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Stabilization of polydopamine modified silver nanoparticles bound trypsin: Insights on protein hydrolysis
- Siddiqui, Irfanah, Husain, Qayyum
- Colloids and surfaces 2019 v.173 pp. 733-741
- casein, chemical bonding, colloids, enzyme activity, hydrolysis, nanocomposites, nanosilver, ovalbumin, pH, proteolysis, storage temperature, storage time, trypsin
- This study presents an effective method to enhance the proteolytic activity of trypsin by designing a nanobioconjugate of trypsin and polydopamine coated silver nanoparticles (Ag-PDA). Ag-PDA nanocomposite was synthesized and trypsin was covalently attached to this matrix. A multifold enhancement in enzyme activity was observed after conjugation, with an effectiveness factor of η = 5.62. Conjugated trypsin was more stable to extremes of pH and temperature as compared to normal unconjugated version. Unconjugated trypsin retained only 41% of activity after 60 days of storage at 4 °C, whereas the conjugated enzyme preserved 91% of activity. Immobilized trypsin conserved 83% of activity even after its ten repeated uses. It was found that conjugated trypsin required lower incubation periods for complete hydrolysis of casein, BSA & ovalbumin as compared to free enzyme. Contrary to this, even long hours of incubation with free trypsin were unable to completely digest these proteins. The current observations suggest that Ag-PDA conjugated trypsin could be more suitable for efficient hydrolysis of various proteins under industrial environments.