Objective:To isolate,purify and characterize extracellular protease produced by Xylaria psidii(X.psidii)KT30.Methods:In the present study,the extracellular protease secreted by X.psidii KT30 was isolated and purified ...Objective:To isolate,purify and characterize extracellular protease produced by Xylaria psidii(X.psidii)KT30.Methods:In the present study,the extracellular protease secreted by X.psidii KT30 was isolated and purified by using three steps of protein purification,then the purified protease was characterized by applying qualitative and quantitative enzymatic assays.Results:Extracellular protease with molecular mass 71 kDa has been purified successfully by applying diethylaminoethanol-Sepharose followed by sephadex SG75 with its final specific protease activity of 0.091 IU/mg.Protease was the most active at temperature 60℃ and pH 7.The activity of enzyme was abolished mostly by phenylmethanesulfonyl fluoride,showing it is family of serine protease.Conclusions:Extracellular serine protease produced by X.psidii KT30 with good biochemical properties displayed some promising results for its further application in field of biotechnology or medicine.展开更多
基金Supported by Ministry of Research and Technology,Republic of Indonesia(Grant No.RD-2013-0552).
文摘Objective:To isolate,purify and characterize extracellular protease produced by Xylaria psidii(X.psidii)KT30.Methods:In the present study,the extracellular protease secreted by X.psidii KT30 was isolated and purified by using three steps of protein purification,then the purified protease was characterized by applying qualitative and quantitative enzymatic assays.Results:Extracellular protease with molecular mass 71 kDa has been purified successfully by applying diethylaminoethanol-Sepharose followed by sephadex SG75 with its final specific protease activity of 0.091 IU/mg.Protease was the most active at temperature 60℃ and pH 7.The activity of enzyme was abolished mostly by phenylmethanesulfonyl fluoride,showing it is family of serine protease.Conclusions:Extracellular serine protease produced by X.psidii KT30 with good biochemical properties displayed some promising results for its further application in field of biotechnology or medicine.
