MpADC, an l-aspartate-α-decarboxylase, from Myzus persicae, that enables production of β-alanine with high yield by whole-cell enzymatic catalysis

Table 1 Comparison of β-alanine production by ADCs from different sources

Source	Enzymes	The concentration of cells²	Reaction time (h)	yield (g/L)	Space–time yield (g/(L*h))	References
Prokaryotic	panD
C. glutamicum	CgADC	20 g/L	36	12.85	0.357	[12]
B. subtilis	I46V/I88M/K104S/I126*	20 g/L	14	124.3	9.563	[21]
B. subtilis	E56S	OD₆₀₀ = 100	9	215.3	23.90	[11]
B. aryabhattai	I88M	20 g/L	12	128.67	10.72	[26]
Eukaryotic	ADC
T. castaneum	R98H/K305S	OD₆₀₀ = 100	48	170.5	3.550	[8]
T. castaneum	G369A	OD₆₀₀ = 200	35	162	4.629	[23]
T. castaneum	K221R	OD₆₀₀ = 200	23	134.72	5.857	[49]
M. persicae	Δ39	50 g/L(OD₆₀₀ = 18.4)	13.5	232.36	17.21	This work
Co-expressing PanD and ADC
B. subtilis/T. castaneum	BTW	OD₆₀₀ = 60	30	271.5	9.05	[48]

1. ‘*’ represents the termination codon
2. The amount of engineered bacteria added was expressed as the concentration of bacterial suspension (OD₆₀₀ or the concentration of bacterial wet weight)

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