Thermophilic microorganisms could be isolated from harsh environments where thernenvironmental conditions are not favorable for most microorganisms. Enzymes isolated fromrnthese microbes could have higher activity and stability. Thermostable enzymes can be extractedrnfrom thermophilic microbes and be employed for industrial purposes. The isolation andrncharacterization of these enzymes are crucial steps in biotechnology and enzyme sciences.rnIn this study, five (5) water samples and five (5) soil samples from Afar, a regional state inrnEthiopia. Isolates in all the samples were grown at 70 0C to screen for thermophilicrnmicroorganisms. Among these thermophiles, thirty five (35) colonies from each sample whichrnshowed a positive amylolytic response were selected and the ratio of the clear halo created to therncolony size (HCR) was compared. Based on the HCR, isolates from ALS and MS were selectedrnfor further characterization.rnThe optimum fermentation temperature was found to be 65 0C for both isolates with arnfermentation period of 48 hours under the normal pH of the basal medium. The pH optima forrnthe production of the enzymes were pH 6 for MS and pH 8 for ALS.rnThe enzymes isolated from both isolates were found to be very active at high temperature.rnEnzyme from ALS had a maximum activity at 90 0C while the enzyme from MS had itsrnmaximum activity at 85 0C. pH optimum for ALS was 8 and it was functional in a pH range of 6-rn11. The enzyme from MS had maximum activity at pH value of 6 and it had amylolytic activityrnin a pH range of 4-9.rnBoth enzymes showed good stability for pH and temperature. The enzyme from ALS retainedrn62% of its original activity (2.3817 Â± 0.11 U/ml) after 40 minutes of incubation at 900C however,rnmaintained 6% of its activity at 100 0C. The enzyme was deactivated after 30 minutes (retainingrnonly 5% at 105 0C of its original activity). This enzyme was fairly stable for 30 minutesrnmaintaining more than 50 % of its activity at pH values of 6-9, with no activity at pH values lessrnthan 6. The ion Zn2+ and higher concentrations (10 mM) of Mg2+ strongly inhibited enzymernivrnactivity while 5mM concentration of Ca2+ and Ba2+ induced higher catalysis on the enzyme fromrnALS.rnThe enzyme from MS retained 65% of its original activity (2.5782 Â± 0.56 U/ml) after 40 minutesrnof incubation at 85 0C however, maintained 4% of its activity at 100 0C. The enzyme was fairlyrnstable for 40 minutes maintaining more than 50 % of its activity at pH values of 5-7, with nornactivity at pH values higher than 9. It had 69 % of its activity at pH value of 6 after 40 minutesrnof reaction time and maintained 53 % of its original activity at pH value of 4 after 30 minutes ofrnreaction time. The ion Zn2+ and higher concentrations (10 mM) of Mg2+ strongly inhibitedrnenzyme activity while 5mM concentration of Ca2+ and Ba2+ induced higher catalysis.rnConsidering the requirement of starch liquefaction process of an enzyme with a low pHrnoptimum, the enzyme isolated from MS may offer an advantage since it functions well in acidicrnpH value of up to 4.rnEven though the enzyme activities of ALS and MS improved with the addition of CaCl2, theyrnhad good amylolytic activities in the absence of Ca2+ which is a requirement in large-scale starchrnhydrolysis processes. Therefore, the enzymes from ALS and MS can be employed for starchrnhydrolysis in large-scale processes.