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Cosmarium sp is unicellular microalga which was grown in bold basal medium with the controlled condition and investigated biochemical characterizations for biodiesel production and evaluated standardization of ethanol production. Once microalgae were reaches the proper growth stage total lipid was analyzed and these lipids were used for the production of biodiesel by transesterification process using Calcium oxide (0.66%) as a catalyst. Bioethanol production was done by using the defatted residues of Cosmarium sp. with Saccharomyces cerevisiae (10%). In view of the above-mentioned facts, the present study has been designed to enhance the production of biodiesel and bioethanol.

Background: Peptidyl-prolyl cis-trans isomerisation (PPIases) enzyme plays a vital role in protein folding. It catalyses the cis-trans isomerisation of peptide bonds, an essential step for newly synthesized protein to acquire its correct functional conformation in both prokaryotes and eukaryotes. Objective: The present study showed the biochemical and molecular characterisation of cyclophilins (PpiB), a type of peptidyl-prolyl isomerases proteins from the pathogenic bacteria Salmonella Typhimurium. Methods: Salmonella Typhimurium is one of the leading serovars responsible for human and animal salmonellosis globally, with the majority of human cases originating through the food chain. Here successful expression and purification of PpiB protein have been demonstrated and LC-MS based analyses showed high protein score and similarity with other PPi protein. Further the enzymatic activity of the purified recombinant PpiB was determined using Succinyl-Ala-Phe-Pro-Phe-p nitroanilide as substrate and enzyme-catalysed reaction. Result: Km and Vmax were calculated and found to be Vm = 1.023 ± .06400 min/µg, Km = 0.6219 ± 0.1701 µM, respectively.We have reported for the first time the presence of Salmonella PPIase-B (PpiB) protein isoforms in salmonella genome having PPi activity. Conclusion: Taken together, our data clearly showed that Salmonella Cyclophilin B (PpiB) protein is active and involved in diverse biological processes and highly similar to the different domain of Cyclophilin proteins.

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