Aims and background. Amylases are one of the major industrial enzymes that occupy 25 % of the world enzyme market. These enzymes are used in many different areas, such as paper, textiles, pharmaceutical, food, starch saccharafication and processing industries. Much research has been carried out regarding application of amylolytic enzymes produced by the genus Bacillus, to the production of glucose and beverages, food and detergent industries. Because of the extensive applicability of amylolytic enzymes, research in relation to identification of these enzymes and their characteristic is continuously being carried out. Hence, the aim of this research was to investigate the amylolytic enzyme profile of a native Bacillus strain, and determine its enzyme characteristics.

Materials and Methods. In this study, the enzymatic profile of the bacterium, Bacillus amyloliquefaciens BEH 111, was determined by using the SDS-PAGE, zymogram and TLC methods. Zymography and TLC were used to identify the amylolytic enzyme profile of the bacterium. The molecular weight of α-amylase was estimated by SDS-PAGE. The 3, 5-Dinitrosalisyclic acid (DNS) indicator was used to examine α-amylase activity, quantitatively. Investigation of enzyme characteristics and determination of maximal enzyme activity was carried by the DNS method, at different temperatures, pH values, substrate concentrations and time periods.

Results. The molecular weight of α-amylase was estimated to be 55 kDa by SDS-PAGE. Investigation of enzyme characteristics showed that maximum α-amylase activity was achieved at a temperature of 50oC, pH 7, presence of 2% starch, during a 90 min time period. Enzyme activity obtained under these conditions was 8222 U/L.

Conclusion. The high level of enzyme activity produced by B. amyloliquefaciens BEH 111 can thus be of commercial significance. Furthermore, by having activity at 50oC and above, makes it possible for this enzyme to be applied to processes that use high temperatures. The optimized pH levels of 6-7 that resulted in high enzyme activity can also allow the potential use of this enzyme in processes such as starch liquefaction and gelatinization.

Aim and Background: Lipases are the valuable biocatalysts which have many applications in the industry. It is widely used in catalyzing chemical reactions such as water, alcoholic, acidic hydrolysis and also esterification. Bacterial lipases are the most important kinds of enzymes in the industry because they have special advantages such as the high stability in organic solvent, the ability of soft catalyzation of hydrolytic reactions, facility in production process and it’s relatively low cost. Bacillus pumilus is one of the most considerable bacterial sources of this enzyme but the main problem for producing this enzyme is low expression and secretion. The aim of this research is the production of recombinant lipase from native strain in secreting manner for increasing the level of expression in Bacillus subtilis.

Materials and methods : Lipase-coding gene of bacillus pumilus was cloned into pWB980 plasmid by genetic engineering. After this step, construction plasmids were transferred to Bacillus subtilis WB600 as a host. Then expression and secretion level between native and recombinant forms was evaluated and compared.

Results: Secretory form of lipase enzyme was expressed in Bacillus subtilis. An expression level of this enzyme is higher than normal strain. Conclusion : Recombinant lipase production in Bacillus subtilis is a suitable method for increasing the expression of this enzyme