Table 2.
Kinetic parameters of AIs
| Source | L-arabinose | D-galactose | |||||
|---|---|---|---|---|---|---|---|
| V max (U mg-1) | K m (mM) | k cat/K m (min-1 mM-1) | V max (U mg-1) | K m (mM) | k cat/K m (min-1 mM-1) | ||
| B. coagulans NL01 | 43.7 | 269.8 | 8.7 | 6.8 | 355.1 | 1.0 | This study |
| B. halodurans | 33.1 | 36 | 51 | 1.3 | 167 | 0.4 | [13] |
| B. licheniformis | NR | 369 | 34 | NR | NR | NR | [15] |
| B. substilis | NR | 120 | 121 | ND | ND | ND | [12] |
| G. thermodenitrificans | 86 | 142 | 48 | NR | NR | 0.5 | [22] |
| P. pentosaceus PC-5 | ND | ND | ND | 7.8 | 66 | 2.9 | [24] |
| A. flavithermus | NR | 78.5 | 0.7 | NR | 25.2 | 5.2 | [11] |
| T. neapolitana | 119 | 116 | 58.1 | 14.3 | 250 | 3.2 | [36] |
Kinetic parameters of BCAI were determined by using 12.5 to 700 mM substrate (L-arabinose or D-galactose) at standard enzyme assay conditions (60 °C, pH 7.5 and 20 min)