Immobilization of modified penicillin G acylase on Sepabeads carriers
Samo za registrovane korisnike
2009
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
An approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads(R) carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads(R) EC EA and Sepabeads(R) EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable... than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5-fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme.
Ključne reči:
penicillin G acylase / modification / immobilization / Sepabeads carriersIzvor:
Chemical Papers, 2009, 63, 2, 117-124Izdavač:
- Versita, Warsaw
Finansiranje / projekti:
- Razvoj biotehnoloških postupaka za proizvodnju aditiva i novih formulacija za prehrambenu industriju (RS-20064)
DOI: 10.2478/s11696-009-0012-z
ISSN: 0366-6352
WoS: 000263300100003
Scopus: 2-s2.0-60249090445
Institucija/grupa
Tehnološko-metalurški fakultetTY - JOUR AU - Žuža, Milena AU - Milosavić, Nenad AU - Knežević-Jugović, Zorica PY - 2009 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1447 AB - An approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads(R) carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads(R) EC EA and Sepabeads(R) EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5-fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme. PB - Versita, Warsaw T2 - Chemical Papers T1 - Immobilization of modified penicillin G acylase on Sepabeads carriers EP - 124 IS - 2 SP - 117 VL - 63 DO - 10.2478/s11696-009-0012-z ER -
@article{ author = "Žuža, Milena and Milosavić, Nenad and Knežević-Jugović, Zorica", year = "2009", abstract = "An approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads(R) carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads(R) EC EA and Sepabeads(R) EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5-fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme.", publisher = "Versita, Warsaw", journal = "Chemical Papers", title = "Immobilization of modified penicillin G acylase on Sepabeads carriers", pages = "124-117", number = "2", volume = "63", doi = "10.2478/s11696-009-0012-z" }
Žuža, M., Milosavić, N.,& Knežević-Jugović, Z.. (2009). Immobilization of modified penicillin G acylase on Sepabeads carriers. in Chemical Papers Versita, Warsaw., 63(2), 117-124. https://doi.org/10.2478/s11696-009-0012-z
Žuža M, Milosavić N, Knežević-Jugović Z. Immobilization of modified penicillin G acylase on Sepabeads carriers. in Chemical Papers. 2009;63(2):117-124. doi:10.2478/s11696-009-0012-z .
Žuža, Milena, Milosavić, Nenad, Knežević-Jugović, Zorica, "Immobilization of modified penicillin G acylase on Sepabeads carriers" in Chemical Papers, 63, no. 2 (2009):117-124, https://doi.org/10.2478/s11696-009-0012-z . .