摘要
Objective: In the present work, we have extended the study and immobilized the metalloprotease enzyme in glutaraldehyde cross-linked chitosan nanogels to scrutinize the enzyme's features including stability over its soluble free form. Method: The immobilized metalloprotease was characterized using scanning electron microscopy (SEM), followed by Fourier transform infrared (FTIR) spectroscopy. The enzyme is optimally active at 50 degrees C and pH range of 8.0-10. Results: Thermal stability of the enzyme enhanced when immobilized on the nanogel. After 5 min of incubation at 50 degrees C, immobilized enzymes retained 60% of their original activity, while negligible activity (23%) was observed in the case of the free enzyme. Conclusion: The results obtained here provide a powerful demonstration of the benefits of taking the glutaraldehyde cross-linked chitosan matrices to enhance metalloprotease stability. The high stability of the immobilized enzyme serves to improve its performance for possible application on the industrial scale.
- 出版日期2016-12