Stabilization of serine proteases by immobilization

Citations of this article
Mendeley users who have this article in their library.
Get full text


Water-insoluble serine proteases derivatives from Acremonium chrysogenum, Bac. subtilis, and trypsin were prepared by immobilizing onto the surface of magnetic chitin and chitosan by adsorption and covalent fixation. Magnetic carriers were prepared by direct posmagnetization with ferrofluid and/or deposition of fine magnetite particles from Fe3+/Fe2+salts mixture. Qualitative and quantitative investigations have been provided with the aid of AAS, IR and Mossbauer spectroscopy, SEM methods. Total iron amount in magnetic products of chitin and/or chitosan depended on the nature of the preparation. The stabilization of trypsin and serine proteases I and II from Acremonium chrysogenum against thermal inactivation and autolysis was achieved by optimization of the immobilization conditions. The pH, thermal and storage stability of the immobilized proteases were higher than those of free ones. © 1998 Elsevier B.V. All rights reserved.




Bendikiene, V., & Juodka, B. (1998). Stabilization of serine proteases by immobilization. Progress in Biotechnology, 15(C), 583–588.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free