Journal of Biotechnology & Biomaterials
Open Access

Abstract

Catalase is a ubiquitous enzyme present in almost all life forms that are exposed to oxygen. It belongs to oxido-reductase class of enzymes (E.C No: 1.11.1.6.) and catalyses decomposition of hydrogen peroxide into water and oxygen. Due to its high rate of turnover, abundance, high thermal stability and catalytic activity in large range of pH, catalases have been employed in various applications in food, textile and biomedical industries. However, instability of enzymes in �in vitro� conditions poses a big obstacle for their industrial applications. Immobilization of enzymes particularly their encapsulation into an inorganic/organic matrix offers significant advantages such as increasing the stability of enzymes, protection against protease digestion, ease of separation from reaction-product mixture and reusability in industrial applications. Encapsulation of enzymes in porous silica matrices have been one of the most widely used method for immobilization. Early attempts of encapsulation in pre-formed silica matrix resulted into very little encapsulation/loading of enzymes because once an enzyme molecule is encapsulated it blocks the penetration of further enzyme molecules. In the present work, catalase molecules are encapsulated in silica nanoparticles (~100-200 nm) in two steps; Functionalization of catalase surface with (3-aminopropyl) triethoxysilane (APTES) through EDC/NHS cross-linking chemistry, In situ silica shell synthesis by TEOS hydrolysis in reverse micro-emulsion system. The APTES group of APTES-catalase will get integrated into silica shell through -O-Si-O- bonds. The catalase at silica nanoparticles (Cat-SiNPs) were characterized through different structural and optical techniques. The enzyme activity of catalase was monitored by modified Goth Method.

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