Abstract
β-Alanine is mainly produced by chemical methods in current industrial processes. Here, panD from Corynebacterium glutamicum encoding l-aspartate-α-decarboxylase (ADC) was cloned and expressed in Escherichia coli BL21(DE3). ADC C.g catalyzes the α-decarboxylation of l-aspartate to β-alanine. The purified ADC C.g was optimal at 55 °C and pH 6 with excellent stability at 16–37 °C and pH 4–7. A pH–stat directed, fed-batch feeding strategy was developed for enzymatic synthesis of β-alanine to keep the pH value within 6–7.2 and thus attenuate substrate inhibition. A maximum conversion of 97.2 % was obtained with an initial 5 g l-aspartate/l and another three feedings of 0.5 % (w/v) l-aspartate at 8 h intervals. The final β-alanine concentration was 12.85 g/l after 36 h. This is the first study concerning the enzymatic production of β-alanine by using ADC.
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Acknowledgments
This work was financially supported by the National High Technology Research and Development Program of China (Grant No. 2012AA021201), the Program for New Century Excellent Talents in University (Grant No. NCET-11-0665) and the Research Program of State Key Laboratory of Food Science and Technology, Jiangnan University (Project No. SKLF-ZZA-201201).
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Shen, Y., Zhao, L., Li, Y. et al. Synthesis of β-alanine from l-aspartate using l-aspartate-α-decarboxylase from Corynebacterium glutamicum . Biotechnol Lett 36, 1681–1686 (2014). https://doi.org/10.1007/s10529-014-1527-0
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DOI: https://doi.org/10.1007/s10529-014-1527-0