Xylanase immobilization on functionalized polyaniline support by covalent attachment

MADAKBAŞ S., DANIŞ Ö., DEMİR S., KAHRAMAN M. V.

STARCH-STARKE, cilt.65, ss.146-150, 2013 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 65
  • Basım Tarihi: 2013
  • Doi Numarası: 10.1002/star.201200104
  • Dergi Adı: STARCH-STARKE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.146-150
  • Anahtar Kelimeler: Immobilization, PANI, Xylanase, ALPHA-AMYLASE, ACTIVATION, CARBONATE, ENZYMES
  • Marmara Üniversitesi Adresli: Evet

Özet

Chemically synthesized polyaniline (PANI) was used as polymeric support for xylanase immobilization. The polymer was first activated with glutaraldehyde and then xylanase was successfully immobilized. Xylanase bound polymer was characterized using FTIR. The optimum pH of the immobilized enzyme was at pH 5, which was shifted 1.0?pH unit to the acidic region when compared to the free enzyme. Thermal stability of the xylanase was improved with the immobilization. The characteristic properties of the immobilized and native enzyme, such as kinetic activity, reusability and storage stability were also studied at optimum pH and temperature. Immobilized enzyme exhibited better reusability and storage stability than the free one. Vmax values for the free and immobilized enzymes were calculated as 1.44 and 0.44?mg/mL/min, respectively. The Km values for the immobilized xylanase were found to be lower.