Volume 6, Issue 1 (5-2019)                   NBR 2019, 6(1): 39-49 | Back to browse issues page


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Mortazavi M, Parvaresh N, Torkzadeh M. An enzymatic and bioinformatics study of native cutinase bacteria. NBR 2019; 6 (1) :39-49
URL: http://nbr.khu.ac.ir/article-1-2802-en.html
, m.mortazavi@kgut.ac.ir
Abstract:   (4727 Views)

Cutin is a polymer that is constructed in plants by the condensation and oxidation of fatty acids and plays a key role in the protection of plants against pathogens. Cutinase is a hydrolase enzyme that breaks down the cutin. The purpose of this study was to extract cutin from red apples with oxalate buffer, cutinase enzyme activity assay in LB culture, and bioinformatic analysis. To attain these purposes the cutinase-producing strains that had previously been isolated were inoculated in culture medium containing cutin. After initial culture, the bacteria were cultured in LB medium and cutinase activity was measured using the p-Nitrophenyl butyrate. In order to execute bioinformatic analysis, the isolated sequences of six cutinase-producing bacteria were analyzed based on computational data bases and their phylogenetic trees were prepared. Then, the similarities in the sequences of a large number of cutinase-producing samples were analyzed by drawing the phylogenetic tree. The results showed the separation of cutinase-producing prokaryotes from cutinase-producing eukaryotes. Then, the sequence of 16S rDNA of these cutinase-producing samples as well as the samples we had prepared were evaluated and their phylogenetic relationships were determined. This analysis showed that the new sequence stood alongside the bacterial samples. Thus, our cutinases may be similar with these bacterial cutinases in structure and function.
 

 
 

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Type of Study: Original Article | Subject: Genetics
Received: 2017/04/5 | Revised: 2019/05/5 | Accepted: 2018/09/25 | Published: 2018/04/24 | ePublished: 2018/04/24

References
1. Abou-Zeid, D-M., Müller, R-J. and Deckwer, W-D. 2004. Biodegradation of aliphatic homopolyesters and aliphatic− aromatic copolyesters by anaerobic microorganisms. - Biomacromolecules. 5: 1687-1697. [DOI:10.1021/bm0499334]
2. Calado, C.R., Monteiro, S.M., Cabral, J.M. and Fonseca, L.P. 2002. Effect of pre-fermentation on the production of cutinase by a recombinant Saccharomyces cerevisiae. - J. Biosci. Bioeng. 93: 354-359. [DOI:10.1263/jbb.93.354]
3. Carvalho, C.M., Aires-Barros, M.R. and Cabral, J. 1998. Cutinase structure, function and biocatalytic applications. - Electron. J. Biotechnol. 1: 28-29. [DOI:10.2225/vol1-issue3-fulltext-8]
4. Degani, O., Salman, H., Gepstein, S., Dosoretz, C.G. 2006. Synthesis and characterization of a new cutinase substrate, 4-nitrophenyl (16-methyl sulfone ester) hexadecanoate. - J. Biotechnol. 121: 346-350. [DOI:10.1016/j.jbiotec.2005.08.011]
5. Fich, E.A., Segerson, N.A. and Rose, J.K. 2016. The plant polyester cutin: biosynthesis, structure, and biological roles. - Annu. Rev. Plant Biol. 67: 207-233. [DOI:10.1146/annurev-arplant-043015-111929]
6. Flandrois, J-P., Perrière, G. and Gouy, M. 2015. LeBIBI QBPP: a set of databases and a web tool for automatic phylogenetic analysis of prokaryotic sequences. - BMC bioinformatics.16: 251. [DOI:10.1186/s12859-015-0692-z]
7. Gerard, C.H., Fett, F.W., Osman, F.S. and Moreau, A.R. 1993. Evaluation of cutinase activity of various industrial lipases. - Biotechnol. Appl. Biochem. 17: 181-189.
8. Heredia, A. 2003. Biophysical and biochemical characteristics of cutin, a plant barrier biopolymer. - Biochim. Biophys. Acta 1620: 1-7. [DOI:10.1016/S0304-4165(02)00510-X]
9. Huson, D.H. and Bryant, D. 2006. Application of phylogenetic networks in evolutionary studies. - Mol. Biol. Evol. 23: 254-267. [DOI:10.1093/molbev/msj030]
10. Jelsch, C., Longhi, S. and Cambillau, C. 1998. Packing forces in nine crystal forms of cutinase. -Proteins 31: 320-333. https://doi.org/10.1002/(SICI)1097-0134(19980515)31:3<320::AID-PROT8>3.3.CO;2-R [DOI:10.1002/(SICI)1097-0134(19980515)31:33.3.CO;2-R]
11. Kolattukudy, P., Purdy, R. and Maiti, I. 1981. Cutinases from fungi and pollen. - Methods Enzymol. 71: 652-664. [DOI:10.1016/0076-6879(81)71078-4]
12. Kutschera, U. and Niklas, K. 2007. The epidermal-growth-control theory of stem elongation: an old and a new perspective. - J. Plant Physiol.164: 1395-1409. [DOI:10.1016/j.jplph.2007.08.002]
13. LIN, T.S.and Kolattukudy, P. 1980. Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus. - Eur. J. Biochem.106: 341-351. [DOI:10.1111/j.1432-1033.1980.tb04580.x]
14. Liu, S-H, Zeng, G-M., Niu, Q-Y., Liu, Y., Zhou, L., Jiang, L-H., Tan, X.F., Xu, P., Zhang, C. and Cheng, M. 2017. Bioremediation mechanisms of combined pollution of PAHs and heavy metals by bacteria and fungi: A mini review. - Bioresour Technol. 224: 2 [DOI:10.1016/j.biortech.2016.11.095]
15. Longhi, S., Nicolas, A., Creveld, L., Egmond, M., Verrips, C.T., de Vlieg, J., Martinez, C. and Cambillau, C. 1996. Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. - Proteins 26: 442-458. https://doi.org/10.1002/(SICI)1097-0134(199612)26:4<442::AID-PROT5>3.3.CO;2-H [DOI:10.1002/(SICI)1097-0134(199612)26:43.3.CO;2-H]
16. Martinez, C., de Geus, P., Stanssens, P., Lauwereys, M. and Cambillau, C. 1993. Engineering cysteine mutants to obtain crystallographic phases with a cutinase from Fusarium solani pisi. - Protein Eng. 6: 157-165. [DOI:10.1093/protein/6.2.157]
17. Murphy, C.A., Cameron, J., Huang, S.J. and Vinopal, R.T. 1996. Fusarium polycaprolactone depolymerase is cutinase. - Appl. Environ. Microbiol. 62: 456-460.
18. Okkels, J. 1997. Preparing polypeptide variants with improved functional properties. US patent, 97-09664.
19. Parvaresh, N., Mortazavi, M. and Torkzadeh, M.M. 2017. Isolation and identification of cutinase enzyme production bacteria. - Nova Biol. Reperta 4: 38-46. [DOI:10.21859/acadpub.nbr.4.1.39]
20. Pocalyko, D.J. and Tallman, M. 1998. Effects of amphipaths on the activity and stability of Fusarium solani pisi cutinase. - Enzyme Microb. Technol. 22: 647-651. [DOI:10.1016/S0141-0229(98)00013-1]
21. Raziyafathima, M., Praseetha, P. and Rimal Isaac, R. 2016. Microbial degradation of plastic waste: a review. - J. Pharma. Chem. Biol. Sci. 4: 231-242.
22. Sebastian, J., Chandra, A. and Kolattukudy, P. 1987. Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in the phyllosphere. - J. Bacteriol. 169: 131-136. [DOI:10.1128/jb.169.1.131-136.1987]
23. Sebastião, M., Cabral, J. and Aires‐Barros, M. 1993. Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles. - Biotechnol. Bioeng. 42: 326-332. [DOI:10.1002/bit.260420309]
24. Serrano, M., Coluccia, F., Martha, T., Lhardion, F. and Métraux, J. 2014. The cuticle and plant defense to pathogens. - Front. Plant Sci. 5: 6-13. [DOI:10.3389/fpls.2014.00274]
25. Tenhaken, R., Arnemann, M., Köhler, G. and Barz, W. 1997. Characterization and cloning of cutinase from Ascochyta rabiei. - Z. Naturforsch. C. 52: 197-208. [DOI:10.1515/znc-1997-3-411]
26. Van der Vlugt-Bergmans, C., Wagemakers, C. and Van Kan, J. 1997. Cloning and expression of the cutinase A gene of Botrytis cinerea. - Mol. Plant-Microbe Interact. 10: 21-29. [DOI:10.1094/MPMI.1997.10.1.21]
27. Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., Toyohara, K., Miyamoto, K. Kimura, Y. and Oda, K. 2016. A bacterium that degrades and assimilates poly (ethylene terephthalate). - Science 351: 1196-1199. [DOI:10.1126/science.aad6359]
28. Zhang, Y., Chen, S., Xu, M., Cavoco-Paulo, A., Wu, J. and Chen, J. 2010. Characterization of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins and their potential application in bioscouring. - Appl. Environ. Microbiol. 76: 6870-6876. [DOI:10.1128/AEM.00896-10]

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