Synthesis of β-alanine from l-aspartate using l-aspartate-α-decarboxylase from Corynebacterium glutamicum View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-08

AUTHORS

Yan Shen, Lianzhen Zhao, Youran Li, Liang Zhang, Guiyang Shi

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. More... »

PAGES

1681-1686

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-014-1527-0

DOI

http://dx.doi.org/10.1007/s10529-014-1527-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030245095

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24737081


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