In vivo immobilization of d-hydantoinase in Escherichia coli

摘要: d - p -Hydroxyphenylglycine ( -HPG) is a precursor required for the synthesis of semi-synthetic antibiotics. This unnatural amino acid can be produced by transformation reaction mediated -hydantoinase -HDT) and -amidohydrolase. In this study, method was developed to integrate production immobilization recombinant -HDT in vivo . approached first fusion gene encoding with phaP (encoding phasin) Ralstonia eutropha H16. The then expressed Escherichia coli strain that carried heterologous synthetic pathway polyhydroxyalkanoate (PHA). As result, found associate isolated PHA granules. Further characterization illustrated immobilized on exhibited maximum activity at pH 9 60°C had half-life 95 h 40°C. Moreover, PHA-bound could reused 8 times conversion yield exceeding 90%. Overall, it illustrates feasibility approach facilitate enzymes E. strain, which may open new avenue enzyme application industry.