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Comprehensive Study of Serratia Peptidase Immobilization From Serratia Sp. Zf03 Onto Chitosan Nanogels; [Serratia Sp. Zf03 Kaynakli Serratia Peptidaz’In Kitosan Nanojellerin Uzerine Immobilziasyonunun Kapsamli Incelenmesi] Publisher



Salarizadeh N2 ; Hasannia S1 ; Sajedi RH3 ; Lamei N4 ; Mohsenifar A5 ; Noghabi KA5
Authors
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Authors Affiliations
  1. 1. Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Jalal Ale Ahmad Highway, P.O. Box: 14115-111, Tehran, Iran
  2. 2. Department of Biology, Faculty of Science, University of Guilan, Rasht, Iran
  3. 3. Department of Biochemistry, Faculty of Biological sciences, Tarbiat Modares University, Tehran, Iran
  4. 4. Drug Design and Development Research Center, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran

Source: Turkish Journal of Biochemistry Published:2016


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 character ized 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 metallo protease stability. The high stability of the immobilized enzyme serves to improve its performance for possible application on the industrial scale. © 2016 Turkish Biochemistry Society. All rights reserved.