Table 1.
Purification of recombinant protein MxynB-8, XynB-DT, Xln-DT, and Dt-xyl3.
Enzyme | Culture extract | Ni affinity chromatography | Yield (%) | Fold purification | ||||
---|---|---|---|---|---|---|---|---|
Total activity (U) | Total protein (mg) | Specific activity (U/mg) | Total activity (U) | Total protein (mg) | Specific activity (U/mg) | |||
MxynB-8 | 56,312.8 | 97.7 | 576.38 | 43,923.9 | 48.2 | 910.68 | 78.1 | 1.58 |
XynB-DT | 13,766.1 | 2,935.2 | 4.69 | 9,553.7 | 352.2 | 27.12 | 69.4 | 5.78 |
Xln-DT | 560.4 | 190.5 | 2.94 | 318.3 | 37.2 | 8.56 | 56.8 | 2.91 |
Dt-xyl3 | 532.4 | 287.9 | 1.85 | 285.4 | 46.3 | 6.16 | 53.4 | 3.35 |
Substrate for MxynB-8 and XynB-DT was beechwood xylan, while substrate for Xln-DT and Dt-xyl3 was p-nitrophenyl-β-d-xylopyranoside.