Activity and stability of urease entrapped in thermosensitive poly(N-isopropylacrylamide-co-poly(ethyleneglycol)-methacrylate) hydrogel

BAYRAMOĞLU G., Arica M. Y.

BIOPROCESS AND BIOSYSTEMS ENGINEERING, cilt.37, sa.2, ss.235-243, 2014 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 37 Sayı: 2
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1007/s00449-013-0990-7
  • Dergi Adı: BIOPROCESS AND BIOSYSTEMS ENGINEERING
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.235-243
  • Anahtar Kelimeler: N-isopropyl acrylamide, Thermoresponsive hydrogel, Immobilization, Entrapment, Urease, LIPASE NANOGEL, COVALENT IMMOBILIZATION, N-ISOPROPYLACRYLAMIDE, NETWORKS, NANOPARTICLES, ADSORPTION, CATALYSIS, MEMBRANE, BEHAVIOR, LINKING
  • Gazi Üniversitesi Adresli: Evet

Özet

Urease was entrapped in thermally responsive poly(N-isopropylacrylamide-co-poly(ethyleneglycol)-methacrylate), p[NIPAM-p(PEG)-MA], copolymer hydrogels. The copolymer membrane shows temperature-responsive properties similar to conventional p(NIPAM) hydrogels, which reversibly swell below and de-swell above the lower critical solution temperature of p(NIPAM) hydrogel at around 32 A degrees C. The retained activities of the entrapped urease (in p[NIPAM-p(PEG)-MA]-4 hydrogels) were between 83 and 53 % compared to that of the same quantity of free enzyme. Due to the thermo-responsive character of the hydrogel matrix, the maximum activity was achieved at around 25 A degrees C with the immobilized urease. Optimum pH was the same for both free and entrapped enzyme. Operational, thermal and storage stabilities of the enzyme were found to increase with entrapment of urease in the thermoresponsive hydrogel matrixes. As for reusability, the immobilized urease retained 89 % of its activity after ten repeated uses.