This study aimed to characterize the enzymatic properties of L-aspartate-α-decarboxylase (ADC) derived from red flour beetles in order to provide theoretical and technical support for β-alanine bioproduction. A mutant K49R derived from red flour beetles was purified and characterized, followed by conducting a whole-cell catalysis. It was found that the optimum reaction pH and temperature of K49R was 6.5 and 42 ℃, respectively, and the thermal stability of K49R was 1.7 times higher than that of the wild type. The substrate affinity of K49R was greatly improved, and the catalytic efficiency was 1.8 times higher that of the wild type. Additionally, the biomass of the recombinant Escherichia coli and the expression level of ADC were effectively increased by adding 10 g/L glucose into the medium. The addition of pyridoxal phosphate (PLP) shorted the reaction time and improved the catalytic efficiency. In conclusion, by construction of an engineered strain this study provides a green and efficient biosynthesis method to produce β-alanine, which lays an important foundation for industrializing the biosynthesis of L-aspartate.
YE Wenqi
,
XUE Lan
,
WANG Chao
,
CUI Wenjing
,
ZHOU Zhemin
,
LIU Zhongmei
. Characterization of enzymatic properties of an insect-derived L-aspartate-α-decarboxylase variant[J]. Food and Fermentation Industries, 2019
, 45(19)
: 63
-67
.
DOI: 10.13995/j.cnki.11-1802/ts.021344
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