As 1% (w/v) starch solution = 1 g starch in 100 ml water. 0.07% (w/v) = 4.375 µmols 0.14% (w/v) = 8.75 µmols 0.28% (w/v) = 17.5 µmols. To calculate Km: -1/-0.058 mg/ml = 17.24 µmols.min-1.mg-1 and to determine Vmax: 1/1.9 mg/ml = 0.52 µmols.min-1.mg- 1 from these results, we show Vmax in µmoles of maltose produced per minute per mg of α-amylase (µmols.min-1. mg-1). The smaller km valve suggests that the affinity of the enzymes is higher. The results of the graph showing the amount of maltose released by the action of α-amylase in each tube show that as the starch concentration increases, the kinetic energy accelerates. The starch concentration of 0.28% (w/v) showed that when the maximum measured time is reached, the maltose concentration is 1.12 mM, showing that the maximum activity occurred at this stage. A study conducted by Enemchukwu et al., (2013) on α-amylase enzyme samples from one hundred healthy adult smokers and fifty non-smokers. This experiment showed the effects of temperature, pH and substrate concentration. The results showed that the valve Km of 3.30 × 10–2 mg/ml and 3.37 × 10–2 mg/ml results in smokers and non-smokers. The results suggest that maximum activity occurred at the optimal temperature (40°C). Enemchukwu et al. (2013) concluded by stating that smoking has no effect on the salivary α-amylase enzyme.