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Calorimetric analysis of the interaction between trypsin and EUDRAGIT® L100.-
BRAIA, MAURICIO; TUBIO, GISELA; NERLI, BIBIANA; LOH, WATSON; ROMANINI, DIANA
Congreso; 22th International Conference on Chemical Thermodynamics and the 67th Calorimetry Conference; 2012
International Association for Chemical Thermodynamics
Trypsin (TRP) is a serin-protease with a molecular weight of 23 kDa and a pI close to 11. It is widely used in the food and pharmaceutical industries and in molecular biology. Eudragit® L100 (EL100) is a synthetic flexible-chain polymer with a molecular weight of 135 kDa. It has ionizable acrylic groups that are negatively charged at high values of pH. It is widely use in the pharmaceutical industry to coat drugs for oral-delivery formulations. At pH 5.00, TRP has a positive density of charges and EL100 has negative charges. Both molecules interact at pH 5.00 to form insoluble protein-polymer complexes. Since these complexes can be used for industrial and scientific purposes, it is very important to know the mechanism of interaction between TRP and EL100, and the structural stability of the enzyme. ITC experiments were performed at pH 5.00 in order to study the formation of the insoluble complex. DSC experiments allowed determining the thermal stability of the enzyme at pH 5.00 in absence and presence of EL100.