Original scientific paper
Preparation and Property of Urease Immobilization with Cationic Poly(4-vinylpyridine) Functionalized Colloidal Particles
J. Zhou
; College of Pharmaceutical Science, and Medical College, Soochow University, Suzhou 215123, P. R. China
J. Cao
; College of Pharmaceutical Science, and Medical College; College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, P. R. China
W. Huang
; College of Pharmaceutical Science, and Medical College; College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, P. R. China
L. Huang
; College of Pharmaceutical Science, and Medical College; College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, P. R. China
Y. Wang
; College of Pharmaceutical Science, and Medical College; College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, P. R. China
S. Zhang
; College of Pharmaceutical Science, and Medical College; College of Chemistry, Chemical Engineering and Materials Science
Y. Yuan
; College of Pharmaceutical Science, and Medical College, Soochow University, Suzhou 215123, P. R. China
D. Hua
; College of Pharmaceutical Science, and Medical College; College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, P. R. China
Abstract
We report here a novel immobilization matrix for high enzyme loading using cationic hairy latex particles. Specifically, poly(4-vinyl-N-ethylpyridine bromide)-functionalized polymeric colloidal particle was used to immobilize urease by its long charged chain structure. The successful immobilization of urease on the cationic hairy colloidal particles was confirmed by Field-emitting scanning electron microscopy (SEM) images, Fourier transform infrared (FT-IR) spectra and zeta potential measurements. Under the optimized conditions of pH = 8.0 and 1.4 mg mL–1 of urease concentration, the enzyme
loading could reach 355 ± 22 mg g–1 support with the activity of 1.486 × 104 ± 169 U g–1 support. The pH and thermal stability of urease was enhanced upon immobilization, and it could retain almost 100 % of its initial activity after repeating the catalysis reaction 10 times. The cationic hairy colloidal particles had not only high protein loading, but also enhanced the stability of enzyme. These properties prompt this type of cationic hairy colloidal particles to be used as a promising matrix for enzyme immobilization.
Keywords
Urease; poly(4-vinylpyridine); colloidal particles; immobilization
Hrčak ID:
112353
URI
Publication date:
19.12.2013.
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