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This dissertation by Linda Helmfors investigates the dual role of lysozyme, a protein found in bodily fluids, as both a protective agent and a contributor to disease. Using a Drosophila melanogaster model, the research explores lysozyme's involvement in amyloidosis and its potential impact on Alzheimer's disease (AD). The study highlights how lysozyme mutations lead to protein misfolding and aggregation, contributing to systemic amyloidosis. Additionally, the research examines the interaction between lysozyme and amyloid β peptide, revealing lysozyme's protective role against AD-related neurotoxicity. The work also studies the role of serum amyloid P component (SAP) in amyloid diseases, suggesting it may aid in correct protein folding. This dissertation is aimed at scientists and researchers in the fields of biochemistry, molecular biology, and neurology, offering insights into protein misfolding diseases and potential therapeutic approaches.
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This dissertation by Liza Bergkvist explores the beneficial effects of lysozyme and serum amyloid P component in models of Alzheimer's disease and lysozyme amyloidosis using Drosophila melanogaster as a model organism. The study investigates two protein misfolding diseases: Alzheimer's disease, characterized by amyloid-beta peptide aggregates in the brain, and lysozyme amyloidosis, a hereditary condition leading to organ failure due to protein aggregation. The research demonstrates that lysozyme can mitigate the toxic effects of amyloid-beta in fruit fly models, suggesting its potential as a therapeutic agent for Alzheimer's disease. Additionally, serum amyloid P is shown to reduce toxicity and promote aggregate formation in lysozyme amyloidosis models. This work aims to enhance understanding of protein misfolding and its implications for treatment strategies.
Alzheimer's disease. --- Lysozyme. --- Alzheimer's disease --- Lysozyme
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ADVANCES IN PROTEIN CHEMISTRY VOL 41
Proteins. --- Lysozyme. --- Mucopeptide glucohydrolase --- Muramidase --- Glycosidases --- Proteids --- Biomolecules --- Polypeptides --- Proteomics
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Lysozyme --- Adsorption --- Enzyme activity --- Immobilization --- Cellulose --- Support solide --- Echangeur d'ions --- Avicel rc-591
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Voedselallergieën zijn een groter wordend probleem in de wereld. Het treft twee tot drie procent van de wereldbevolking. Daarom is er nood aan kennis van allergenenoverdracht in de voedingsindustrie. ALLMOD (Allergeen modellering) is een Flanders' Food project waarin de allergeenrisico's in kaart gebracht worden in functie van proces-, product- en installatie-eigenschappen tijdens verdringing en na reiniging. In deze thesis wordt de kruiscontaminatie via productverdringing in gesloten processen voor emulsies en suspensies bestudeerd alsook adhesie van allergenen aan contactmaterialen.De productverdringing werd bestudeerd met behulp van het indicatorallergeen lysozyme. Eerst werd een batch allergeenbevattende emulsie/suspensie door de installatie gestuurd. Dit werd verdrongen door een batch allergeenvrij product. Kruiscontaminatie werd vergeleken tussen emulsie en suspensie met een gelijke viscositeit, emulsie met hoge en lage viscositeit en ook de complexiteit van de installatie werd gevarieerd.De concentratie lysozyme is het hoogst na 4 minuten verdringen bij hoogviskeuze emulsie (15,5 %), dan suspensie (7,3 %) en tenslotte bij laagviskeuze emulsie (1,5 %).Meer onderzoek is nodig om te kijken wanneer het product geen allergische reactie meer kan uitlokken, want dit is na 4 minuten nog steeds het geval. Ook om de invloed van de complexiteit van de installatie te bepalen moet nog verder onderzoek uitgevoerd worden.De adhesie van respectievelijk RVS, teflon, neopreen en HDPE met lysozyme en gliadine in emulsies en suspensies werd getest. Hieruit blijkt dat de adhesie het kleinst is bij HDPE en RVS en het grootst is bij teflon en neopreen.
Adhesie. --- Emulsie. --- Gluten. --- H350-linguïstiek. --- Indicatorallergenen. --- Kruiscontaminatie. --- Lysozyme. --- Productverdringing. --- S190-bedrijfsbeleid. --- S191-marktstudie. --- Suspensie. --- T430-levensmiddelentechnologie. --- Viscositeit.
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Enzymology --- Medical microbiology, virology, parasitology --- Pathological biochemistry --- Muramidase. --- Lysozyme --- -Mucopeptide glucohydrolase --- Muramidase --- Glycosidases --- Leftose --- N-Acetylmuramide Glycanhydrolase --- Glycanhydrolase, N-Acetylmuramide --- N Acetylmuramide Glycanhydrolase --- Congresses --- -Congresses --- Mucopeptide glucohydrolase
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Lactoglobulins --- Egg white --- Enzymes --- Animal protein --- Texture --- chemical reactions --- Temperature. --- Temperature --- pH --- Ion exchange --- Structure moleculaire --- Hen egg white lysozyme --- Hewl --- Bovine beta-lactoglobulin
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577.15 --- 57.083.332 --- Lysozyme --- #abib:almm --- Mucopeptide glucohydrolase --- Muramidase --- Glycosidases --- Enzymes. Catalysts of biological reactions. Enzymology --- Lytic reactions. Bacteriolytic reactions --- 57.083.332 Lytic reactions. Bacteriolytic reactions --- 577.15 Enzymes. Catalysts of biological reactions. Enzymology
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Malaria remains an alarming emergency in developing countries. It is thus urgent to identify any parasite or host molecules that can serve as new affordable markers for early diagnosis of disease complications or as new targets for vector control. In this context, human and mosquito lysozymes are good candidate molecules, as their involvement in malaria has been recently reported by several independent groups. This book reviews the grounded knowledge on malaria etiology and physiopathology, as well as the current approaches for diagnosis, therapy, and vector control. In addition, the emerging evidence on the involvement of human and mosquito lysozymes in malaria from available experimental models and clinical studies is thoroughly discussed, as is the potential use of other antimicrobial peptides against malaria. Intriguingly, the contributors propose that old well-known molecules such as lysozymes might be used as new targets for cost-effective strategies to fight malaria. About the Editor Mauro Prato currently works as an Adjunct Professor of Biochemistry at the University of Torino, Italy. His research activity focuses on the involvement of proteolytic enzymes in malaria. His track-record includes 40 papers published by peer-reviewed journals, 1 book, 7 book chapters, 97 communications in well-established conferences, and 1 patent.
Biomedicine. --- Parasitology. --- Medical Microbiology. --- Immunology. --- Medicine. --- Microbiology. --- Medical parasitology. --- Médecine --- Immunologie --- Microbiologie --- Parasitologie médicale --- Biology --- Health & Biological Sciences --- Microbiology & Immunology --- Lysozyme. --- Mucopeptide glucohydrolase --- Muramidase --- Medical microbiology. --- Glycosidases --- Immunobiology --- Life sciences --- Serology --- Microbial biology --- Microorganisms --- Human beings --- Human parasitology --- Medical sciences --- Parasitology --- Parasitic diseases --- Parasites
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Enzyme-mediated catalysis offers special advantages over chemical methods. First of all, enzymes are considered an environmentally friendly tool as they help to avoid the requirements of toxic chemicals and high energy. In addition, more feasible processes can be accomplished through enzymatic reactions owing to the enzyme’s innate properties related to high substrate specificity and selectivity. For this reason, biotechnological production of a wide range of products, such as alternative fuels and value-added biochemicals, has been commercially applicable with the aid of enzymes, either in isolated form or in the whole-cell system. In particular, enzymatic transformation of low-value but cheap/abundant starting materials (i.g. biomass) into high-value materials can facilitate the circular and sustainable bioeconomy. This Special Issue on “Enzyme Catalysis: Advances, Techniques, and Outlooks” consists of six articles, which address diverse industrially relevant enzymes with applications in foods, detergent, cosmetics, medicine, etc. A robust methodology related to enzyme kinetics is also addressed.
Technology: general issues --- History of engineering & technology --- CYP102A1 --- atorvastatin --- 4-hydroxy atorvastatin --- hydrogen peroxide --- P450 peroxygenase --- NADPH --- enzyme inhibition --- integrated Michaelis–Menten equations --- reaction product inhibition --- two mutually exclusive inhibitors --- protease --- detergent --- surfactant --- cleaning --- glucose isomerase --- xylose isomerase --- high-fructose corn syrup --- HFCS --- bioethanol --- structure --- l-fucose isomerase --- l-fucose --- l-fuculose --- extremophile --- halothermophilic bacteria --- Halothermothrix orenii --- lysozyme --- muramidase --- N-acetylmuramide glycanhydrolase --- human --- N-acetyl-β-d-glucosaminidase --- NAG --- crystal structure --- n/a --- integrated Michaelis-Menten equations
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