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Common carp (Cyprinus carpio) is highly important culturable species in freshwater and cultured throughout the globe. Its farming require formulated feed with balance protein and energy. Most of the time fish meal is used as a protein source, but it is not acceptable from sustainability point of view. The replacement of fish meal by plant based protein source is advised. The limitation of plant based ingredients like soybean meal is the presence of anti-digestive factors in the form of several protease inhibitors. Kunitz type soybean protease inhibitor (SPI) is the most abundant protease inhibitor in soybean meal and it reduces the digestibility of feed. The data regarding molecular interaction and binding affinity of SPI with proteases is available in mammalian organism like pig but in fishes it has not been studied in detail. So the present study was conducted to gain insight into the protein-protein interaction and binding affinity of common carp trypsin (ccTrypsin1) and SPI using computational modelling. The sequence and 3D structure of ccTrypsin1 is highly similar to its mammalian counterpart pig. The protein-protein interaction analysis using knowledge based docking approach showed that the interaction was more or less similar like porcine trysin with SPI. The predicted binding affinity (-9.2 kcal/mol) and dissociation constant (1.9E-0.7) showed strong interaction between the interactor governed by strong attractive forces like electrostatic forces. | Computational interaction analysis of cyprinus Carpio trypsin1 and Kunitz type soybean protease inhibitor
