Adsorption of Candida rugosa lipase at water-polymer interface: The case of poly(dl)lactide

Kamel, Gihan; Bordi, F.; Chronopoulou, Laura; Lupi, S.; Palocci, Cleofe; Sennato, Simona; Verdes, P. V.

doi:10.1016/j.susc.2011.07.021

Cited by 9 publications

(3 citation statements)

References 38 publications

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“…binding, aggregation and/or mixing) [47] , [48] , [49] , [50] , [51] , [52] . The thermodynamics of the interaction is usually investigated by depositing at the air-subphase interface premixed mixtures of the peptide with the membrane models, at increasing molar ratios [53] , [54] , [55] , [56] , [57] , [58] , [59] . The surface pressure isotherms provide useful information on the nature of the short-range and long-range interactions between the molecules, especially between lipids and Aβ peptides [59] , [60] .…”

Section: Introductionmentioning

confidence: 99%

Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts

Diociaiuti

Giordani

Kamel

et al. 2016

Biochemistry and Biophysics Reports

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GM1 ganglioside is known to be involved in the amyloid-associated diseases and it is a crucial factor for the assembly of amyloid proteins on lipid-rafts, which are lipid structures located on the synaptic plasma membranes. Due to its slow aggregation rate, we employed salmon calcitonin (sCT) as a suitable probe representative of amyloid proteins, to study the interaction between this class of proteins and a membrane model. Here, we prepared a neuronal membrane model by depositing onto mica two Langmuir-Blodgett films in liquid-condensed phase: the outer monolayer was characterized by high content of GM1 (50%) and minority parts of cholesterol and POPC (25–25%), while the inner one by plain POPC. To deeply investigate the interaction of sCT with this model and the role-played by GM1, we prepared the outer leaflet adding sCT at a concentration such that the number of proteins equals that of GM1. Atomic Force Microscopy revealed the occurrence of two distinct kinds of flat surfaces, with globular aggregates localized exclusively on top of the highest one. To unravel the nature of the interaction, we studied by ζ-potential technique liposomes composed as the outer leaflet of the model. Results demonstrated that an electrostatic interaction sCT-GM1 occurred. Finally, to investigate the interaction thermodynamics between sCT and the outer leaflet, Langmuir films as the outer monolayer and containing increasing content of sCT were studied by compression isotherms and Brewster Angle Microscopy experiments. Based on the all body of results we propose an interaction model where GM1 plays a pivotal role.

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Section: Introductionmentioning

confidence: 99%

Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts

Diociaiuti

Giordani

Kamel

et al. 2016

Biochemistry and Biophysics Reports

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“…The biocompatibility of a biomaterial is mainly determined by interface‐triggered interactions with the biological environment. Investigations of ultrathin polymer films at the air–water interface allow studying interactions between polymer monolayers and biomolecules like enzymes in order to elucidate adsorption processes of enzymes at biomaterial surfaces . Additionally, hydrolytic and enzymatic degradation of polymer monolayers can be recorded as a function of type and pH of the degradation medium by Langmuir monolayer degradation (LMD) technique .…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Degradation of Oligo(ε‐caprolactone)s End‐Capped with Phenylboronic Acid Derivatives at the Air–Water Interface

Roßberg

Rottke

Schulz

et al. 2016

Macromol. Rapid Commun.

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The influence of terminal functionalization of oligo(ε-caprolactone)s (OCL) with phenylboronic acid pinacol ester or phenylboronic acid on the enzymatic degradation behavior at the air-water interface is investigated by the Langmuir monolayer degradation technique. While the unsubstituted OCL immediately degrades after injection of the enzyme lipase from Pseudomonas cepacia, enzyme molecules are incorporated into the films based on end-capped OCL before degradation. This incorporation of enzymes does not inhibit or suppress the film degradation, but retards it significantly. A specific binding of lipase to the polymer monolayer allows studying the enzymatic activity of bound proteins and the influence on the degradation process. The functionalization of a macromolecule with phenyl boronic acid groups is an approach to investigate their interactions with diol-containing biomolecules like sugars and to monitor their specified impact on the enzymatic degradation behavior at the air-water interface.

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“…Therapeutic applications are also foreseen, such as the use of enzymes in extra-corporeal shunts [6] Lipases can be immobilized on various supports by physical adsorption, covalent binding, ionic interactions or by entrapment [7]. Lipase of Candida rugosa was adsorbed on different types of supports including synthetic or natural polymers [8][9][10][11], bentonite [12], kaolin [13], acrylic resins and textile membranes [14], glass beads [15] and magnetic beads [16]. The forces between the support and the enzymes in this method include hydrogen bonding, van der Waals forces and hydrophobic interactions [8].…”

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confidence: 99%

Use of mesoporous MnO2 as a support for immobilization of lipase from Candida rugosa

Babaei¹,

Karimi²,

Hejazi³

2014

CI&CEQ

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Article Highlights• We used a new mesoporous carrier for immobilization of lipase from Candida rugosa • The amount of enzyme loading on support was reached to 700 units per 1 g of support • The thermal resistance of the enzyme was enhanced by immobilization • The physical adsorption of enzyme to the support was strong Abstract In this study, immobilization of lipase from Candida rugosa on mesoporous manganese dioxide by adsorption was carried out and the effect of three immobilization variables including temperature, process time and enzyme/support ratio on immobilization efficiency were studied. The characteristics of synthesized MnO 2 and lipase-bound MnO 2 were investigated by scanning electron microscopy (SEM), transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FT-IR) methods. The porous property of the support particles was also studied by X-ray diffraction (XRD) and Brunauer, Emmett and Teller (BET) measurements. The thermal stability of immobilized lipase was determined to be better than that of free enzyme. Also the operational stability of lipase-bound MnO 2 was studied and showed an almost strong attachment of enzyme to support. The Michaelis-Menten kinetic parameters (K m and V max ) were also determined for both free and immobilized lipases. It was observed that there is an increase of the K m value (672.96 mg/ml) and a decrease of the V max value (130.99 U/mg) for the immobilized enzyme comparing with the corresponding values of the free lipase.

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Adsorption of Candida rugosa lipase at water-polymer interface: The case of poly(dl)lactide

Cited by 9 publications

References 38 publications

Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts

Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts

Enzymatic Degradation of Oligo(ε‐caprolactone)s End‐Capped with Phenylboronic Acid Derivatives at the Air–Water Interface

Use of mesoporous MnO2 as a support for immobilization of lipase from Candida rugosa

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