TY - JOUR AU - Cecchini, Davide A. AU - Serra, Immacolata AU - Ubiali, Daniela AU - Terreni, Marco AU - Albertini, Alessandra M. PY - 2007 DA - 2007/09/10 TI - New active site oriented glyoxyl-agarose derivatives of Escherichia colipenicillin G acylase JO - BMC Biotechnology SP - 54 VL - 7 IS - 1 AB - Immobilized Penicillin G Acylase (PGA) derivatives are biocatalysts that are industrially used for the hydrolysis of Penicillin G by fermentation and for the kinetically controlled synthesis of semi-synthetic β-lactam antibiotics. One of the most used supports for immobilization is glyoxyl-activated agarose, which binds the protein by reacting through its superficial Lys residues. Since in E. coli PGA Lys are also present near the active site, an immobilization that occurs through these residues may negatively affect the performance of the biocatalyst due to the difficult diffusion of the substrate into the active site. A preferential orientation of the enzyme with the active site far from the support surface would be desirable to avoid this problem. SN - 1472-6750 UR - https://doi.org/10.1186/1472-6750-7-54 DO - 10.1186/1472-6750-7-54 ID - Cecchini2007 ER -