Volume 14, Issue 6 (Nov-Dec 2020)                   mljgoums 2020, 14(6): 23-27 | Back to browse issues page

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Gharagozloo Hesari N, Esmaeili D, Mohammadian T, Shahhosseini M H, Ferdosi A. Bioinformatical Analysis of Lipase-Subtilisin Protein Fusion. mljgoums. 2020; 14 (6) :23-27
URL: http://mlj.goums.ac.ir/article-1-1286-en.html
1- Department of Microbiology, Shahr-e-Qods Branch, Islamic Azad University, Tehran, Iran
2- Department of Microbiology and Applied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran and Applied Virology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
3- Department of Microbiology, Shahr-e-Qods Branch, Islamic Azad University, Tehran, Iran , tmohammadian@qodsiau.ac.ir
Abstract:   (90 Views)
Background and objectives: Industrial wastewater is worldwide health concern. Microorganisms present in the environment have an important role in the biodegradation of lipids, fats and proteins from wastewater. In this regard, microbial lipases and proteases are interesting research targets because of high stability, broad substrate specificity, high yields and availability. In this study, we analyze sequences encoding lipase of Pseudomonas putida and subtilisin of Bacillus subtilis for generation of a new recombinant protein for degradation of environmental contaminations caused by lipids and proteins.
      Methods: In this study, sequences of the genes encoding lipase and subtilisin were obtained from GenBank. To predict the 3D structure of the protein, modeling was carried out. The prediction of secondary structure, tertiary structure and solvent accessibility was carried using bioinformatics tools including I-TASSER, GoR4 and ExPasy.
      Results: The lipase-subtilisin fusion protein was well-characterized by bioinformatical studies with appropriate spatial and secondary structures. The protein had appropriate hydrophilicity, biological half-life and thermal and acidic stability. The codon optimization was performed appropriately.
      Conclusion: Overall, the bioinformatical analysis of the designed protein showed that the recombinant lipase-subtilisin protein has a stable structure both in vitro and in vivo, a negative normalized B-factor and lipolytic and proteolytic activities, which makes it suitable for treatment of lipid and protein contaminations.
Full-Text [PDF 666 kb]   (40 Downloads)    
Type of Study: Review Article | Subject: Microbiology
Received: 2020/03/24 | Accepted: 2020/06/29 | Published: 2020/10/29 | ePublished: 2020/10/29

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