Modulation of egg-white lysozyme activity by viscosity intensifier additives

1990 ◽  
Vol 36 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Louis Lamy ◽  
Marie-Odile Portmann ◽  
Mohamed Mathlouthi ◽  
Véronique Lurreta-Garde
1979 ◽  
Vol 25 (3) ◽  
pp. 484-485 ◽  
Author(s):  
N Grossowicz ◽  
M Ariel ◽  
T Weber

Abstract We describe a simple, rapid, sensitive, and highly reproducible assay for lysozyme, with use of concentrated cell suspensions of Micrococcus lysodeikticus in Tris-buffered glycerol/water (40/60 by vol), pH 7.5. Stored at -20 degrees C, the cells' susceptibility to lysozyme remains unaltered over long periods. Almost identical concentration curves were obtained with different aliquots of the same preparation during eight months. Lysozyme activity was reflected in the decrease in absorbance of the reaction mixture after incubation for 15 min at 37 degrees C. Concentrations of egg-white lysozyme as low as 0.02 mg/L can be accurately assayed.


1993 ◽  
Vol 56 (2) ◽  
pp. 153-156 ◽  
Author(s):  
T. S. YANG ◽  
F. E. CUNNINGHAM

The effects of pH, ionic strength (I), and selected antimicrobial substances on the lytic activity of egg white lysozyme over an extended storage period of 30 d were studied by observing the rate of clearing of a cell suspension of Micrococcus lysodeikticus. During prolonged storage, lysozyme activity remained relatively stable at pH 7 and ionic strength <0.10, whereas lower activity (P < 0.05) was observed at pH 9 and ionic strength >0.14. Lysozyme activity was highly stable (i.e., maintained over 90% of lytic activity from day 1 to day 30) in solutions of 1.0% sodium chloride, 100 ppm sodium nitrite, 4.0% ethanol, and 100 ppm butylated hydroxytoluene. Lysozyme activity also was stable (i.e., retained over 80% of lytic activity) in solutions of 0.1% sodium benzoate and 100 ppm butylated hydroxyanisol. The lysozyme activity was relatively stable (i.e., retained over 70% of lytic activity) in Solutions of 0.3% calcium propionate, 0.1% potassium sorbate, and 0.1% propyl paraben. About half (50%) of the lysozyme activity was retained in solution of 0.5% EDTA. Activity was lost when lysozyme was combined with 0.5% lactic acid, 4% acetic acid, and 100 ppm chlorine water.


1995 ◽  
Vol 73 (5-6) ◽  
pp. 307-309 ◽  
Author(s):  
Jean Trudel ◽  
Alain Asselin

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.


1977 ◽  
Vol 75 (4) ◽  
pp. 895-900 ◽  
Author(s):  
J.M. Fernández-Sousa ◽  
J.G. Gavilanes ◽  
A.M. Municio ◽  
R. Rodriguez

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein

1972 ◽  
Vol 247 (9) ◽  
pp. 2905-2916
Author(s):  
Ellen M. Prager ◽  
Norman Arnheim ◽  
George A. Mross ◽  
Allan C. Wilson

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