Abstract
Abstract 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°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°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.
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