Human lysozyme and hen egg-white lysozyme have antibacterial, antiviral, and antifungal properties with numerous potential commercial applications. Currently, hen egg-white lysozyme dominates low cost applications but the recent high-level expression of human lysozyme in rice could provide an economical source of lysozyme. This work compares human lysozyme and hen egg-white lysozyme adsorption to the cation exchange resin, SP-Sepharose FF, and the effect of rice extract components on lysozyme purification. With one exception, the dynamic binding capacities of human lysozyme were lower than those of hen egg-white at pH 4.5, 6, and 7.5 with ionic strengths ranging from 0 to 100 mM (5-20 mS). Ionic strength and pH had a similar effect on the adsorption capacities, but human lysozyme was more sensitive to these two factors than hen egg-white lysozyme. In the presence of rice extract, the dynamic binding capacities of human and hen egg-white lysozymes were reduced by 20-30% and by 32-39% at pH 6. Hen egg-white lysozyme was used as a benchmark to compare the effectiveness of human lysozyme purification from transgenic rice extract. Process simulation and cost analyses for human lysozyme purification from rice and hen egg-white lysozyme purification from egg-white resulted in similar unit production costs at 1 ton per year scale.
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http://dx.doi.org/10.1002/btpr.593 | DOI Listing |
Acta Crystallogr F Struct Biol Commun
February 2025
Department of Chemistry `Ugo Schiff', Università degli Studi di Firenze, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy.
Hen egg-white lysozyme (HEWL) is a small polycationic protein which is highly soluble and stable. This has led to it becoming a `molecular laboratory' where chemical biological operations and structural techniques are tested. To date, HEWL accounts for 1233 PDB entries, roughly 0.
View Article and Find Full Text PDFCureus
December 2024
Department of Pediatrics, IMS Group, IMS Memorial Hospital, Tokyo, JPN.
Food protein-induced enterocolitis syndrome (FPIES) is a non-immunoglobulin E (IgE)-mediated food allergy. IgE sensitization to the causative food is often not observed, and the rate of sensitization to other common foods is not exceptionally high. This report discusses the case of a boy being followed up for FPIES due to egg yolk, who developed a buckwheat allergy during the disease.
View Article and Find Full Text PDFAllergy Asthma Clin Immunol
January 2025
Department of Prevention of Environmental Hazards, Allergology and Immunology, Medical University of Warsaw, Zwirki I Wigury 61, 02-097, Warsaw, Poland.
Background: Nasal allergen provocation tests are an important part of the diagnostics of allergic diseases triggered by environmental factors. Recently, increased attention has been paid to the potential use of this method in the diagnosis of food allergy. The objective of the study was to evaluate the usefulness of the nasal allergen provocation test in a group of subjects allergic to hen's egg white allergens.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
KU Leuven: Katholieke Universiteit Leuven, Chemistry, BELGIUM.
Understanding the impact of oxidative modification on protein structure and functions is essential for developing therapeutic strategies to combat macromolecular damage and cell death. However, selectively inducing oxidative modifications in proteins remains challenging. Herein we demonstrate that [V6O13{(OCH2)3CCH2OH}2]2- (V6-OH) hybrid metal-oxo cluster can be used for selective protein oxidative cleavage and modifications.
View Article and Find Full Text PDFBiomolecules
December 2024
Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Prospect 47, 119991 Moscow, Russia.
This study describes the applicability of the fluorescence polarization assay (FPA) based on the use of FITC-labeled oligosaccharide tracers of defined structure for the measurement of active lysozyme in hen egg white. Depending on the oligosaccharide chain length of the tracer, this method detects both the formation of the enzyme-to-tracer complex (because of lectin-like, i.e.
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