Abstrait

In silico Structural Determination of Fatty acid Hydrolysis and Synthesizing Enzymes for Biofuel Production in Microalgae

S. Sathya, S. Meenakshi and S. Srisudha

Twenty five sequences of algae were retrieved from NCBI for lipase, fatty acid synthase and glycerol 3- phosphate dehydrogenase. Physicochemical parameters were determined using pepstats, ProtParam, ProtScale and Network protein sequence analysis. Conserved regions were identified by multiple sequence alignment using Clustal W. The primary structure analysis of three enzymes indicates that the percentage of Methionine residues is approximately 4% among the selected microalgae. Secondary structure analysis revealed that the proteins are largely alpha helical; this was supported by the homology modeling of three enzymes of Chlamydomonas reinhardtii (L2), Osterococcus lucimarnus (F7) and Osterococcus taurii (G7). Structural validation tools viz., Ramachandran Plot, VERIFY 3D and ERRAT indicates the overall accuracy of the developed models. More active sites are present in Osterococcus lucimarnus (F7) than Chlamydomonas reinhardtii (L2) and Osterococcus taurii (G7). The results revealed that the structural models developed from this study will give useful information for biofuel production