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Relevant bibliographies by topics / Lysozyme and bacteria

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Journal articles

Academic literature on the topic 'Lysozyme and bacteria'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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Journal articles on the topic "Lysozyme and bacteria"

1

CARRILLO, W., A. GARCÍA-RUIZ, I. RECIO, and M. V. MORENO-ARRIBAS. "Antibacterial Activity of Hen Egg White Lysozyme Modified by Heat and Enzymatic Treatments against Oenological Lactic Acid Bacteria and Acetic Acid Bacteria." Journal of Food Protection 77, no. 10 (2014): 1732–39. http://dx.doi.org/10.4315/0362-028x.jfp-14-009.

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The antimicrobial activity of heat-denatured and hydrolyzed hen egg white lysozyme against oenological lactic acid and acetic acid bacteria was investigated. The lysozyme was denatured by heating, and native and heat-denatured lysozymes were hydrolyzed by pepsin. The lytic activity against Micrococcus lysodeikticus of heat-denatured lysozyme decreased with the temperature of the heat treatment, whereas the hydrolyzed lysozyme had no enzymatic activity. Heat-denatured and hydrolyzed lysozyme preparations showed antimicrobial activity against acetic acid bacteria. Lysozyme heated at 90°C exerted

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2

Ren, Qian, Chunyang Wang, Min Jin, et al. "Co-option of bacteriophage lysozyme genes by bivalve genomes." Open Biology 7, no. 1 (2017): 160285. http://dx.doi.org/10.1098/rsob.160285.

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Eukaryotes have occasionally acquired genetic material through horizontal gene transfer (HGT). However, little is known about the evolutionary and functional significance of such acquisitions. Lysozymes are ubiquitous enzymes that degrade bacterial cell walls. Here, we provide evidence that two subclasses of bivalves (Heterodonta and Palaeoheterodonta) acquired a lysozyme gene via HGT, building on earlier findings. Phylogenetic analyses place the bivalve lysozyme genes within the clade of bacteriophage lysozyme genes, indicating that the bivalves acquired the phage-type lysozyme genes from bac

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3

Huang, Hai, Juan Du, Shang-Wei Li, and Tao Gong. "Identification and Functional Analysis of a Lysozyme Gene from Coridius chinensis (Hemiptera: Dinidoridae)." Biology 10, no. 4 (2021): 330. http://dx.doi.org/10.3390/biology10040330.

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Coridius chinensis is a valuable medicinal insect resource in China. Previous studies have indicated that the antibacterial and anticancer effects of the C. chinensis extract mainly come from the active polypeptides. Lysozyme is an effective immune effector in insect innate immunity and usually has excellent bactericidal effects. There are two kinds of lysozymes in insects, c-type and i-type, which play an important role in innate immunity and intestinal digestion. Studying lysozyme in C. chinensis will be helpful to further explore the evolutionary relationship and functional differences amon

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4

Kusumaningrum, Harsi Dewantari, Syahrizal Nasution, E. Kusumaningtyas, and D. N. Faridah. "Lysozyme from Chicken Egg White as an Antibacterial Agent." Indonesian Bulletin of Animal and Veterinary Sciences 28, no. 4 (2019): 175. http://dx.doi.org/10.14334/wartazoa.v28i4.1882.

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<p class="00-6Abstrak2Wtz">Lysozyme is one of the constituent proteins of chicken egg white that plays an important role in a protection system during the embryo growing process. Lysozyme protection systems can be applied in food and for health. This paper aims to describe the role of egg white lysozyme which has the antibacterial activity to improve food safety and health. Mechanism and activity of lysozyme protection can be explored by understanding the structure of proteins, type of amino acids, and the sequence of amino acids. The mechanism of lysozyme antibacterial activity against

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5

Gabrieli, A., P. Wild, E. M. Schraner, A. Pellegrini, and R. von Fellenberg. "How does lysozyme affect Escherichia coli: questions arising from impact frozen and freeze-substitutet bacteria." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 876–77. http://dx.doi.org/10.1017/s0424820100140750.

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Since the discovery by Fleming in 1922 that lysozyme has the ability to lyse Grampositive bacteria but not Gram-negative bacteria the assumption was established that lysozyme per se cannot affect Gram-negative bacteria. One basis of this assumption is that lysozyme is an enzyme with muramidase activity acting on the peptidoglycan. In E. coli, the peptoglycan layer is protected by the outer membrane, and, thus lysozyme has no access to it unless the outer membrane is destroyed, e.g. by EDTA or complement1. Accidentally, Pellegrini et al. found that lysozyme kills but does not lyse E. coli. Elec

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6

Martinez, Jose G., Michael Waldon, Qiyu Huang, et al. "Membrane-targeted synergistic activity of docosahexaenoic acid and lysozyme against Pseudomonas aeruginosa." Biochemical Journal 419, no. 1 (2009): 193–200. http://dx.doi.org/10.1042/bj20081505.

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Antimicrobial polypeptides, including lysozymes, have membrane perturbing activity and are well-documented effector molecules of innate immunity. In cystic fibrosis, a hereditary disease with frequent lung infection with Pseudomonas aeruginosa, the non-esterified fatty acid DA (docosahexaenoic acid), but not OA (oleic acid), is decreased, and DA supplementation has been shown to improve the clinical condition in these patients. We hypothesized that DA may, either alone or in conjunction with lysozyme, exert antibacterial action against Ps. aeruginosa. We found that DA and lysozyme synergistica

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7

Stenfors, Lars-Eric, Helga-Marie Bye, and Simo Räisänen. "Immunocytochemical localization of lysozyme and lactoferrin attached to surface bacteria of the palatine tonsils during infectious mononucleosis." Journal of Laryngology & Otology 116, no. 4 (2002): 264–68. http://dx.doi.org/10.1258/0022215021910717.

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Bacterial samples were obtained from the tonsillar surfaces of seven patients (four males, three females; median age 18 years, range 15 to 21 years) suffering from acute infectious mononucleosis with concomitant pharyngotonsillitis, and from five healthy controls. By using gold-labelled antiserum to human lysozyme and lactoferrin, micro-organisms on the tonsillar surfaces coated with these antibacterial substances could be identified by tracing the gold particles in the transmission electron microscope. In healthy individuals, most of the bacteria were coated with lysozyme and significantly mo

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8

Salm, Heike, and Klaus Geider. "Dual Activity of a Viral Lysozyme with High Efficiency for Growth Inhibition of Erwinia amylovora." Phytopathology® 94, no. 12 (2004): 1315–22. http://dx.doi.org/10.1094/phyto.2004.94.12.1315.

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The lysozyme from Erwinia amylovora phage ΦEa1h was investigated for its ability to inhibit growth of bacteria and compared with the lysozyme from Escherichia coli phage T4. The assays to measure lysozyme activity included cell lysis and growth inhibition of bacteria. Bacterial strains with kanamycin resistance were not affected by lysates containing the ΦEa1h-enzyme. The titer of Micrococcus luteus but not of Erwinia amylovora was diminished by cell extracts containing T4 lysozyme. In contrast, ΦEa1h lysozyme preferentially inhibited E. amylovora, exceeding the T4 lysozyme activity at least o

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9

Kudo, Shigeharu. "Enzymes responsible for the bactericidal effect in extracts of vitelline and fertilisation envelopes of rainbow trout eggs." Zygote 8, no. 3 (2000): 257–65. http://dx.doi.org/10.1017/s0967199400001052.

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Extracts from both the vitelline envelope (VE) and fertilisation envelopes (FE) of rainbow trout eggs have the ability to exert a bactericidal effect on Gram-positive and -negative bacteria. The effect may be due to the presence of phospholipase D (PLD), lysozyme, proteinase and DNases, as the extracts contain these enzyme activities. The intensity of chorionic PLD and lysozyme activities in the VE extract was maintained in the FE without any alteration in activity even after transformation in the course of the cortical reaction, as components of a fundamental architecture of the envelope. Bot

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10

Teneback, Charlotte C., Thomas C. Scanlon, Matthew J. Wargo, Jenna L. Bement, Karl E. Griswold, and Laurie W. Leclair. "Bioengineered Lysozyme Reduces Bacterial Burden and Inflammation in a Murine Model of Mucoid Pseudomonas aeruginosa Lung Infection." Antimicrobial Agents and Chemotherapy 57, no. 11 (2013): 5559–64. http://dx.doi.org/10.1128/aac.00500-13.

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ABSTRACTThe spread of drug-resistant bacterial pathogens is a growing global concern and has prompted an effort to explore potential adjuvant and alternative therapies derived from nature's repertoire of bactericidal proteins and peptides. In humans, the airway surface liquid layer is a rich source of antibiotics, and lysozyme represents one of the most abundant and effective antimicrobial components of airway secretions. Human lysozyme is active against both Gram-positive and Gram-negative bacteria, acting through several mechanisms, including catalytic degradation of cell wall peptidoglycan

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