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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

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Aim and Background: High efficient transformation of external DNA into the bacterial cells accounts as the main step of microbial biotechnology. For this purpose, some conventional methods have been developed. Using cold CaCl2 is one of the most important and cheapest ways for DNA transformation into the gram negative bacteria such as Escherichia coli. Commonly used methods have a low transformation rate about 105 to 107 transformants per 1μg of DNA. Due to the importance of DNA transformation procedure, numerous attempts have been applied to optimize the conventional methods such as cold CaCl2. In this study we showed that it is possible to increase DNA transformation efficiency into the E. coli in standard CaCl2 method, using a membrane permeable cationic peptide (CM11). Material and methods: Based on ClCa2 competent cell preparation method, the bacterial cells were treated by different concentration of peptide (0.5, 1, 2, 3 and 6 μg/ml) in two different ways. Thereafter pET-28a (+), pGEX4T-1 and pUC19 as model plasmids were separately transformed into the competent cells. 

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In the past two decades, given the importance of biotech drugs and its effective role in the treatment of many diseases, the commercialization and selling of these products is dramatically grown worldwide and many large companies have obtained macro-economic benefits for their own and their mother country by investing in this area. The United States is the largest investor in the research, production and sales of pharmaceutical products derived from biotechnology therefore, studying the biotechnological drugs market can provide an overall vision about the commercialization process and the market for these types of drugs in the world. For the young researchers in biotechnology and pharmaceutical field to be familiar with commercial status and sales of biotechnological drugs, the business development and selling of these products in the United States in a period of 10 years (2002-2012) was studied as a reference model. Data presented in this article is based on the reports from 2007 to 2014, which are published in each year in the Nature Biotechnology Journal.