화학공학소재연구정보센터
Biotechnology Letters, Vol.22, No.4, 291-293, 2000
An efficient purification with a high recovery of the inulin fructotransferase of Arthrobacter sp A-6 from recombinant Escherichia coli
Inulin fructotransferase (IFTase, EC 2.4.1.93) of Arthrobacter sp. A-6 was purified from a cell extract of the recombinant Escherichia coli DH5 alpha/pDFE cells carrying the IFTase gene using heat treatment followed by gel filtration. The enzyme was purified 45-fold to apparent homogeneity with a recovery of 79%. SDS-PAGE yielded a single protein band of M-r 46.5 kDa. The recombinant IFTase had a similar thermostability as the original enzyme from Arthrobacter sp. A-6.