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Relevant bibliographies by topics / Hen egg lysozymes

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Academic literature on the topic 'Hen egg lysozymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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Journal articles on the topic "Hen egg lysozymes"

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 (October 1, 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 potent activity against Acetobacter aceti CIAL-106 and Gluconobacter oxydans CIAL-107 with concentrations required to obtain 50% inhibition of growth (IC50) of 0.089 and 0.013 mg/ml, respectively. This preparation also demonstrated activity against Lactobacillus casei CIAL-52 and Oenococcus oeni CIAL-91 (IC50, 1.37 and 0.45 mg/ml, respectively). The two hydrolysates from native and heat-denatured lysozyme were active against O. oeni CIAL-96 (IC50, 2.77 and 0.3 mg/ml, respectively). The results obtained suggest that thermal and enzymatic treatments increase the antibacterial spectrum of hen egg white lysozyme in relation to oenological microorganisms.

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Shick, Kari A., K. Asish Xavier, Arvind Rajpal, Sandra J. Smith-Gill, and Richard C. Willson. "Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1340, no. 2 (July 1997): 205–14. http://dx.doi.org/10.1016/s0167-4838(97)00035-6.

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3

Smith, S. G., M. Lewis, R. Aschaffenburg, R. E. Fenna, I. A. Wilson, M. Sundaralingam, D. I. Stuart, and D. C. Phillips. "Crystallographic analysis of the three-dimensional structure of baboon α-lactalbumin at low resolution. Homology with lysozyme." Biochemical Journal 242, no. 2 (March 1, 1987): 353–60. http://dx.doi.org/10.1042/bj2420353.

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The crystal structure of baboon alpha-lactalbumin has been determined at 6 A and at 4.5 A (0.6 nm and 0.45 nm) resolution by the method of isomorphous replacement. The principal derivative was prepared by reducing a disulphide bridge in the crystals and inserting a mercury atom. Detailed comparison of the electron-density maps with corresponding maps of hen egg-white lysozyme shows that they are closely similar, with correlation coefficients of 0.57 and 0.44 at 6 A and 4.5 A resolution respectively. This result, in accordance with earlier predictions based upon comparisons of amino-acid sequences, provides further evidence that class C lysozymes and alpha-lactalbumins are homologous proteins and it is in keeping with the hypothesis that the alpha-lactalbumins evolved from a lysozyme precursor.

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MAENAKA, Katsumi, Masaaki MATSUSHIMA, Gota KAWAI, Akinori KIDERA, Kimitsuna WATANABE, Ryota KUROKI, and Izumi KUMAGAI. "Structural and functional effect of Trp-62→Gly and Asp-101→Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes." Biochemical Journal 333, no. 1 (July 1, 1998): 71–76. http://dx.doi.org/10.1042/bj3330071.

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In order to clarify the structural role of subsite B of hen egg-white lysozyme in hydrolytic activity towards a carbohydrate substrate, we analysed the structures of Trp-62 → Gly and Asp-101 → Gly mutant hen lysozymes, which have no side chain at positions 62 or 101, complexed with a substrate analogue, (N-acetyl-d-glucosamine)3 [(GlcNAc)3], using X-ray crystallography. The overall protein structures in the mutant lysozyme complexes were almost identical to those in the wild type. In the crystals of all the mutant complexes, the (GlcNAc)3 molecule, which is an inhibitor of wild-type lysozyme, had no inhibitory effect, but was hydrolysed as a substrate. One of the products, (GlcNAc)2, the reducing end of which is an α-anomer, was bound in an unproductive binding mode, protruding from the active-site cleft, and was able to act as an inhibitor. Hydrolysis of the synthetic substrate by the mutants occurred in a β-anomer-retaining manner, and so the α-anomer product was converted from the β-anomer product. Thus the interactions of Asp-101 and Trp-62 in subsite B are not essential for the catalytic mechanism, but co-operatively enhance the affinity of the substrate in the productive binding mode, other than the inhibitor in the unproductive mode.

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Lieu, Valerie H., Josephine W. Wu, Steven S. S. Wang, and Chia-Hung Wu. "Inhibition of Amyloid Fibrillization of Hen Egg-White Lysozymes by Rifampicin and p-Benzoquinone." Biotechnology Progress 23, no. 3 (September 5, 2008): 698–706. http://dx.doi.org/10.1021/bp060353n.

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Taylor, Edward J., Michael Skjøt, Lars K. Skov, Mikkel Klausen, Leonardo De Maria, Garry P. Gippert, Johan P. Turkenburg, Gideon J. Davies, and Keith S. Wilson. "The C-Type Lysozyme from the upper Gastrointestinal Tract of Opisthocomus hoatzin, the Stinkbird." International Journal of Molecular Sciences 20, no. 22 (November 6, 2019): 5531. http://dx.doi.org/10.3390/ijms20225531.

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Muramidases/lysozymes are important bio-molecules, which cleave the glycan backbone in the peptidoglycan polymer found in bacterial cell walls. The glycoside hydrolase (GH) family 22 C-type lysozyme, from the folivorous bird Opisthocomus hoazin (stinkbird), was expressed in Aspergillus oryzae, and a set of variants was produced. All variants were enzymatically active, including those designed to probe key differences between the Hoatzin enzyme and Hen Egg White lysozyme. Four variants showed improved thermostability at pH 4.7, compared to the wild type. The X-ray structure of the enzyme was determined in the apo form and in complex with chitin oligomers. Bioinformatic analysis of avian GH22 amino acid sequences showed that they separate out into three distinct subgroups (chicken-like birds, sea birds and other birds). The Hoatzin is found in the “other birds” group and we propose that this represents a new cluster of avian upper-gut enzymes.

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Song, Youtao, Hiroyuki Azakami, Mika Hamasu, and Akio Kato. "In vivo glycosylation suppresses the aggregation of amyloidogenic hen egg white lysozymes expressed in yeast." FEBS Letters 491, no. 1-2 (February 20, 2001): 63–66. http://dx.doi.org/10.1016/s0014-5793(01)02151-2.

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Kumagai, I., F. Sunada, S. Takeda, and K. Miura. "Redesign of the substrate-binding site of hen egg white lysozyme based on the molecular evolution of C-type lysozymes." Journal of Biological Chemistry 267, no. 7 (March 1992): 4608–12. http://dx.doi.org/10.1016/s0021-9258(18)42876-1.

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Düring, K. "Differential Patterns of Bacteriolytic Activities in Potato in Comparison to Bacteriophage T4 and Hen Egg White Lysozymes." Journal of Phytopathology 141, no. 2 (June 1994): 159–64. http://dx.doi.org/10.1111/j.1439-0434.1994.tb01457.x.

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Kato, Akio, Shota Tanimoto, Yoshifumi Muraki, Yoshiki Oda, Yuichi Inoue, and Kunihiko Kobayashi. "Relationships between conformational stabilities and surface functional properties of mutant hen egg-white lysozymes constructed by genetic engineering." Journal of Agricultural and Food Chemistry 42, no. 1 (January 1994): 227–30. http://dx.doi.org/10.1021/jf00037a041.

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Dissertations / Theses on the topic "Hen egg lysozymes"

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Ryan, R. P. "Physical and chemical studies of monoclonal antibodies to lysozyme." Thesis, University of Oxford, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235248.

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Barron, Sarah Elizabeth. "Misfolded forms of hen egg white lysozyme." Thesis, University of Glasgow, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.341983.

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Limb, Michael. "Modelling catalysis in hen egg-white lysozyme." Thesis, University of Bristol, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.687436.

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Hen egg-white lysozyme (HEWL), a paradigmatic glycoside hydrolase (GH), is a retaining β-glycosidase catalysing the cleavage of β-glycosidic bonds found in the cell wall of Grampositive bacteria. Despite extensive research, the nature and role of substrate distortion in catalysis is still unclear. Here, MM and QM/MM modelling was performed on a HEWL trisaccharide (NAM-B-β(1→4)-NAG-C-β(1→4)-NAM-D) product complex to investigate distortion and reactivity of the NAM-D ring bound in the -1 site of the enzyme.

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Miti, Tatiana. "Thermodynamic and Kinetic Aspects of Hen Egg White Lysozyme Amyloid Assembly." Scholar Commons, 2017. https://scholarcommons.usf.edu/etd/7425.

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Deposition of protein fibers with a characteristic cross-β sheet structure is the molecular marker associated with human disorders ranging from Alzheimer's disease to type II diabetes and spongiform encephalopathy. Given the large number of non-disease related proteins and peptides that have been shown to form amyloid fibrils in vitro, it has been suggested that amyloid fibril formation represents a generic protein phase transition. In the last two decades it has become clear that the same protein/peptide can assemble into distinct morphologically and structurally amyloid aggregates depending on the solution conditions. Moreover, recent studies have shown that the early stage, oligomeric amyloid assemblies are the main culprit in vivo. We have investigated the amyloid assemblies formed under denaturing conditions for Hen Egg White Lysozyme (HewL) whose human homologue is directly implicated in hereditary non-neuropathic systemic amyloidosis. Our early investigations showed that HewL can aggregate via at least two distinct assembly pathways depending on solution ionic strength at fixed pH, temperature, and protein concentration. By combining Dynamic Light Scattering (DLS), Static Light Scattering (SLS) and Atomic Force Microscopy (AFM) we showed that at low ionic strength, the pathway is characterized by the nucleation and growth of long (several micron), rigid fibrils (RF) via monomers assembly. A second, high ionic strength pathway is characterized by the rapid assembly of monomers into globular oligomers that further polymerize into curvilinear fibrils (aO/CF). At NaCl concentrations above 400 mM, aggregation resulted in precipitate formation. Next, we used Foureir Transform Infrared spectroscopy (FTIR) and an amyloid-specific dye, Thioflavin T (ThT), to show that both RF and (a)O/CF are amyloidogenic species, but they have detectable structural differences. Moreover, we have determined that each assembly pathway has unique SLS, DLS, FTIR and ThT response signatures that help determine the assembly type prior to AFM imaging of aggregates. Taking advantage of the morphological, structural and kinetic signatures for the two distinct HewL amyloid aggregates I mapped out their amyloid aggregates phase diagram spanning over two orders of magnitude in protein concentration and from 50 to 800 mM NaCl in ionic strength. This is the most complete phase diagram for amyloid aggregates of a given protein up to date. The phase diagram has three distinct regions delineated by sharp boundaries. The RF- aO/CF was called Critical Oligomer Concentration, and we commonly refer to “above the COC” as the region were aO/CF are kinetically favored.. In the region of low salt/high protein concentrations, RF were the only amyloid species to nucleate and grow. As both salt and protein concentrations increase, aO/CF become the kinetically favored species, and RF nucleate and grow after several days of incubation. At high protein and high salt concentrations, aO/CF form very fast and eventually lose solubility forming a precipitate (Ppt). Cross-seeding experiments showed that RF is the thermodynamically stable aggregate phase, while the O/CF are the metastable species. Finally, we used the phase diagram to design experiments that would allow us to reveal the RF nucleation mechanism in presence of aO/CF. RF nucleation above the COC can undergo either via internal restructuring of aO/CF (NCC) or through a random coalescence of monomers into a nucleus (NP). The experimental results obtained so far strongly indicate that RF nucleate via NP mechanism both below and above the COC.

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Kapavarapu, Susmita. "Extracellular expression, oxidation and purification of hen egg white lysozyme double mutant (H15S+N77H) /." Connect to resource online, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1197658857.

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Chung, Evonne W. "Protein folding and interactions examined by electrospray ionisation mass spectrometry." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298237.

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Bowman, Anna Louise. "Modelling the mechanism and dynamics of hen egg white lysozyme and glutathione S-transferase." Thesis, University of Bristol, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.411106.

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Susmita, Kapavarapu. "Extracellular Expression, Oxidation and Purification of Hen Egg White Lysozyme Double Mutant (H15S+N77H)." Youngstown State University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1197658857.

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Amoyaw, Charles Duah. "Optimization of the Small Scale Expression of the Mutant Hen Egg White Lysozyme, H15S." Youngstown State University / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1587473897537747.

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Patton, Nichole L. "GENERATION, CLONING, AND SMALL-SCALE EXPRESSION OF SITE-DIRECTED MUTANTS OF HEN EGG WHITE LYSOZYME IN PICHIA PASTORIS." Youngstown State University / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1348846216.

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Books on the topic "Hen egg lysozymes"

1

Castello, Ignasi Velazquez I. Proteins in Vacuo Molecular Dynamics Studies of Hen Egg White Lysozyme Submitted to Unfolding and Relaxation Conditions. Uppsala Universitet, 1999.

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Book chapters on the topic "Hen egg lysozymes"

1

Kato, Akio. "Engineering Hen Egg-White Lysozyme." In Nutraceutical Proteins and Peptides in Health and Disease, 583–602. CRC Press, 2005. http://dx.doi.org/10.1201/9781420028836.ch29.

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Ibrahim, H. R. "Insights into the Structure-Function Relationships of Ovalbumin, Ovotransferrin, and Lysozyme." In Hen Eggs, 37–56. CRC Press, 2018. http://dx.doi.org/10.1201/9780203752081-4.

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Silvetti, Tiziana, Stefano Morandi, Martin Hintersteiner, and Milena Brasca. "Use of Hen Egg White Lysozyme in the Food Industry." In Egg Innovations and Strategies for Improvements, 233–42. Elsevier, 2017. http://dx.doi.org/10.1016/b978-0-12-800879-9.00022-6.

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Kato, A. "The use of genetic engineering to modify protein functionality: molecular design of hen egg white lysozyme using genetic engineering." In Proteins in Food Processing, 352–69. Elsevier, 2004. http://dx.doi.org/10.1533/9781855738379.2.352.

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Helliwell, John, Antoine Schreurs, Loes Kroon-Batenburg, and Simon Tanley. "Cisplatin coordination chemistry determination at hen egg white lysozyme His15 with ligand distances and angles, and their standard uncertainties, and also reporting a split occupancy effect." In Data Review. The University of Manchester, 2016. http://dx.doi.org/10.3927/45371856.

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Conference papers on the topic "Hen egg lysozymes"

1

Shah, Naina K., and Richard D. Ludescher. "Hydration and the internal dynamics of hen egg-white lysozyme." In OE/LASE '92, edited by Joseph R. Lakowicz. SPIE, 1992. http://dx.doi.org/10.1117/12.58212.

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Besar, Bediha, and Kristina Woods. "Picosecond time scale solvent fluctuations and enzymatic regulation in hen egg white lysozyme ligand reactions." In 2011 36th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz 2011). IEEE, 2011. http://dx.doi.org/10.1109/irmmw-thz.2011.6105252.

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Fujiwara, Seiji, Syou Maki, Seiichi Tanaka, Ryunosuke Maekawa, Tomoki Masuda, and Masayuki Hagiwara. "Measurements of thermal conductivity and thermal diffusivity of hen egg-white lysozyme crystals using a short hot wire method." In PROCEEDING OF THE 3RD INTERNATIONAL CONFERENCE OF GLOBAL NETWORK FOR INNOVATIVE TECHNOLOGY 2016 (3RD IGNITE-2016): Advanced Materials for Innovative Technologies. Author(s), 2017. http://dx.doi.org/10.1063/1.4993351.

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Komiya, Atsuki, Shigenao Maruyama, and Shuichi Moriya. "Development of Precise Visualization System for Small Transient Diffusion Field of Protein Using Phase Shifting Interferometer." In ASME/JSME 2007 Thermal Engineering Heat Transfer Summer Conference collocated with the ASME 2007 InterPACK Conference. ASMEDC, 2007. http://dx.doi.org/10.1115/ht2007-32617.

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This paper deals with a development of precise visualization system for mass diffusion field of micro quantity proteins by using phase shifting interferometer. The visualization system developed in this study could solve several measurement difficulties and accomplish quick and precise measurement of mass diffusion coefficient. For the observation of small transient diffusion field, Mach-Zehnder type phase shifting interferometer and small shearing cell were utilized. The designed small shearing cell requires only 10 micro liter solutions to form the transient diffusion field. As a target protein, lysozyme extracted from hen egg white was used. For the avoidance of protein denaturation, the lysozyme was dissolved in universal buffer solution over a wide pH range from pH 4.29 to 8.44. This range corresponds to that of digestive system in human body. Also, to investigate concentration dependency of mass diffusion coefficient, solutions over a wide range of concentration were prepared. The experimental results indicated that the concentration profile in a diffusion field could be detected clearly even though the field of view is smaller than 1.0mm square. The mass diffusion coefficient was derived by an analytical method proposed by authors. This method can derive mass diffusion coefficient as a function of concentration from one measurement datum. From the experimental data, the dependency of pH value of surrounding buffer and that of concentration on diffusion phenomena were discussed.

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