Purifi cation and Characterization of Protease From Bacillus sp. TBRSN- 1  

Oleh:

Margino, Sebastian ; Jumi’ati ; Ngadiman

Jenis: Article from Journal - ilmiah nasional - terakreditasi DIKTI
Dalam koleksi: Indonesian Journal of Biotechnology vol. 18 no. 02 (2013), page 151-160.
Topik: protease; purifi cation; indigenous Bacillus sp. TBRSN-1
Fulltext: 251-668-1-PB_Ros.pdf (312.2KB)

Isi artikel

Potato Cyst Nematode (PCN), Globodera rostochiensis, is one of the important potato’s pests and caused economic looses up to 70% in the several centrals of potato plantations in Indonesia. PCN’s shell component of egg shell containing chitin (inner layer) and viteline/ protein (outer layer). The purpose of this research was to purify of protease Bacillus sp. TBRSN-1, isolate from tomato’s rhizosfer in Yogyakarta province. The purifi ed protease could be used for cutting the life cycle of PCN. Results showed that Bacillus sp. TBRSN-1 could produce extracellular protease and purifi cation using DEAE-cellulose ion-exchange chromatography and Sephacryl S-300 gel fi ltration chromatography resulted in specifi c activity 4.31 fold and 1.68% recovery. Analysing using SDS-PAGE 12.5% and molecular weight 48.1 kDa. Km and Vmax values of the protease for casein substrate were 7.83 mg/ml and 4.03 ìg/h, respectively. The optimum activity at the temperature 30oC and pH 7.0.

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