As 1% (w/v) starch solution = 1 g starch in 100 ml water. 0.07% (w/v) = 4.375 µmol 0.14% (w/v) = 8.75 µmol 0.28% (w/v) = 17.5 µmol . To calculate Km: -1/-0.058 mg/ml = 17.24 µmols.min-1.mg-1 and to determine Vmax: 1/1.9mg/ml = 0.52 µmols.min-1.mg-1 from these results you can see Vmax in µmols 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 increases. The starch concentration of 0.28% (w/v) demonstrated that once the maximum measured time was reached, the maltose concentration was 1.12 mM, demonstrating that maximum activity occurred at this point . 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 Km valve of 3.30 × 10–2 mg/ml and 3.37 × 10–2 mg/ml comes from smokers and non-smokers. The results suggest that maximum activity occurred at the optimal temperature (40°C). Enemchukwu et al., (2013) concluded that smoking has no effect on the salivary α-amylase enzyme