Preliminary fractionation and derivatives changes of myoglobin from tilapia (O. niloticus x O. aureus) dark muscle with ammonium sulfate

摘要

Ammonium sulfate fractionation was implicated as one of essential steps to purified Myoglobin (Mb).We adopted SDS-PAGE analysis and absorption spectra scanning to demonstrate the effect of ammonium sulfate on Mb and its derivatives. The results shown that protein with the molecular weight above 37.8kDa were dominated in myoglobin extract of tilapia, which can be precipitated with ammonium sulfate. Mb molecular weight of tilapia is about 15.8 kDa, which can be collected by the treatment of ammonium sulfate with saturation between 60%-70% to remove unwanted protein. The absorption spectra show that Mb derivatives could be transferred to met-myoglobin after preliminary fractionating with ammonium sulfate.