Catalysis science and technology p. 5971 - 5978 (2019)
Update date:2022-08-10
Topics:
Yin, Dong-Ya
Pan, Jiang
Zhu, Jie
Liu, You-Yan
Xu, Jian-He
l-Carnosine (l-Car, β-alanyl-l-histidine) is a bioactive dipeptide with important physiological functions. Direct coupling of unprotected β-Ala (β-alanine) with l-His (l-histidine) mediated by an enzyme is a promising method for l-Car synthesis. In this study, a new recombinant dipeptidase (SmPepD) from Serratia marcescens with a high synthetic activity toward l-Car was identified by a genome mining approach and successfully expressed in Escherichia coli. Divalent metal ions strongly promoted the synthetic activity of SmPepD, with up to 21.7-fold increase of activity in the presence of 0.1 mM MnCl2. Higher temperature, lower pH and increasing substrate loadings facilitated the l-Car synthesis. Pilot biocatalytic syntheses of l-Car were performed comparatively in batch and continuous modes. In the continuous process, an ultra-filtration membrane reactor with a working volume of 5 L was employed for catalyst retention. The dipeptidase, SmPepD, showed excellent operational stability without a significant decrease in space-time yield after 4 days. The specific yield of l-Car achieved was 105 gCar gcatalyst-1 by the continuous process and 30.1 gCar gcatalyst-1 by the batch process. A nanofiltration membrane was used to isolate the desired product l-Car from the reaction mixture by selectively removing the excess substrates, β-Ala and l-His. As a result, the final l-Car content was effectively enriched from 2.3% to above 95%, which gave l-Car in 99% purity after ethanol precipitation with a total yield of 60.2%. The recovered substrate mixture of β-Ala and l-His can be easily reused, which will enable the economically attractive and environmentally benign production of the dipeptide l-Car.
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