Purification of a dimeric arginine deiminase from Enterococcus faecium GR7 and study of its anti-cancerous activity
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文摘

E. faecium GR7 isolated from dairy a product was used as a source of ADI enzyme.

A three-step protocol for purification of ADI to homogeneity from E. faecium GR7.

Purified enzyme showed the specific ADI activity of 76.65 IU/mg with a 49.17% recovery.

First time reported heterodimer ADI protein with a molecular weight of 94.36 kDa.

Purified ADI exhibited growth inhibition at IC50-1.95 μg/ml against Hep-G2 cells.

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