Abstract
The deacylation of Pen G was carried out by using recombinant E. coli in an aqueous two-phase system consisting of polyethylene glycol and potassium phosphate solution, which partitions the cells to the bottom phase and the products to the top phase. Bioconversion and product separation were carried out in the same reactor. Repeated batch conversion was employed ten times and enzymic activity showed only a slight decline. When pure enzyme was used for bioconversion in an aqueous two-phase system, the decline was fast and bioconversion using whole cell penicillin acylase was better than that obtained using the pure acylase.
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