Stabilization of Tyrosinase-Bovine Serum Albumin Crystals by Glutaraldehyde
D. Norouzian, A. Akbarzadeh, M.H. Abnosi, S.M. Atyabi, A. Farahngi, M.R. Mehrabi and A. Eslamifar
DOI : 10.3844/ajbbsp.2007.110.113
American Journal of Biochemistry and Biotechnology
Volume 3, Issue 3
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.
© 2007 D. Norouzian, A. Akbarzadeh, M.H. Abnosi, S.M. Atyabi, A. Farahngi, M.R. Mehrabi and A. Eslamifar. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.