Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei

Publication date: Available online 13 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Shalyda Md Shaarani, Jamaliah Md Jahim, Roshanida A. Rahman, Ani Idris, Abdul Munir Abdul Murad, Rosli Md Illias Numerous state-of-the-art technologies and new types of carriers have been developed recently to improve enzyme immobilization. Cross-linked enzyme aggregate (CLEA) technology is a lucrative prospect, as several robust biocatalysts have been generated using this simple method of carrier-free immobilization with the possibility of using semipurified enzyme. However, the low lysine content in the enzyme remains a challenge for effective crosslinking. In this work, maghemite (γ- Fe2O3), a recently sought after nanoparticle, was silanized with (3-aminopropyl) triethoxysilane (APTES) for use in the preparation of cross-linked enzyme aggregates of recombinant xylanase from Trichoderma reesei (Xyl-CLEA-silanized maghemite). Prior screening revealed ethanol to be the best precipitant, and a 0.2: 1 (v: v) glutaraldehyde to enzyme ratio was essential to form active CLEAs. The Xyl-CLEA-silanized maghemite succeeded in increasing the activity recovery 1.66- and 1.5-fold compared to conventional Xyl-CLEAs and Xyl-CLEA-BSA, respectively. The silanization of maghemite with APTES was proven feasible when a 0.0075:1 (v: v) maghemite to enzyme ratio was able to achieve a 78% activity recovery of the xylanase aggregates, whereas the non-silanized maghemite on...
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research