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Lysozyme Solution (lysozyme + solution)

Distribution by Scientific Domains

Chemistry	42%
Polymers and Materials Science	28%

Selected Abstracts

Effects of chitosan solution concentration and incorporation of chitin and glycerol on dense chitosan membrane properties

JOURNAL OF BIOMEDICAL MATERIALS RESEARCH, Issue 2 2007
Paula Rulf Marreco Dallan
Abstract The aim of this work was to perform a systematic study about the effects induced by chitosan solution concentration and by chitin or glycerol incorporation on dense chitosan membranes with potential use as burn dressings. The membrane properties analyzed were total raw material cost, thickness, morphology, swelling ratio, tensile strength, percentage of strain at break, crystallinity, in vitro enzymatic degradation with lysozyme, and in vitro Vero cells adhesion. While the use of the most concentrated chitosan solution (2.5% w/w) increased membrane cost, it also improved the biomaterial mechanical resistance and ductility, as well as reduced membrane degradation when exposed for 2 months to lysozyme. The remaining evaluated properties were not affected by initial chitosan solution concentration. Chitin incorporation, on the other hand, reduced the membranes cost, swelling ratio, mechanical properties, and crystallinity, resulting in thicker biomaterials with irregular surface more easily degradable when exposed to lysozyme. Glycerol incorporation also reduced the membranes cost and crystallinity and increased membranes degradability after exposure to lysozyme. Strong Vero cells adhesion was not observed in any of the tested membrane formulations. The overall results indicate that the majority of the prepared membranes meet the performance requirements of temporary nonbiodegradable burn dressings (e.g. adequate values of mechanical resistance and ductility, low values of in vitro cellular adhesion on their surfaces, low extent of degradation when exposed to lysozyme solution, and high stability in aqueous solutions). © 2006 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2007 [source]

Functional Properties of Antimicrobial Lysozyme-Chitosan Composite Films

JOURNAL OF FOOD SCIENCE, Issue 8 2004
S.-I. Park
ABSTRACT: Lysozyme-chitosan composite films were developed for enhancing the antimicrobial properties of chitosan films. A 10% lysozyme solution was incorporated into 2% chitosan film-forming solution (FFS) at a ratio of 0%, 20%, 60%, and 100% (w lysozyme/w chitosan). Films were prepared by solvent evaporation. Lysozyme release from the film matrix, the antimicrobial activity of films against Escherichia coli and Streptococcus faecalis, and basic film properties were investigated. The lysozyme release proportionally increased with increasing initial concentration of lysozyme in the film matrix, and the amount of released lysozyme was in natural log relationship with time. The films with 60% lysozyme incorporation enhanced the inhibition efficacy of chitosan films against both S. faecalis and E. coli, where 3.8 log cycles reduction in S. faecalis and 2.7 log cycles reduction in E. coli were achieved. Water vapor permeability of the chitosan films was not affected by lysozyme incorporation, whereas the tensile strength and percent elongation values decreased with increased lysozyme concentration. Scanning electron microscopy images revealed that lysozyme was homogeneously distributed throughout the film matrix. This study demonstrated that enhanced antimicrobial activity of lysozyme-chitosan composite films can be achieved by incorporating lysozyme into chitosan, thus broadening their applications in ensuring food quality and safety. [source]

Interactive functional poly(vinylidene fluoride) membranes with modulated lysozyme affinity: a promising class of new interfaces for contactor crystallizers

POLYMER INTERNATIONAL, Issue 12 2009
Annarosa Gugliuzza
Abstract BACKGROUND: One of the challenges of current researches in biotechnological fields is the achievement of regular and increasingly smaller protein crystals for genomics and biocatalyst applications. The membrane contactor-based methodology appears to be a time-effective and economically competitive technology for accomplishing this target. RESULTS: A new class of interactive polymeric interfaces enabling the nucleation of very small protein crystals in a short time through controlling attractive interactions is discussed. Specifically, the role of attractive interfacial forces between a model lysozyme solution and modified poly(vinylidene fluoride) membranes is examined. The insertion of amphiphilic motifs in the fluorinated membranes allows quicker agglomeration of protein crystals at the membrane surface reducing significantly the induction time for protein nucleation. The chemical nature of the modifier permits the modulation of the membrane affinity to the lysozyme, involving polar and non-polar attractive interactions and preserving intrinsic structural features, transport properties and the hydrophobic character of the interfaces, according to the basics of membrane crystallization technology. The formation of critical nuclei is observed after 3 h and micro-sized crystals are formed in less than 24 h. CONCLUSION: The experimental evidence suggests these membranes as a promising class of interactive interfaces that may rapidly bring advances in genomics research. Copyright © 2009 Society of Chemical Industry [source]

Studies of lysozyme binding to histamine as a ligand for hydrophobic charge induction chromatography

BIOTECHNOLOGY PROGRESS, Issue 1 2010
Qing-Hong Shi
Abstract Histamine was immobilized on Sepharose CL-6B (Sepharose) for use as a ligand of hydrophobic charge induction chromatography (HCIC) of proteins. Lysozyme adsorption onto Histamine-Sepharose (HA-S) was studied by adsorption equilibrium and calorimetry to uncover the thermodynamic mechanism of the protein binding. In both the experiments, the influence of salt (ammonium sulfate and sodium sulfate) was examined. Adsorption isotherms showed that HA-S exhibited a high salt tolerance in lysozyme adsorption. This property was well explained by the combined contributions of hydrophobic interaction and aromatic stacking. The isotherms were well fitted to the Langmuir equation, and the equilibrium parameters for lysozyme adsorption were obtained. In addition, thermodynamic parameters (,Hads, ,Sads, and ,Gads) for the adsorption were obtained by isothermal titration calorimetry by titrating lysozyme solutions into the adsorbent suspension. Furthermore, free histamine was titrated into lysozyme solution in the same salt-buffers. Compared with the binding of lysozyme to free histamine, lysozyme adsorption onto HA-S was characterized by a less favorable ,Gads and an unfavorable ,Sads because histamine was covalently attached to Sepharose via a three-carbon-chain spacer. Consequently, the immobilized histamine could only associate with the residues on the protein surface rather than those in the hydrophobic pocket, causing a less favorable orientation between histamine and lysozyme. Further comparison of thermodynamic parameters indicated that the unfavorable ,Sads was offset by a favorable ,Hads, thus exhibiting typical enthalpy-entropy compensation. Moreover, thermodynamic analyses indicated the importance of the dehydration of lysozyme molecule and HA-S during the adsorption and a substantial conformational change of the protein during adsorption. The results have provided clear insights into the adsorption mechanisms of lysozyme onto the new HCIC material. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2010 [source]

[Ru(bpy)2(dcbpy)NHS] Labeling/Aptamer-Based Biosensor for the Detection of Lysozyme by Increasing Sensitivity with Gold Nanoparticle Amplification

CHEMISTRY - AN ASIAN JOURNAL, Issue 11 2008
Jianguo Bai
Abstract A novel [Ru(bpy)2(dcbpy)NHS] labeling/aptamer-based biosensor combined with gold nanoparticle amplification for the determination of lysozyme with an electrochemiluminescence (ECL) method is presented. In this work, an aptamer, an ECL probe, gold nanoparticle amplification, and competition assay are the main protocols employed in ECL detection. With all the protocols used, an original biosensor coupled with an aptamer and [Ru(bpy)2(dcbpy)NHS] has been prepared. Its high selectivity and sensitivity are the main advantages over other traditional [Ru(bpy)3]2+ biosensors. The electrochemical impedance spectroscopy (EIS) and atomic force microscopy (AFM) characterization illustrate that this biosensor is fabricated successfully. Finally, the biosensor was applied to a displacement assay in different concentrations of lysozyme solution, and an ultrasensitive ECL signal was obtained. The ECL intensity decreased proportionally to the lysozyme concentration over the range 1.0×10,13,1.0×10,8,mol,L,1 with a detection limit of 1.0×10,13,mol,L,1. This strategy for the aptasensor opens a rapid, selective, and sensitive route for the detection of lysozyme and potentially other proteins. [source]

Cross-relaxation bottleneck in water,lysozyme proton magnetization exchange

BIOPOLYMERS, Issue 1 2006
J. F. Kakule
Abstract The proton spin-lattice relaxation parameters in natural and deuterated lysozyme solutions have been measured as a function of temperature (0,50°C). The variation of the apparent magnitudes of the water proton magnetizations in the solutions with temperature indicates that magnetic coupling mixes protein and water proton magnetizations. The results are consistent with an exchange cross-relaxation model (Hills, B. P., Mol Phys 1992, 76, 489,508) in which the cross-relaxation acts between the labile and nonlabile protons, rather than between water and protein protons. Although this cross-relaxation pathway clearly affects the observed magnetization fractions in this protein solution, its influence on the relaxation rates is less apparent. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 11,19, 2006 This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source]