Covalent immobilization of penicillin acylase from Streptomyces lavendulae

@article{TorresBacete2004CovalentIO,
  title={Covalent immobilization of penicillin acylase from Streptomyces lavendulae},
  author={Jes{\'u}s Torres-Bacete and Miguel Arroyo and Raquel Torres-G{\'u}zman and Isabel de la Mata and Mar{\'i}a Pilar Castill{\'o}n and Carmen Acebal},
  journal={Biotechnology Letters},
  year={2004},
  volume={22},
  pages={1011-1014}
}
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… CONTINUE READING

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