The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (...
It is evident that the preparation of pure pepsin must present very great difficulty to the investig...
The utilization of industrial sunflower meal to produce protein-rich products for the food industry ...
International audienceFood processing affects the structure and chemical state of proteins. In parti...
The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated us...
To obtain detailed information about properties of pepsin in thermal denaturing conditions, polyacr...
Pepsin is generally used in the preparation of F(ab)2 fragments from antibodies. The antibodies that...
A zymogen-derived protein, pepsin, appears to be incapable of folding to the native state without th...
The present work reports the pH-induced conformational changes of pepsin in solution at room tempera...
ABSTRACT: A zymogen-derived protein, pepsin, appears to be incapable of folding to the native state ...
1. Evidence is presented that pepsin is a univalent acid with a value for pK of 6.85 (or a base, wit...
Pepsin is the first protease that food proteins encounter in the digestive tract. However, most of t...
In order to increase understanding of the basis of the stability of the native conformational state ...
The high resistance of Brazil nut 2S albumin, previously identified as an allergen, against proteoly...
AbstractThe thermal stability of lentil lectin in the 5.0–10.0 pH range was studied by high-sensitiv...
The activation process of pepsinogen was followed by the appearance of peptic activity and the confo...
It is evident that the preparation of pure pepsin must present very great difficulty to the investig...
The utilization of industrial sunflower meal to produce protein-rich products for the food industry ...
International audienceFood processing affects the structure and chemical state of proteins. In parti...
The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated us...
To obtain detailed information about properties of pepsin in thermal denaturing conditions, polyacr...
Pepsin is generally used in the preparation of F(ab)2 fragments from antibodies. The antibodies that...
A zymogen-derived protein, pepsin, appears to be incapable of folding to the native state without th...
The present work reports the pH-induced conformational changes of pepsin in solution at room tempera...
ABSTRACT: A zymogen-derived protein, pepsin, appears to be incapable of folding to the native state ...
1. Evidence is presented that pepsin is a univalent acid with a value for pK of 6.85 (or a base, wit...
Pepsin is the first protease that food proteins encounter in the digestive tract. However, most of t...
In order to increase understanding of the basis of the stability of the native conformational state ...
The high resistance of Brazil nut 2S albumin, previously identified as an allergen, against proteoly...
AbstractThe thermal stability of lentil lectin in the 5.0–10.0 pH range was studied by high-sensitiv...
The activation process of pepsinogen was followed by the appearance of peptic activity and the confo...
It is evident that the preparation of pure pepsin must present very great difficulty to the investig...
The utilization of industrial sunflower meal to produce protein-rich products for the food industry ...
International audienceFood processing affects the structure and chemical state of proteins. In parti...