Comparison of the single molecule activity distributions of recombinant and non-recombinant bovine intestinal alkaline phosphatase

Single molecule assays were performed on bovine intestinal alkaline phosphatase and the recombinant enzyme expressed in Pichia pastoris using a capillary electrophoresis-based method. The catalytic rates for the bovine and recombinant enzymes were found to be 11,000 ± 7000 min−1 (N = 161) and 12,000 ± 7000 min−1 (N = 173), respectively. Mean catalytic rates and variances did not differ significantly between the enzyme from both sources. Furthermore, the distribution of catalytic rates were indistinguishable.