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[Trypsin immobilization on organo-silica surface]
Ukrainskii Biokhimicheskii Zhurnal (1978)
|July 1, 1979
Summary
Enzyme immobilization using cyanuric chloride and maleic anhydride on organo-silica surfaces enhances trypsin stability. Immobilized trypsin exhibits increased thermostability, with a half-life of 40 hours at 55°C.
Area of Science:
- Biochemistry and Materials Science
- Enzyme immobilization techniques
Context:
- Developing robust enzyme immobilization methods is crucial for biocatalysis and diagnostics.
- Organo-silica surfaces offer a versatile platform for enzyme carrier coupling.
Purpose:
- To investigate and compare two methods for immobilizing trypsin on organo-silica surfaces: cyanuric chloride and maleic anhydride.
- To analyze the kinetics of enzyme-carrier coupling and assess the thermal stability of the immobilized enzyme.
Summary:
- Two distinct chemical activation methods, cyanuric chloride and maleic anhydride, were employed to immobilize trypsin onto organo-silica substrates.
- Kinetic analysis at 22°C revealed immobilization times of 70 minutes for cyanuric chloride and 35 minutes for maleic anhydride.
- The resulting immobilized trypsin demonstrated significantly enhanced thermostability compared to its soluble form, maintaining a half-life of approximately 40 hours at 55°C.
Impact:
- This research provides efficient protocols for enzyme immobilization, enhancing enzyme utility in various applications.
- The improved thermal stability of immobilized trypsin opens possibilities for its use in demanding industrial processes and diagnostic assays.
- The findings contribute to the field of biocatalysis by offering stable and reusable enzyme preparations.