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. 2016 Jul 28;11(7):e0160044. doi: 10.1371/journal.pone.0160044

Table 1. Biochemical properties of DAEases and DTEases.

Enzyme pH Temp. (°C) Metal ions Half-life at 60°C (min) kcat (1/s) Km (mM) kcat/K m (1/mM/min) d-Allulose (g/L)[d-Fructose, g/L] Reference
d-Allulose d-Fructose d-Allulose d-Fructose d-Allulose d-Fructose
A. tumefaciens DAEase 8.0 50 Mn2+ 4b 40 35 12 24 205 85 230 [700] [9]
Clostridium sp. DAEase 8.0 65 Co2+ 10c 537 273 228 279 141 59 120 [500] [10]
C. bolteae DAEase 7.0 55 Co2+ 45b 49 59 27 60 107 59 216 [750] [11]
C. cellulolyticum DAEase 8.0 55 Co2+ 408c 54 56 17 54 186 63 218 [750] [12]
C. scindens DAEase 7.5 55 Mn2+ 50b 31 9 28 40 65 9 NR [13]
Desmospora sp. DAEase 7.5 60 Co2+ NRa 86 1,060 81 549 327 116 143 [500] [14]
Dorea sp. DAEase 6.0 70 Co2+ 60c, 30b 1,311 508 191 153 412 199 115 [500] [15]
P. cichorii DTEase 7.5 60 None NR NR NR NR NR NR NR 150 [780] [7]
R. sphaeroides DTEase 9.0 40 Mn2+ NR NR NR NR NR NR NR 118 [700] [8]
Ruminococcus sp. DAEase 7.5–8.0 60 Mn2+ 96b 41 59 48 216 51 16 125 [500] [16]
T. primita DAEase 8.0 70 Co2+ < 30b 503 292 209 279 144 63 138 [500] [17]
F. plautii DAEase 7.0 65 Co2+ 130b 421 342 162 323 156 64 239 [750] This study

aNR, not reported.

b and c represent that the half-life of each enzyme was measured without and with metal ions, respectively.