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Background   Trans- 4-hydroxy-L-proline ( trans -Hyp), one of the hydroxyproline (Hyp) isomers, is a useful chiral building block in the production of many pharmaceuticals. Although there are some natural biosynthetic pathways of  trans -Hyp existing in microorganisms, the yield is still too low to be scaled up for industrial applications. Until now the production of  trans -Hyp is mainly from the acid hydrolysis of collagen. Due to the increasing environmental concerns on those severe chemical processes and complicated downstream separation, it is essential to explore some environment-friendly processes such as constructing new recombinant strains to develop efficient process for  trans -Hyp production.    Result  In this study, the genes of  trans- proline 4-hydroxylase ( trans- P4H) from diverse resources were cloned and expressed in  Corynebacterium glutamicum  and  Escherichia coli , respectively. The  trans -Hyp production by these recombinant strains was investigated. The results showed that all the genes from different resources had been expressed actively. Both the recombinant  C. glutamicum  and  E. coli  strains could produce  trans -Hyp in the absence of proline and 2-oxoglutarate.    Conclusions  The whole cell microbial systems for  trans -Hyp production have been successfully constructed by introducing  trans- P4H into  C. glutamicum  and  E. coli . Although the highest yield was obtained in recombinant  E. coli , using recombinant  C. glutamicum  strains to produce  trans -Hyp was a new attempt.

Biosynthesis of trans-4-hydroxyproline by recombinant strains of Corynebacterium glutamicum and Escherichia coli