Synergistic Contributions of Asparagine 46 and Aspartate 52 to the Catalytic Mechanism of Chicken Egg White Lysozyme†

Biochemistry ◽  
1996 ◽  
Vol 35 (6) ◽  
pp. 1890-1896 ◽  
Author(s):  
Ichiro Matsumura ◽  
Jack F. Kirsch
Keyword(s):  
Catalytic Mechanism ◽  
Egg White ◽  
Chicken Egg ◽  
Egg White Lysozyme

scholarly journals Unconventional effects of long-term storage of microwave-modified chicken egg white lysozyme preparations

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Grzegorz Leśnierowski ◽  
Tianyu Yang ◽  
Renata Cegielska-Radziejewska
Keyword(s):  
Microwave Radiation ◽  
Egg White ◽  
Process Time ◽  
High Quality ◽  
Chicken Egg ◽  
Egg White Lysozyme ◽  
Physicochemical Changes ◽  
Long Term Storage ◽  
Term Storage

AbstractThermal modification is an effective method that induces significant expansion of the antimicrobial properties and other valuable properties of chicken egg white lysozyme. In our latest research, a new innovative method of enzyme modification was developed, in which microwave radiation was used as an energy source to process liquid lysozyme concentrate (LLC). After modification, high-quality preparations were obtained. However, long-term storage in a concentrated form initiated various processes that caused darkening over time and could also lead to other significant changes to their structure and, consequently, to their functional properties. This necessitated multidirectional research to explain this phenomenon. This paper presents the results of research aimed at assessing the physicochemical changes in the properties of microwave-modified lysozyme in the form of a liquid concentrate after long-term storage under refrigeration conditions. The assessment also considered the conditions under the acidity of the modifying medium and the duration of the microwave modification. The analysis showed that the values of the basic parameters determining the quality and usefulness of the modified enzyme significantly improved during long-term storage of the preparations. The greatest changes were observed in the preparations modified for the longest time and in the most acidic environment (process time 260 s, pH 2.0), the number of oligomers under these conditions increased by 18% after 12 months of holding, and the surface hydrophobicity increased by as much as 31%. In addition, microbiological tests showed that the preparations of microwave-modified lysozyme had an effect on gram-positive bacteria as well as on gram-negative, and this effect was significantly enhanced after 12 months. The results confirm that LLC modification with microwave radiation is a highly efficient method to prepare high-quality and high utility potential lysozyme. Notably, an interesting and important phenomenon was the observation of the unconventional behaviour of the preparations during their long-term storage, which increased their utility potential significantly.

The effect of solution thermal history on chicken egg white lysozyme nucleation

2001 ◽  
Vol 232 (1-4) ◽  
pp. 301-307 ◽  
Author(s):  
Michael W. Burke ◽  
Russell A. Judge ◽  
Marc L. Pusey
Keyword(s):  
Thermal History ◽  
Egg White ◽  
Chicken Egg ◽  
Egg White Lysozyme

Crystallization of chicken egg white lysozyme from assorted sulfate salts

1999 ◽  
Vol 196 (2-4) ◽  
pp. 332-343 ◽  
Author(s):  
Elizabeth L Forsythe ◽  
Edward H. Snell ◽  
Christine C Malone ◽  
Marc L Pusey
Keyword(s):  
Egg White ◽  
Chicken Egg ◽  
Egg White Lysozyme ◽  
Sulfate Salts

Modulation of the catalytic mechanism of hen egg white lysozyme (HEWL) by photochromism of azobenzene

2005 ◽  
Vol 175 (2-3) ◽  
pp. 100-107 ◽  
Author(s):  
Taeko Inada ◽  
Takashi Terabayashi ◽  
Yoshiki Yamaguchi ◽  
Koichi Kato ◽  
Koichi Kikuchi
Keyword(s):  
Catalytic Mechanism ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Expression of chicken egg white lysozyme by Saccharomyces cerevisiae

Gene ◽  
1985 ◽  
Vol 40 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Jacques Oberto ◽  
John Davison
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Egg White ◽  
Chicken Egg ◽  
Egg White Lysozyme

scholarly journals Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme.

1989 ◽  
Vol 86 (1) ◽  
pp. 133-137 ◽  
Author(s):  
B. A. Malcolm ◽  
S. Rosenberg ◽  
M. J. Corey ◽  
J. S. Allen ◽  
A. de Baetselier ◽  
...  
Keyword(s):  
Egg White ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Catalytic Residues ◽  
Chicken Egg ◽  
Egg White Lysozyme
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