Stabilization of Tyrosinase-Bovine Serum Albumin Crystals by Glutaraldehyde
D. Norouzian1, A. Akbarzadeh1, M.H. Abnosi2, S.M. Atyabi2, A. Farahngi2, M.R. Mehrabi2 & A. Eslamifar2 Show affiliations
- Pasteur Institute of Iran, Iran
- Arak University, Iran
American Journal of Biochemistry and Biotechnology, Volume 3, Issue 3, pp. 110–113 · doi.org/10.3844/ajbbsp.2007.110.113
Abstract
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.
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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. https://doi.org/10.3844/ajbbsp.2007.110.113
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