited by 18 publications

(7 citation statements)

References 58 publications

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“…From the FT-IR spectra, it was shown that BGI9 underwent a strong conformational modification. Amide I and amide II in the spectrum of BGI9 were quite superimposed due to a shift of amide I band towards lower wavenumbers, indicating a high degree of unfolding/aggregation [47]. Instead, BGI2 had amide I and amide II bands in about the same positions and intensity ratio as lyophilized BG, pointing out a smaller modification of the protein conformation.…”

Section: Resultsmentioning

confidence: 92%

“…Amide I band originated mainly from the C=O stretching vibration of the peptide group, whose frequency was influenced by the strength of hydrogen bonds and the dipole-dipole interactions between carboxyl groups along the chain. This band consists of overlapping components representing secondary structure elements [47]. The results of amide I band fitting are reported in Figure 2.…”

Section: Resultsmentioning

confidence: 99%

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Covalent Immobilization of β-Glucosidase into Mesoporous Silica Nanoparticles from Anhydrous Acetone Enhances Its Catalytic Performance

et al. 2020

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An immobilization protocol of a model enzyme into silica nanoparticles was applied. This protocol exploited the use of the bifunctional molecule triethoxysilylpropylisocyanate (TEPI) for covalent binding through a linker of suitable length. The enzyme β-glucosidase (BG) was anchored onto wrinkled silica nanoparticles (WSNs). BG represents a bottleneck in the conversion of lignocellulosic biomass into biofuels through cellulose hydrolysis and fermentation. The key aspect of the procedure was the use of an organic solvent (anhydrous acetone) in which the enzyme was not soluble. This aimed to restrict its conformational changes and thus preserve its native structure. This approach led to a biocatalyst with improved thermal stability, characterized by high immobilization efficiency and yield. It was found that the apparent KM value was about half of that of the free enzyme. The Vmax was about the same than that of the free enzyme. The biocatalyst showed a high operational stability, losing only 30% of its activity after seven reuses.

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Section: Resultsmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Covalent Immobilization of β-Glucosidase into Mesoporous Silica Nanoparticles from Anhydrous Acetone Enhances Its Catalytic Performance

et al. 2020

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“…Seven bands were identified and assigned based on Natalello et al . and Califano et al . Conformational structure of lipase was sensitive to pressure treatments.…”

Section: Resultsmentioning

confidence: 99%

High Pressure Processing of Lipase (Thermomyces lanuginosus): Kinetics and Structure Assessment

Ramos‐de‐la‐Peña

Aguilar

2019

Euro J Lipid Sci & Tech

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Lipases are highly demanded enzymes, used to synthesize high commercial value products in food, pharmaceutical, cosmetic, textile, paper, and detergent industries. The effect of high pressure processing (HPP) on Thermomyces lanuginosus lipase is studied at 0.1, 100, and 300 MPa and 25 °C. Kinetics is assessed after HPP treatment in three sets of time series: 0–25, 51–75, and 101–112 min. Conformational change of lipase is studied by infrared attenuated total reflectance (ATR)–FTIR spectra deconvolution and 1D 1H NMR. Pressure treatment lead to changes in enzymatic activity from 51 to 75 and from 101 to 112 min. Treated enzyme at 300 MPa has the highest activity (≈twofold higher than untreated lipase). Statistical difference in activity (p > 0.05) is not found during the first 25 min. Lipase activity is best described by first‐order model (0–25 min) and zero‐order model (51–75 and 101–112 min). Lipase unfolding is evident at 100 MPa due to an increase of β‐turns and β‐sheet components. Pressurized enzyme at 300 MPa enhances its activity from 51 to 112 min, due to an increase of β‐sheet and α‐helix structures (refolding). These findings impact directly on cost‐effectiveness of lipase catalyzed products manufacture. Practical Applications: Enzyme enhanced activity and stability improves the performance of manufacture processes. Assessment of structure changes of lipase induced by HPP lead to accurate parameter selection to increase stability and profitability of lipase catalyzed products processing. Pressure levels of 100 MPa led to enzyme unfolding, whereas 300 MPa causes improved activity and stability provoked by lipase refolding. Pressure treatment at 300 MPa of Thermomyces lanuginosus lipase is recommended for long term bioprocessing (≥112 min), which require increased activity and stability of the enzyme.

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“…The resulting advantages are also related to the long-term stability of the coated surface. MAPLE is particularly suited for the deposition of organic molecules, polymers and biomolecules [ 22 , 23 , 24 , 25 , 26 ], but it also allows for the fabrication of either inorganic, organic, or hybrid coatings with a high versatility [ 27 , 28 , 29 , 30 ]. Recently, MAPLE techniques have been used also for the preparation of coatings and layered materials based on carbon-based nanomaterials including carbon nanotubes (CNTs) and graphene-related materials (GRMs) [ 30 , 31 , 32 ].…”

Section: Introductionmentioning

confidence: 99%

Coating of Flexible PDMS Substrates through Matrix-Assisted Pulsed Laser Evaporation (MAPLE) with a New-Concept Biocompatible Graphenic Material

et al. 2022

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In this study, matrix-assisted pulsed laser evaporation (MAPLE) was used to deposit graphene-like materials (GL), a new class of biocompatible graphene-related materials (GRMs) obtained from a controlled top-down demolition of a carbon black, on silicone slices to test their potential use as functional coating on invasive medical devices as indwelling urinary catheters. Results indicate that the relevant chemical-physical features of the deposit (controlled by FTIR and AFM) were maintained after MAPLE deposition. After deposition, GL films underwent a biological survey toward target cellular lines (murine fibroblast NIH3T3, human keratinocytes HaCAT and the human cervical adenocarcinoma epithelial-like HeLa). Results indicate that the GL films did not lead to any perturbations in the different biological parameters evaluated. The presented results and the possibility to further functionalize the GL or combine them with other functional materials in a hybrid fashion to assure a tighter adhesion onto the substrate for use in harsh conditions open the door to practical applications of these new-concept medical devices (drug delivery, next generation flexible devices, multifunctional coatings) paving the way to the prevention of nosocomial infections driven by catheterization through antibiotics-free approaches.

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Frozen Microemulsions for MAPLE Immobilization of Lipase

Cited by 18 publications

References 58 publications

Covalent Immobilization of β-Glucosidase into Mesoporous Silica Nanoparticles from Anhydrous Acetone Enhances Its Catalytic Performance

Covalent Immobilization of β-Glucosidase into Mesoporous Silica Nanoparticles from Anhydrous Acetone Enhances Its Catalytic Performance

High Pressure Processing of Lipase (Thermomyces lanuginosus): Kinetics and Structure Assessment

Coating of Flexible PDMS Substrates through Matrix-Assisted Pulsed Laser Evaporation (MAPLE) with a New-Concept Biocompatible Graphenic Material

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