The properties of unmodified crab hepatopancreas proteolytic complex and the complex immobilized on chitosan-containing cellulose substrates were investigated. The kinetics of immobilization and storage of dried preparations was investigated. Three stages of inactivation of the immobilized sample were established: in immobilization, during drying and storage. It was shown that immobilization of the complex on a textile substrate protects enzymes from thermal inactivation in model buffer solutions at different pH.The Scientific-Research Institute of Textile Materials is manufacturing various biologically active substances (BAS), including enzymes immobilized on insoluble textile substrates, on the industrial scale. These materials are used for medical purposes as applications, lints, or powders, as dressings for treating purulent and necrotic, burn, and other wounds [1].Incorporation of hydrocarbons in the structure of drugs significantly reduces their harmful side effects on the body and increases bioavailability [2,3]. Chitosan (more precisely, the products of its degradation in the wound by endogenous enzymes) has a powerful wound-healing property [2] and as the literature indicates, antiseptic activity with respect to the most frequently encountered pathogens of purulent complications [4]. The strength of its effect is inferior to antibiotics, but it retains its bacteriostatic activity for 2-2.5 days on contact with microbial flora in liquid medium. It is especially active in the acid medium characteristic of the initial stages of any wound process, and this is characteristic of antibiotics and Furacin solution to a lesser degree [4,5].The proteolytic complex from crab hepatopancreas (CP) is widely used in medicine, cosmetology, the food industry, and other sectors due to the content of unique proteases (including true collagenase), availability, and low cost [5][6][7]. One problem in obtaining insoluble derivatives of CP on oxidized or unmodified cellulose is the rapid desorption of CP from the textile substrate due to the unusually low isoelectric point of the enzymes it contains (pI < 3.5) [6,7].We synthesized substrates made from cellulose, oxidized cellulose, and chitosan with a positive charge on which CP was also immobilized [8,9].
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.