Reversible Sodium Dodecyl Sulfate Activation of Latent Peach Polyphenol Oxidase by Cyclodextrins

2000 ◽  
Vol 379 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Francisco Laveda ◽  
Estrella Núñez-Delicado ◽  
Francisco García-Carmona ◽  
Alvaro Sánchez-Ferrer
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Polyphenol Oxidase ◽  
Sodium Dodecyl ◽  
Dodecyl Sulfate ◽  
Sulfate Activation

Differential Activation of a Latent Polyphenol Oxidase Mediated by Sodium Dodecyl Sulfate

2005 ◽  
Vol 53 (17) ◽  
pp. 6825-6830 ◽  
Author(s):  
Fernando Gandía-Herrero ◽  
Mercedes Jiménez-Atiénzar ◽  
Juana Cabanes ◽  
Francisco García-Carmona ◽  
Josefa Escribano
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Polyphenol Oxidase ◽  
Sodium Dodecyl ◽  
Differential Activation ◽  
Dodecyl Sulfate

Evidence for a common regulation in the activation of a polyphenol oxidase by trypsin and sodium dodecyl sulfate

2005 ◽  
Vol 386 (6) ◽  
pp. 601-607 ◽  
Author(s):  
Fernando Gandía-Herrero ◽  
Mercedes Jiménez-Atiénzar ◽  
Juana Cabanes ◽  
Francisco García-Carmona ◽  
Josefa Escribano
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Polyphenol Oxidase ◽  
Sodium Dodecyl ◽  
Kinetic Properties ◽  
Activation Process ◽  
Specific Rate ◽  
Ph Optimum ◽  
Beet Root ◽  
A Value ◽  
Dodecyl Sulfate

Abstract Polyphenol oxidase (PPO) was extracted from beet root, in both soluble and membrane fractions, and in both cases the enzyme was in a latent state. PPO from the membrane fraction showed no diphenolase activity unless it was activated by trypsin or sodium dodecyl sulfate (SDS). The kinetics of the activation process of latent PPO by trypsin was studied and the specific rate constant of active PPO formation, k 3, showed a value of 0.03 s−1. The protease-activated form showed a pH optimum (6.5) and kinetic properties identical to those of the SDS-activated enzyme. Evidence is provided for the existence of a common peptide responsible for the regulation of the activity of the enzyme by both proteolysis and SDS detergent. Formation of the active proteolyzate was followed by spectroscopic measurements, Western blotting and partially denaturing SDS-PAGE.

Solubility and adsorption behaviors of chlorophenols in the presence of surfactant

1997 ◽  
Vol 35 (7) ◽  
pp. 123-130 ◽  
Author(s):  
J. C. Liu ◽  
P. S. Chang
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Critical Micelle Concentration ◽  
Sodium Dodecyl ◽  
Adsorption Behaviors ◽  
Brij 35 ◽  
Important Index ◽  
Dodecyl Sulfate ◽  
Triton X

The solubility of chlorophenols as affected by surfactant was investigated. Three kinds of surfactant, sodium dodecyl sulfate, Triton X-100, and Brij 35, were utilized. The solubilization of chlorophenols by surfactant follows the order of 2,4,6-trichlorophenol > 2,4-dichlorophenol > 2,6-dichlorophenol > 2-chlorophenol; and the critical micelle concentration is an important index. The adsorption reactions of 2,4-dichlorophenol and 2,4,6- trichlorophenol onto hydrous montmorillonite in the presence of surfactant were examined. The presence of surfactant decreased the adsorption of chlorophenols significantly. The roles of hydrophobicity of chlorophenols in solubilization and adsorption behaviors are discussed.

Different submicellar solubilization mechanisms revealed by 1H NMR and 2D diffusion ordered spectroscopy (DOSY)

2020 ◽  
Vol 22 (19) ◽  
pp. 11075-11085
Author(s):  
Mengjian Wu ◽  
Zhaoxia Wu ◽  
Shangwu Ding ◽  
Zhong Chen ◽  
Xiaohong Cui
Keyword(s):  
Nmr Spectroscopy ◽  
Sodium Dodecyl Sulfate ◽  
1H Nmr ◽  
Sodium Dodecyl ◽  
Butyl Methacrylate ◽  
H Nmr ◽  
Molecular Scale ◽  
Two Systems ◽  
Dodecyl Sulfate ◽  
Triton X

Different submicellar solubilization mechanisms of two systems, Triton X-100/tetradecane and sodium dodecyl sulfate (SDS)/butyl methacrylate, are revealed on the molecular scale by 1H NMR spectroscopy and 2D diffusion ordered spectroscopy (DOSY).

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