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1.
RBCF, Rev. bras. ciênc. farm. (Impr.) ; 37(3): 347-353, set.-dez. 2001. graf
Article in English | LILACS | ID: lil-314057

ABSTRACT

Egg albumin and cellulase solutions were used to study the surface protein concentration at an air-water interfaces. It was found that the surface tensions of egg albumin and cellulase solutions were a function of the bulk solution pH and concentration. Both surface tensions of egg albumin and cellulase decrease significantly and linearly when the bulk protein concentration increases. Two lines were employed to fit the surface tensions vs. protein concentrations. The intersection of these two lines could be interpreted as the protein monolayer formed entire the interface. Below the monolayer regime, the interfacial protein concentrantion can be estimated by using the Gibbs' isotherm...


Subject(s)
Albumins , Cellulase , Eggs , Chemical Phenomena , Proteins/metabolism , Electrophoresis , Surface Tension
2.
Rev. farm. bioquim. Univ. Säo Paulo ; 34(2): 101-7, jul.-dez. 1998. graf
Article in English | LILACS | ID: lil-235223

ABSTRACT

Aqueous cellulase solutions were vigorously shaked in a separatory funnel, promoting a partition of the enzyme between the droplets formed and the residual bulk solution. The partition coefficient (K ANTPOT. p) was defined as the ratio of protein concentrations in the droplets and in the residual bulk solution. The K ANTPOT. p depended on both initial pH and cellulase concentration, being markedly favoured by using dilute enzyme solutions (up to 40 mg/L) and initial pH between 2.0 and 3.0


Subject(s)
Cellulase , Enzymes , Proteins , Chemical Fractionation , Hydrogen-Ion Concentration
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