Enzymes immobilized in Langmuir-Blodgett films: Why determining the surface properties in Langmuir monolayer is important?

Caseli, Luciano

doi:10.1590/0001-3765201720170453

Cited by 30 publications

(19 citation statements)

References 74 publications

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“…Caseli et al. reported a condensed state compressibility modulus of 25.1 mN/m for an L–B film of alkaline phosphatase, , and De Zotti et al , reported a maximum compressibility modulus of 40 mN/m for an L–B film of a peptide, similar to that which we observe. The low-compressibility modulus has been associated with possible conformational changes within the L–B film or eruption/desorption of the peptide at the interphase …”

Section: Resultssupporting

confidence: 88%

Aligned Assembly in a 2-D Gel of a Water-Soluble Peptide

et al. 2020

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We demonstrate the assembly of a compact, gel-like Langmuir−Blodgett film of rods formed by self-assembly of a βsheet-forming water-soluble peptide, Ac-IKHLSVN-NH 2 , at the surface of aqueous electrolytes. We characterize surface pressure hysteresis and demonstrate shear stiffening of the surface caused by area cycling, which we interpret as due to rearrangement and alignment of the rods. We show strong effects of the electrolyte on the assembly of the elementary rods, which can be related to the Hofmeister series and interpreted by effects on the interaction energies mediated by ions and water. Formation of β-sheet structures and assembly of these into surface-segregated semicrystalline gels was strongly promoted by ammonium sulfate electrolyte. With ammonium sulfate electrolyte as subphase for Langmuir−Blodgett film deposition, shear stiffening by surface area cycling resulted in very compact films on transfer to a substrate.

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Section: Resultssupporting

confidence: 88%

Aligned Assembly in a 2-D Gel of a Water-Soluble Peptide

et al. 2020

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“…Possarle et al [91] managed to insert carbon nanotubes (CNT) in Langmuir-Blodgett (LB) films of stearic acid (SA), which work as supports for ASNase confinement. The LB technique enables the preparation of ultrathin layers, whose bioinspired support provided by the lipid at air-water interfaces is useful for confinement of enzymes since it allows them to maintain its secondary and tertiary structures [141,142]. After 30 days, the SA-ASNase-CNT monolayer and SA-ASNase In recent years, calcium alginate has stood out as a confinement support material due to its physicochemical features in gel form, essential in the entrapped biologically active material reactions outcome [133].…”

Section: Asnase Confinement By Entrapmentmentioning

confidence: 99%

Recent Strategies and Applications for l-Asparaginase Confinement

et al. 2020

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l-asparaginase (ASNase, EC 3.5.1.1) is an aminohydrolase enzyme with important uses in the therapeutic/pharmaceutical and food industries. Its main applications are as an anticancer drug, mostly for acute lymphoblastic leukaemia (ALL) treatment, and in acrylamide reduction when starch-rich foods are cooked at temperatures above 100 °C. Its use as a biosensor for asparagine in both industries has also been reported. However, there are certain challenges associated with ASNase applications. Depending on the ASNase source, the major challenges of its pharmaceutical application are the hypersensitivity reactions that it causes in ALL patients and its short half-life and fast plasma clearance in the blood system by native proteases. In addition, ASNase is generally unstable and it is a thermolabile enzyme, which also hinders its application in the food sector. These drawbacks have been overcome by the ASNase confinement in different (nano)materials through distinct techniques, such as physical adsorption, covalent attachment and entrapment. Overall, this review describes the most recent strategies reported for ASNase confinement in numerous (nano)materials, highlighting its improved properties, especially specificity, half-life enhancement and thermal and operational stability improvement, allowing its reuse, increased proteolysis resistance and immunogenicity elimination. The most recent applications of confined ASNase in nanomaterials are reviewed for the first time, simultaneously providing prospects in the described fields of application.

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“…The incorporation of enzymes in solid films using casting, spin-coating, electrodeposition and methods providing organized molecular architectures, e.g., Langmuir-Blodgett (LB) (Blodgett 1935) and layer-by-layer (LbL) (Decher et al 1992), is useful for various applications, including biosensing (Crespilho et al 2006, Leontidis 2016, Moriizumi 1988. Of particular relevance is the LB immobilization of proteins in lipid matrices (Carralero Sanz et al 2005, Vidal et al 2006, which offer a suitable environment for the proteins to retain their activity (Caseli 2018).…”

Section: Introductionmentioning

confidence: 99%

Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films

Pereira

Maximino

Martin

et al. 2021

An. Acad. Bras. Ciênc.

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The immobilization of the enzyme tyrosinase (Tyr) in lipid matrices can be explored to produce biosensors for detecting polyphenols, which is relevant for the food industry. Herein, we shall demonstrate the importance of the lipid composition to immobilize the enzyme tyrosinase in Langmuir-Blodgett (LB) fi lms. Tyr could be incorporated into Langmuir monolayers of arachidic acid (AA), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (sodium salt) (DPPG), having as the main effect an expansion in the monolayers. Results from polarization-modulated infrared refl ection-absorption spectroscopy (PM-IRRAS) pointed to electrostatic interactions between the charged residues of Try and the lipid headgroups, in addition to changes in the order of lipid chains. The interaction between Tyr and DPPC in Langmuir monolayers can be correlated with the superior performance of DPPC/Tyr LB fi lms used as biosensors to detect catechol by cyclic voltammetry. The molecular-level interactions assessed via PM-IRRAS are therefore believed to drive an immobilization process for Tyr in the lipid LB matrix and may serve as a general criterion to identify matrices that preserve enzyme activity.

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Enzymes immobilized in Langmuir-Blodgett films: Why determining the surface properties in Langmuir monolayer is important?

Cited by 30 publications

References 74 publications

Aligned Assembly in a 2-D Gel of a Water-Soluble Peptide

Aligned Assembly in a 2-D Gel of a Water-Soluble Peptide

Recent Strategies and Applications for l-Asparaginase Confinement

Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films

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