## Abstract Penicillin V acylase from the actinomycete __Streptomyces lavendulae__ ATCC 13664 has been immobilized to epoxy‐activated acrylic beads (Eupergit C®) by covalent binding. Further linkage of bovine serum albumin after enzyme immobilization was carried out in order to remove the remaining
Covalent immobilization of penicillin acylase from Streptomyces lavendulae
✍ Scribed by Jesús Torres-Bacete; Miguel Arroyo; Raquel Torres-Guzmán; Isabel de la Mata; María Pilar Castillón; Carmen Acebal
- Book ID
- 110226257
- Publisher
- Springer Netherlands
- Year
- 2000
- Tongue
- English
- Weight
- 42 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0141-5492
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## Abstract Penicillin acylase has been immobilized to carboxymethylcellulose and to the resin Amberlite XAD7. The reaction kinetics of the enzyme were affected by both intrinsic (molecular) and microenvironmental effects. The Michaelis constant for the enzyme increased after immobilization as a re
Penicillin acylase obtained from E. Coli (E. C. 3.5.1.11) was covalently bound via glutaric aldehyde to acrylic carriers crosslinked with divinylbenzene or ethylene glycol dimethacrylate. The best enzymatic preparation was obtained by using ethyl acrylate/ ethylene glycol dimethacrylate copolymer. I