Isolation，Purification and Characterization of Cellulase from Meretrix meretrix L

Abstract:

Electrophoresis-purity cellulase from Meretrix meretrix L was obtained through buffer solution extraction，ammonium sulfate precipitation，DEAE-Sepharose ion exchange chromato- graphy and Phenyl Sepharose 6 Fast Flow hydrophobic chromatography. The specific activity of purified cellulase was 40.33 U/mg with purification fold of 13.12. SDS-PAGE results revealed the molecular weights of the enzyme was 59 700. Its optimum temperature and pH were 45 ℃and 5.2，respectively. The cellulase was relatively stable in the range of 4~50 ℃ and pH 4~6. Furthermore，its Km value was 0.111 mmol/L under the optimal conditions. The study laid a foundation for studying the composition and structure of endogenous cellulase from animals.