期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 90, 期 -, 页码 81-88出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2015.08.056
关键词
Catalase; Nanoparticles; Shear stress; Conformation; Enzymatic activity; Stability
Catalase is a promising therapeutic enzyme; however, it carries risks of inactivation and rapid degradation when it is used in practical bioprocess, such as delivery in vivo. To overcome the issue, we made catalase-only nanoparticles using shear stress alone at a moderate shear rate of 217 s(-1) in a coaxial cylinder flow cell. Properties of nanoparticles, including particle size, polydispersity index and zeta potential, were characterized. The conformational changes of pre- and post-sheared catalase were determined using spectroscopy techniques. The results indicated that the conformational changes of catalase and reduction in ce-helical content caused by shear alone were less significant than that by desolvation method. Catalase-only nanoparticles prepared by single shear retained over 90% of its initial activity when compared with the native catalase. Catalase nanoparticles lost only 20% of the activity when stored in phosphate buffer solution for 72 h at 4 degrees C, whereas native catalase lost 53% under the same condition. Especially, the activity of nanogranulated catalase was decreased only slightly in the simulated intestinal fluid containing alpha-chymotrypsin during 4 h incubation at 37 degrees C, implying that the catalase nanoparticle was more resistant to the degradation of proteases than native catalase molecules. Overall, catalase-only nanoparticles offered a great potential to stabilize enzymes for various pharmaceutical applications. (C) 2015 Elsevier B.V. All rights reserved.
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