Binary immobilization of tyrosinase by using alginate gel beads and poly(acrylamide-co-acrylic acid) hydrogels

Yahsi A., Sahin F., DEMİREL G., Tumturk H.

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, cilt.36, sa.4, ss.253-258, 2005 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 36 Sayı: 4
  • Basım Tarihi: 2005
  • Doi Numarası: 10.1016/j.ijbiomac.2005.06.011
  • Dergi Adı: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.253-258
  • Anahtar Kelimeler: tyrosinase, binary immobilization, alginate, poly(acrylamide-co-acrylic acid), ENZYME IMMOBILIZATION, AMPEROMETRIC BIOSENSOR, POLYPHENOL OXIDASE, PHENOLS, REMOVAL
  • Gazi Üniversitesi Adresli: Evet

Özet

The use of the immobilized and the stable enzymes has immense potential in the enzymatic analysis of clinical, industrial and environmental samples. However, their widespread uses are limited due to the high cost of their production. In this study, binary immobilization of tyrosinase by using Ca-alginate and poly(acrylamide-co-acrylic acid) [P(AAm-co-AA)] was investigated. Maximum reaction rate (V-max) and Michaelis-Menten constant (K-m) were determined for the free and binary immobilized enzymes. The effects of pH, temperature, storage stability, reuse number and thermal stability on the free and immobilized tyrosinase were also examined. For the free and binary immobilized enzymes on Ca-alginate and P(AAm-co-AA), optimum pH was found to be 7 and 5, respectively. Optimum temperature of the free and immobilized enzymes was observed to be 30 and 35 degrees C, respectively. Reuse number, storage and thermal stability of the free tyrosinase were increased by a result of binary immobilization. (c) 2005 Published by Elsevier B.V.