Abstract
Penicillin acylase from Streptomyces lavendulae has been covalently immobilized to epoxy-activated acrylic beads (Eupergit C). Consecutive modification of the matrix with bovine serum albumin leads to a new biocatalyst (ECPVA) with enhanced activity (1.5 fold) in the hydrolysis of penicillin V respect to its soluble counterpart. This biocatalyst had a K m value of 7.6 mM, slightly higher than K m for native acylase (3 mM). In addition, ECPVA can be recycled for at least 50 consecutive batch reactions without loss of catalytic activity.
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Torres-Bacete, J., Arroyo, M., Torres-Guzmán, R. et al. Covalent immobilization of penicillin acylase from Streptomyces lavendulae. Biotechnology Letters 22, 1011–1014 (2000). https://doi.org/10.1023/A:1005601607277
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DOI: https://doi.org/10.1023/A:1005601607277