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:   (5056 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]   (651 Downloads)    
Research Article: Review Article | Subject: Microbiology
Received: 2020/03/24 | Accepted: 2020/06/29 | Published: 2020/10/29 | ePublished: 2020/10/29

References
1. Dzionek A, Wojcieszyńska D, Guzik U. Natural carriers in bioremediation: A review. Electronic Journal of Biotechnology. 2016; 23: 28-36. [DOI:10.1016/j.ejbt.2016.07.003] [Google Scholar]
2. Jaeger K-E, Ransac S, Dijkstra BW, Colson C, van Heuvel M, Misset O. Bacterial lipases. FEMS microbiology reviews. 1994; 15(1): 29-63. [DOI:10.1111/j.1574-6976.1994.tb00121.x] [PubMed] [Google Scholar]
3. Rai S, Vasava H, Upadhaya D. Bacterial Lipase: A Review. Studies in Indian Place Names. 2020; 40(71): 200-8. [Google Scholar]
4. Hasan F, Shah AA, Hameed A. Industrial applications of microbial lipases.Enzyme and Microbial technology. 2006; 39(2): 235-51. [DOI:10.1016/j.enzmictec.2005.10.016] [Google Scholar]
5. Abdel-Raouf N, Al-Homaidan A, Ibraheem I. Microalgae, and wastewater treatment. Saudi journal of biological sciences. 2012; 19(3): 257-75. [DOI:10.1016/j.sjbs.2012.04.005] [PubMed] [Google Scholar]
6. Chipasa K, Mędrzycka K. Behavior of lipids in biological wastewater treatment processes. Journal of industrial microbiology and biotechnology. 2006; 33(8): 635-45. [DOI:10.1007/s10295-006-0099-y] [PubMed] [Google Scholar]
7. Grady Jr CL, Daigger GT, Love NG, Filipe CD. Biological wastewater treatment. CRC press; 2011. [DOI:10.1201/b13775] [Google Scholar]
8. Ali CH, Qureshi AS, Mbadinga SM, Liu J-F, Yang S-Z, Mu B-Z. Biodiesel production from waste cooking oil using onsite produced purified lipase from Pseudomonas aeruginosa FW_SH-1: Central composite design approach. Renewable energy. 2017; 109: 93-100. [DOI:10.1016/j.renene.2017.03.018] [Google Scholar]
9. Nadeem M, Baig S, Qurat-ul-Ain S, Qazi J. Microbial production of alkaline proteases by locally isolated Bacillus subtilis PCSIR-5. Pakistan Journal of Zoology (Pakistan). 2006; 39(2): 109-114. [Google Scholar]
10. Shivasharana C, Naik GR. Ecofriendly applications of thermostable alkaline protease produced from a Bacillus sp. JB-99 under solid-state fermentation. International Journal of Environmental Sciences. 2012; 3(3): 956-64. [Google Scholar]
11. Esmaeili D, Daymad SF, Neshani A, Rashki S, Marzhoseyni Z, Khaledi A. Alerting prevalence of MBLs producing Pseudomonas aeruginosa isolates. Gene Reports. 2019; 16: 100460 [DOI:10.1016/j.genrep.2019.100460] [Google Scholar]
12. Zhang Y. I-TASSER server for protein 3D structure prediction. BMC bioinformatics. 2008; 9(1): 40. doi: 10.1186/1471-2105-9-40. [DOI:10.1186/1471-2105-9-40] [PubMed] [Google Scholar]
13. Hodaei MH, Anduhjerdi RB, Mehrabadi JF, Esmaeili D. Cloning and expression of the L1 immunogenic protein of human papillomavirus genotype 16 by using Lactobacillus expression system. Gene Reports. 2019; 17: 100521. [DOI:10.1016/j.genrep.2019.100521] [Google Scholar]
14. Sen TZ, Jernigan RL, Garnier J, Kloczkowski A. GOR V server for protein secondary structure prediction. Bioinformatics. 2005; 21(11): 2787-8. [DOI:10.1093/bioinformatics/bti408] [PubMed] [Google Scholar]
15. MohabatiMobarez A, Salmanian AH, Hosseini AZ, Esmaeili D. Clearance of Helicobacter pylori with formulation rCagA and LPS in a mouse model. Gene Reports. 2020; 19: 100588. [DOI:10.1016/j.genrep.2020.100588] [Google Scholar]
16. Artimo P, Jonnalagedda M, Arnold K, Baratin D, Csardi G, De Castro E, et al. ExPASy: SIB bioinformatics resource portal. Nucleic acids research. 2012; 40(W1): W597-W603. [DOI:10.1093/nar/gks400] [PubMed] [Google Scholar]

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