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Journal articles on the topic 'Hen egg lysozymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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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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2

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Ose, T., K. Kuroki, M. Matsushima, K. Maenaka, and I. Kumagai. "Importance of the Hydrogen Bonding Network Including Asp52 for Catalysis, as Revealed by Asn59 Mutant Hen Egg-white Lysozymes." Journal of Biochemistry 146, no. 5 (July 15, 2009): 651–57. http://dx.doi.org/10.1093/jb/mvp110.

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12

HARADA, Akihito, Hiroshi YAGI, Akira SAITO, Hiroyuki AZAKAMI, and Akio KATO. "Relationship between the Stability of Hen Egg-White Lysozymes Mutated at Sites Designed to Interact with α-Helix Dipoles and Their Secretion Amounts in Yeast." Bioscience, Biotechnology, and Biochemistry 71, no. 12 (December 23, 2007): 2952–61. http://dx.doi.org/10.1271/bbb.70354.

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13

Trudel, Jean, and Alain Asselin. "Detection of a glycosylated form of hen egg white lysozyme." Biochemistry and Cell Biology 73, no. 5-6 (May 1, 1995): 307–9. http://dx.doi.org/10.1139/o95-038.

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By assaying lysozyme activity after denaturing polyacrylamide gel electrophoresis of commercial hen egg white lysozyme preparations, minor lysozymal activity was detected as an 18-kDa protein. After electrophoretic purification for microsequencing, the N-terminus sequence of the 18-kDa lysozyme was found to be identical with mature 14.4-kDa hen egg white lysozyme. The 18-kDa hen egg white lysozyme was judged to be glycosylated based on a 3.6-kDa decrease in molecular mass after N-glycosidase F treatment, binding to concanavalin A – Sepharose, and staining with periodate – Schiff's reagent. The minor form corresponded to about 0.3% of lyzozyme molecules.Key words: lysozyme, glycosylation, sequential PAGE, N-terminus microsequencing.

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14

Dekina, S. S. "ISOLATION AND PURIFICATION OF LYSOZYME FROM THE HEN EGG WHITE." Biotechnologia Acta 8, no. 6 (2015): 41–47. http://dx.doi.org/10.15407/biotech8.06.041.

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15

Cooke, Delwyn G., and Leonard F. Blackwell. "Clearing of Suspensions of Micrococcus lysodeikticus Catalysed by Lysozymes from Hen, Goose, and Turkey Egg Whites, Human Milk, and Phage T4. Assessment of Potential as Signal Generators for Homogeneous Enzyme Immunoassays for Urinary Steroids." Journal of Immunoassay and Immunochemistry 28, no. 2 (March 22, 2007): 67–90. http://dx.doi.org/10.1080/15321810701209704.

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16

Kang, Hee-Kap, Yun Jo Chung, Chung Ung Park, Yong-Suk Jang, and Byung S. Kim. "Induction of autoimmunity by immunization with hapten-modified hen egg lysozyme in hen egg lysozyme-transgenic mice." Immunology 117, no. 3 (March 2006): 368–78. http://dx.doi.org/10.1111/j.1365-2567.2005.02310.x.

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17

Young, Aideen C. M., Robert F. Tilton, and John C. Dewan. "Thermal expansion of hen egg-white lysozyme." Journal of Molecular Biology 235, no. 1 (January 1994): 302–17. http://dx.doi.org/10.1016/s0022-2836(05)80034-8.

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18

Williams, M. A., J. M. Thornton, and J. M. Goodfellow. "Modelling protein unfolding: hen egg-white lysozyme." Protein Engineering Design and Selection 10, no. 8 (August 1, 1997): 895–903. http://dx.doi.org/10.1093/protein/10.8.895.

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19

CHOU, SHU-TING, and BEEN-HUANG CHIANG. "Reversed Micellar Extraction of Hen Egg Lysozyme." Journal of Food Science 63, no. 3 (May 1998): 399–402. http://dx.doi.org/10.1111/j.1365-2621.1998.tb15751.x.

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20

Howard, Sandra B., Pamela J. Twigg, James K. Baird, and Edward J. Meehan. "The solubility of hen egg-white lysozyme." Journal of Crystal Growth 90, no. 1-3 (July 1988): 94–104. http://dx.doi.org/10.1016/0022-0248(88)90303-x.

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21

Seweryn, Ewa, Emilia Królewicz, Kamilla Stach, and Irena Kustrzeba-Wójcicka. "Nutritional and allergenic properties of hen eggs." Postępy Higieny i Medycyny Doświadczalnej 72 (April 6, 2018): 205–14. http://dx.doi.org/10.5604/01.3001.0011.7339.

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Chicken eggs, along with cow milk, are the most important source of proteins and other valuable nutrients that are introduced to a baby`s diet. Certain components of eggs, besides nutritional, also have other biological functions. Both proteins, phospholipids or carotenoids, are bioactive components which affect the physiological processes in the human body. Regular consumption of chicken eggs rich in substances with antibacterial, anti-inflammatory, immunomodulatory and antioxidant properties may contribute to reducing the incidence of certain lifestyle diseases. Ovomucoid, as a glycoprotein which inhibits bacterial protease, is a component of eggs with bactericidal properties. Similarly, the ovotransferrin protein has a bacteriostatic effect on the Escherichia coli strain or Streptococcus mutans. Due to the strong antioxidant properties, phospholipids, vitamin E and folic acid are extremely valuable egg components. It is believed that the high antioxidant potential of these compounds is important in preventing the development of atherosclerosis and other metabolic syndromes. It is also worth mentioning lutein and zeaxanthin, which are dyes that form a protective barrier against the degeneration of the macula of the human eye. An extremely important function for the human immune system is also met by lysozyme, which stimulates the synthesis of interferon, stimulating the immune response. Unfortunately, hypersensitivity to chicken eggs is one of the most common food allergies in children and affects 0.5-9% of the population. The major egg allergens (Gallus spp.): ovomucoid (Gal d 1), ovalbumin (Gal d 2), conalbumin (Gal d 3) and lysozyme (Gal d 4) are present in egg white and most often cause allergic reactions in children. Minor allergens: serum albumin (Gal d 5) and YGP42 protein (Gal d 6) are found in the egg yolk and are more likely to sensitize adults.

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22

Younvanich, Saronya, and B. Mark Britt. "The Stability Curve of Hen Egg White Lysozyme." Protein & Peptide Letters 13, no. 8 (August 1, 2006): 769–72. http://dx.doi.org/10.2174/092986606777841163.

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23

Nakamura, S., H. Takasaki, K. Kobayashi, and A. Kato. "Hyperglycosylation of hen egg white lysozyme in yeast." Journal of Biological Chemistry 268, no. 17 (June 1993): 12706–12. http://dx.doi.org/10.1016/s0021-9258(18)31445-5.

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24

Lai, Bing, Aoneng Cao, and Luhua Lai. "Organic cosolvents and hen egg white lysozyme folding." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1543, no. 1 (November 2000): 115–22. http://dx.doi.org/10.1016/s0167-4838(00)00189-8.

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25

Heijna, Maurits C. R., Mirjam J. Theelen, Willem J. P. van Enckevort, and Elias Vlieg. "Spherulitic Growth of Hen Egg-White Lysozyme Crystals." Journal of Physical Chemistry B 111, no. 7 (February 2007): 1567–73. http://dx.doi.org/10.1021/jp0643294.

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26

TANAKA, Ryoichi, Matsujiro ISHIBASHI, Hiroko TOKUNAGA, and Masao TOKUNAGA. "Secretion of Hen Egg White Lysozyme fromKluyveromyces lactis." Bioscience, Biotechnology, and Biochemistry 64, no. 12 (January 2000): 2716–18. http://dx.doi.org/10.1271/bbb.64.2716.

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27

Sterpone, Fabio, Matteo Ceccarelli, and Massimo Marchi. "Dynamics of hydration in hen egg white lysozyme." Journal of Molecular Biology 311, no. 2 (August 2001): 409–19. http://dx.doi.org/10.1006/jmbi.2001.4860.

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28

He, Jianwei, Yu Wang, Alan K. Chang, Linan Xu, Na Wang, Xiaoying Chong, Hui Li, Bing Zhang, Gary W. Jones, and Youtao Song. "Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme." Journal of Agricultural and Food Chemistry 62, no. 39 (September 18, 2014): 9442–49. http://dx.doi.org/10.1021/jf5025449.

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29

Voets, Ilja K., Willemberg A. Cruz, Christian Moitzi, Peter Lindner, Elizabeth P. G. Arêas, and Peter Schurtenberger. "DMSO-Induced Denaturation of Hen Egg White Lysozyme." Journal of Physical Chemistry B 114, no. 36 (September 16, 2010): 11875–83. http://dx.doi.org/10.1021/jp103515b.

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30

Schall, Constance A., Edward Arnold, and John M. Wiencek. "Enthalpy of crystallization of hen egg-white lysozyme." Journal of Crystal Growth 165, no. 3 (August 1996): 293–98. http://dx.doi.org/10.1016/0022-0248(96)00180-7.

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31

BARTIK, Kristin, Christopher M. DOBSON, and Christina REDFIELD. "1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme." European Journal of Biochemistry 215, no. 2 (July 1993): 255–66. http://dx.doi.org/10.1111/j.1432-1033.1993.tb18030.x.

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32

Arnaudov, Luben N., and Renko de Vries. "Thermally Induced Fibrillar Aggregation of Hen Egg White Lysozyme." Biophysical Journal 88, no. 1 (January 2005): 515–26. http://dx.doi.org/10.1529/biophysj.104.048819.

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33

RAUCH, PAVEL, IGOR HOCHEL, and JAN KÁš. "Sandwich Enzyme Immunoassay of Hen Egg Lysozyme in Foods." Journal of Food Science 55, no. 1 (January 1990): 103–5. http://dx.doi.org/10.1111/j.1365-2621.1990.tb06027.x.

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34

Thomas, B. R., P. G. Vekilov, and F. Rosenberger. "Effects of Microheterogeneity in Hen Egg-White Lysozyme Crystallization." Acta Crystallographica Section D Biological Crystallography 54, no. 2 (March 1, 1998): 226–36. http://dx.doi.org/10.1107/s0907444997010676.

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35

Faraggi, M., E. Bettelheim, and M. Weinstein. "Inactivation of hen egg-white lysozyme. The azide radical." Journal de Chimie Physique 94 (1997): 356–64. http://dx.doi.org/10.1051/jcp/1997940356.

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36

Yamada, Hiroyuki, Takayuki Nagae, and Nobuhisa Watanabe. "High-pressure protein crystallography of hen egg-white lysozyme." Acta Crystallographica Section D Biological Crystallography 71, no. 4 (March 26, 2015): 742–53. http://dx.doi.org/10.1107/s1399004715000292.

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Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes a phase transition fromP43212 toP43. Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. For example, water molecules penetrate into an internal cavity neighbouring the active site and induce an alternate conformation of one of the catalytic residues, Glu35. These phenomena have not been detected by conventional X-ray crystal structure analysis and might play an important role in the catalytic activity of HEWL.

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37

Walker, Alice R., Nikhil Baddam, and G. Andrés Cisneros. "Unfolding Pathways of Hen Egg-White Lysozyme in Ethanol." Journal of Physical Chemistry B 123, no. 15 (March 26, 2019): 3267–71. http://dx.doi.org/10.1021/acs.jpcb.9b01694.

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38

Croguennec, Thomas, Françoise Nau, Daniel Molle, Yvon Le Graet, and Gérard Brule. "Iron and citrate interactions with hen egg white lysozyme." Food Chemistry 68, no. 1 (January 2000): 29–35. http://dx.doi.org/10.1016/s0308-8146(99)00147-8.

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39

Svanidze, A. V., H. Huth, S. G. Lushnikov, Seiji Kojima, and C. Schick. "Phase transition in tetragonal hen egg-white lysozyme crystals." Applied Physics Letters 95, no. 26 (December 28, 2009): 263702. http://dx.doi.org/10.1063/1.3275858.

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40

Nanev, C. N., and D. Tsekova. "Heterogeneous Nucleation of Hen-Egg-White Lysozyme — Molecular Approach." Crystal Research and Technology 35, no. 2 (February 2000): 189–95. http://dx.doi.org/10.1002/(sici)1521-4079(200002)35:2<189::aid-crat189>3.0.co;2-u.

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41

Rauch, Pavel, Martin Poplstein, Igor Hochel, Ladislav Fukal, Elida Ferri, Carlo Alberto Abagnato, Stefano Girotti, and Aldo Roda. "Enhanced chemiluminescent sandwich enzyme immunoassay for hen egg lysozyme." Journal of Bioluminescence and Chemiluminescence 10, no. 1 (January 1995): 35–40. http://dx.doi.org/10.1002/bio.1170100106.

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42

Huang, Wei, Andreas P. Eichenberger, and Wilfred F. van Gunsteren. "Molecular dynamics simulation of thionated hen egg white lysozyme." Protein Science 21, no. 8 (June 25, 2012): 1153–61. http://dx.doi.org/10.1002/pro.2102.

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43

Lushnikov, S. G., A. V. Svanidze, and I. L. Sashin. "Vibrational density of states of hen egg white lysozyme." Journal of Experimental and Theoretical Physics Letters 82, no. 1 (July 2005): 30–33. http://dx.doi.org/10.1134/1.2045334.

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44

Roberts, Ian N., Donald A. MacKenzie, David J. Jeenes, David B. Archer, Sheena E. Radford, Carol V. Robinson, Robin T. Aplin, and Christopher M. Dobson. "Production of15N-labelled hen egg white lysozyme usingAspergillus niger." Biotechnology Letters 14, no. 10 (October 1992): 897–902. http://dx.doi.org/10.1007/bf01020625.

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45

Altobelli, Gioia, and Shankar Subramaniam. "Kinetics of Association of Anti-lysozyme Monoclonal Antibody D44.1 and Hen-Egg Lysozyme." Biophysical Journal 79, no. 6 (December 2000): 2954–65. http://dx.doi.org/10.1016/s0006-3495(00)76532-5.

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46

McAdam, Stephen N., Burkhard Fleckenstein, Ingunn B. Rasmussen, Dietmar G. Schmid, Inger Sandlie, Bjarne Bogen, Nicholas J. Viner, and Ludvig M. Sollid. "T Cell Recognition of the Dominant I-Ak–Restricted Hen Egg Lysozyme Epitope." Journal of Experimental Medicine 193, no. 11 (May 29, 2001): 1239–46. http://dx.doi.org/10.1084/jem.193.11.1239.

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Type-B T cells raised against the immunodominant peptide in hen egg lysozyme (HEL48–62) do not respond to whole lysozyme, and this has been thought to indicate that peptide can bind to l-Ak in different conformations. Here we demonstrate that such T cells recognize a deamidated form of the HEL peptide and not the native peptide. The sequence of the HEL epitope facilitates rapid and spontaneous deamidation when present as a free peptide or within a flexible domain. However, this deamidated epitope is not created within intact lysozyme, most likely because it resides in a highly structured part of the protein. These findings argue against the existence of multiple conformations of the same peptide–MHC complex and have important implications for the design of peptide-based vaccines. Furthermore, as the type-B T cells are known to selectively evade induction of tolerance when HEL is expressed as a transgene, these results suggest that recognition of posttranslationally modified self-antigen may play a role in autoimmunity.

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47

Yang, Tianyu, and Grzegorz Leśnierowski. "Thermal modification of hen egg white lysozyme using microwave treatment." Acta Scientiarum Polonorum Technologia Alimentaria 19, no. 2 (June 30, 2020): 149–57. http://dx.doi.org/10.17306/j.afs.0773.

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48

NIIMURA, Nobuo, Kazuo KURIHARA, and Mitsuo ATAKA. "Dissolution Rate of Hen Egg-White Lysozyme Crystal Under Microgravity." Biological Sciences in Space 15, Suppl (2001): S176. http://dx.doi.org/10.2187/bss.15.s176.

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49

A. Awad, Dina,, Hamdi, A. Mohammed, Adham, M. Abdou, and Sobhy, A. El Sohaimy. "Separation the Potent Antibacterial Peptides from Hydrolyzed Hen Egg Lysozyme." Benha Veterinary Medical Journal 35, no. 2 (December 1, 2018): 142–49. http://dx.doi.org/10.21608/bvmj.2018.95996.

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50

Awad, Dina, A., Hamdi, A. Mohammed, Adham, M. Abdou, and Sobhy, A. El Sohaimy. "Potent Antibacterial Peptides from Enzymatically Hydrolyzed Hen Egg White Lysozyme." Benha Veterinary Medical Journal 35, no. 2 (December 1, 2018): 150–56. http://dx.doi.org/10.21608/bvmj.2018.96127.

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