Acrylamide grafted poly(ethylene terephthalate) fibers activated by glutaraldehyde as support for urease

Elçin Y. M., Saçak M.

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, cilt.60, sa.1, ss.19-32, 1996 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 60 Sayı: 1
  • Basım Tarihi: 1996
  • Doi Numarası: 10.1007/bf02788056
  • Dergi Adı: APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.19-32
  • Anahtar Kelimeler: urease immobilization, poly(ethylene terephthalate) fibers, graft polymerization, acrylamide grafting, glutaraldehyde activation, urea hydrolysis, POLY(ETHYLENE-TEREPHTHALATE) FIBERS, IMMOBILIZATION, COPOLYMERIZATION, METHACRYLATE, GELATIN, SILICA, ENZYMES, GELS
  • Ankara Üniversitesi Adresli: Evet

Özet

Urease was covalently immobilized on acrylamide-grafted poly (ethylene terephthalate) fibers after glutaraldehyde activation. Urease-containing fibers showed a very high operational stability and reusability, with about 85% of the initial activity after 90 d. The thermostability of the bound urease was positively influenced, and a slight change in optimum temperature was observed after immobilization, when compared with the free enzyme. The pH optimum of both types of urease was found to be the same, but immobilized urease showed an increased stability in a broader range of pH. The kinetic studies exhibited a slightly higher K-m value for the bound enzyme, with a value of 4.50 mmol dm(-3), when compared with the free enzyme (2.82 mmol dm(-3)), which demonstrated that the immobilization procedure did not cause an unfavorable conformation for the substrate-product formation and a hindered diffusion. The graft yield was also found effective on maximum activity of immobilized urease. Twenty-five percent of the acrylamide-grafted fibers exhibited the highest enzymatic activity together with the highest water uptake. Higher graft yields were not suitable for the immobilization of the enzyme molecules as a result of crosslinks formed between the poly(acrylamide) chains and glutaraldehyde.