α-Amylases (EC 3.2.1.1) catalyze the hydrolysis of α- (1,4) glycosidic linkages of starch, amylose, amylopectin,glycogen, and various maltooligosaccharides.1,2 α-Amylases are produced from a wide variety of biological sources such as bacteria, fungi, plants, and animals. α-Amylases from different biological sources produce maltooligosaccharides of different sizes and amounts from starch and related materials due to a different number of D-glucopyranose binding subsites. Cellulases hydrolyze cellulose polymer to smaller oligosaccharides and glucose, and include three major types of enzymes including endoglucanases (EC 3.2.1.4) which randomly attack the cellulose polymer by endoaction, cellobiohydrolases (EC 3.2.1.91) which act as exoenzymes and remove cellobiose or glucose from the non-reducing end of the cellulose chain, and glucosidases (EC 3.2.1.21) which hydrolyze cellooligosaccharides and cellobiose into glucose. These enzymes can either be free, particularly in aerobic microorganisms, or grouped in a multi-component enzyme complex, cellulosome, such as in anaerobic cellulolytic bacteria. In this study we assayed the activity of cellulase alone and cellulase and α-amylase together.Also we measued the activity of α-amylase alone and α-amylase with cellulose. Furthermore the temperature and pH optima and the Vmax and Km of the enzymes were also measured. We observed that the optimum temperature and pH for the activity of cellulase alone and for cellulose + α- amylase were 60 ° C and 4.5, respectively. Values obtained for optimum temperature and pH of both α-amylase alone and α- amylase and cellulose together were 50° C and 6.5,respectively.

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