Research Article Open Access

Stabilization of Tyrosinase-Bovine Serum Albumin Crystals by Glutaraldehyde

D. Norouzian1, A. Akbarzadeh1, M.H. Abnosi2, S.M. Atyabi2, A. Farahngi2, M.R. Mehrabi2 and A. Eslamifar2
  • 1 Pasteur Institute of Iran, Iran
  • 2 Arak University, Iran


Tyrosinase and bovine serum albumin were co-crystallized by saturated ammonium sulfate solution(65%) and 20% polyethylene glycol ( PEG) 6000 and n-propanol as co-solvents .The obtained crystals were cross linked by glutaraldehyde solution(1% v/v).Polyethylene glycol 6000 was found to be better co-solvent than n-propanol. The developed biocatalyst could be recycled 6 times without further loss of tyrosinase activity. No loss of activity of cross linked tyrosinase -bovine serum albumin crystals was observed upon storage of the developed CLECs at refrigerator for six months.

American Journal of Biochemistry and Biotechnology
Volume 3 No. 3, 2007, 110-113


Submitted On: 8 January 2007 Published On: 30 September 2007

How to Cite: Norouzian, D., Akbarzadeh, A., Abnosi, M., Atyabi, S., Farahngi, A., Mehrabi, M. & Eslamifar, A. (2007). Stabilization of Tyrosinase-Bovine Serum Albumin Crystals by Glutaraldehyde. American Journal of Biochemistry and Biotechnology, 3(3), 110-113.

  • 1 Citations



  • Tyrosinase
  • Bovine serum albumin
  • PEG 6000
  • n-propanol
  • crystallization
  • glutaraldehyde
  • stability