Characterization of a novel SGNH-type esterase from Lactobacillus plantarum

International Journal of Biological Macromolecules

Volumn 96, Issue , 2017, Pages 560-568

  Kim, Yonggyu ^a,b   Ryu, Bum Han ^a,b   Kim, Jimin ^a   Yoo, Wanki ^a,b   An, Deu Rae ^a,b   Kim, Boo Young ^a   Kwon, Sena ^a   Lee, Sojeong ^a   Wang, Ying ^a   Kim, Kyeong Kyu ^b   Kim, T Doohun ^a  

^a Sookmyung Women's University   (South Korea)

^b Sungkyunkwan University School of Medicine   (South Korea)

Author keywords

Lactobacillus plantarum; LpSGNH1; SGNH esterase

Indexed keywords

7 AMINOCEPHALOSPORANIC ACID; ACETYLALGINATE; ACETYLXYLAN; CEFOTAXIME; ESTERASE; GLUCOSE PENTAACETATE; KETOPROFEN ACETATE; LACTIC ACID; SGNH1 ESTERASE; UNCLASSIFIED DRUG; IMMOBILIZED ENZYME;

ARTICLE; BACTERIAL STRAIN; BACTERIUM IDENTIFICATION; BIOTECHNOLOGY; CIRCULAR DICHROISM; CONTROLLED STUDY; DEACETYLATION; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME KINETICS; FERMENTATION; FLUORESCENCE; GEL FILTRATION CHROMATOGRAPHY; LACTOBACILLUS PLANTARUM; LACTOBACILLUS PLANTARUM WCFS1 STRAIN; MASS SPECTROMETRY; NONHUMAN; PHYLOGENY; PROTEIN AGGREGATION; RECYCLING; SEQUENCE ANALYSIS; THERMOSTABILITY; AMINO ACID SEQUENCE; CHEMISTRY; ENZYMOLOGY; METABOLISM;

AMINO ACID SEQUENCE; ENZYMES, IMMOBILIZED; ESTERASES; LACTOBACILLUS PLANTARUM; SEQUENCE ANALYSIS;

EID: 85007574969     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2016.12.061     Document Type: Article

References (46)

1. [1] Pedersen, M.B., Iversen, S.L., Sørensen, K.I., Johansen, E., The long and winding road from the research laboratory to industrial applications of lactic acid bacteria. FEMS Microbiol. Rev. 29 (2005), 611–624.
2. [2] Nga, B.H., Genome analysis of lactic acid bacteria in food fermentations and biotechnological applications. Curr. Opin. Microbiol. 8 (2005), 307–312.
3. [3] Bermúdez-Humarán, L.G., Aubry, C., Motta, J.P., Deraison, C., Steidler, L., Vergnolle, N., Chatel, J.M., Langella, P., Engineering lactococci and lactobacilli for human health. Curr. Opin. Microbiol. 16 (2013), 278–283.
4. [4] Charng, Y.C., Lin, C.C., Hsu, C.H., Inhibition of allergen-induced airway inflammation and hyperreactivity by recombinant lactic-acid bacteria. Vaccine 24 (2006), 5931–5936.
5. [5] Tsai, Y.T., Cheng, P.C., Pan, T.M., Anti-obesity effects of gut microbiota are associated with lactic acid bacteria. Appl. Microbiol. Biotechnol. 98 (2014), 1–10.
6. [6] Douillard, F.P., de Vos, W.M., Functional genomics of lactic acid bacteria: from food to health. Microb. Cell Fact., 13, 2014, S8.
7. [7] Schroeter, J., Klaenhammer, T., Genomics of lactic acid bacteria. FEMS Microbiol. Lett. 292 (2009), 1–6.
8. [8] Siezen, R.J., van Hylckama Vlieg, J.E., Genomic diversity and versatility of Lactobacillus plantarum, a natural metabolic engineer. Microb. Cell Fact., 10, 2011, S3.
9. [9] Kleerebezem, M., Boekhorst, J., van Kranenburg, R., Molenaar, D., Kuipers, O.P., Leer, R., Tarchini, R., Peters, S.A., Sandbrink, H.M., Fiers, M.W., Stiekema, W., Lankhorst, R.M., Bron, P.A., Hoffer, S.M., Groot, M.N., Kerkhoven, R., de Vries, M., Ursing, B., de Vos, W.M., Siezen, R.J., Complete genome sequence of Lactobacillus plantarum WCFS1. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 1990–1995.
10. [10] Zhang, Z.Y., Liu, C., Zhu, Y.Z., Zhong, Y., Zhu, Y.Q., Zheng, H.J., Zhao, G.P., Wang, S.Y., Guo, X.K., Complete genome sequence of Lactobacillus plantarum JDM1. J. Bacteriol. 191 (2009), 5020–5021.
11. [11] Wang, Y., Chen, C., Ai, L., Zhou, F., Zhou, Z., Wang, L., Zhang, H., Chen, W., Guo, B., Complete genome sequence of the probiotic Lactobacillus plantarum ST-III. J. Bacteriol. 193 (2011), 313–314.
12. [12] Siezen, R.J., van Enckevort, F.H., Kleerebezem, M., Teusink, B., Genome data mining of lactic acid bacteria: the impact of bioinformatics. Curr. Opin. Biotechnol. 15 (2004), 105–115.
13. [13] Flores, M., Toldrá, F., Microbial enzymatic activities for improved fermented meats. Trends Food Sci. Technol. 22 (2011), 81–90.
14. [14] McFeeters, R.F., Fermentation microorganisms and flavour changes in fermented foods. J. Food Sci. 69 (2004), 35–37.
15. [15] Carroll, A.L., Desai, S.H., Atsumi, S., Microbial production of scent and flavor compounds. Curr. Opin. Biotechnol. 37 (2016), 8–15.
16. [16] Stergiou, P.Y., Foukis, A., Filippou, M., Koukouritaki, M., Parapouli, M., Theodorou, L.G., Hatziloukas, E., Afendra, A., Pandey, A., Papamichael, E.M., Advances in lipase-catalyzed esterification reactions. Biotechnol. Adv. 31 (2013), 1846–1859.
17. [17] Chen, Y., Black, D.S., Reilly, P.J., Carboxylic ester hydrolases: classification and database derived from their primary secondary, and tertiary structures. Protein Sci. 25 (2016), 1942–1953.
18. [18] Akoh, C.C., Lee, G.C., Liaw, Y.C., Huang, T.H., Shaw, J.F., GDSL family of serine esterases/lipases. Prog. Lipid Res. 43 (2004), 534–552.
19. [19] Ryu, B.H., Nguyen, D.D., Ngo, T.D., Oh, C., Pandian, R., Kim, K.K., Kim, T.D., Crystallization and preliminary X-ray analysis of a highly stable novel SGNH hydrolase (Est24) from Sinorhizobium meliloti. Acta Crystallogr. F Struct. Biol. Commun. 70 (2014), 193–195.
20. [20] Wang, G., Meng, K., Luo, H., Wang, Y., Huang, H., Shi, P., Pan, X., Yang, P., Yao, B., Molecular cloning and characterization of a novel SGNH arylesterase from the goat rumen contents. Appl. Microbiol. Biotechnol. 91 (2011), 1561–1570.
21. [21] Leščić Ašler, I., Ivić, N., Kovačić, F., Schell, S., Knorr, J., Krauss, U., Wilhelm, S., Kojić-Prodić, B., Jaeger, K.E., Probing enzyme promiscuity of SGNH hydrolases. Chembiochem 11 (2010), 2158–2167.
22. [22] Antonopoulou, I., Varriale, S., Topakas, E., Rova, U., Christakopoulos, P., Faraco, V., Enzymatic synthesis of bioactive compounds with high potential for cosmeceutical application. Appl. Microbiol. Biotechnol. 100 (2016), 6519–6543.
23. [23] Ding, J.M., Yu, T.T., Han, N.Y., Yu, J.L., Li, J.J., Yang, Y.J., Tang, X.H., Xu, B., Zhou, J.P., Tang, H.Z., Huang, Z.X., Identification and characterization of a new 7-aminocephalosporanic acid deacetylase from thermophilic bacterium Alicyclobacillus tengchongensis. J. Bacteriol. 198 (2015), 311–320.
24. [24] Oh, C., Ryu, B.H., An, D.R., Nguyen, D.D., Yoo, W., Kim, T., Ngo, T.D., Kim, H.S., Kim, K.K., Kim, T.D., Structural and biochemical characterization of an octameric carbohydrate acetylesterase from Sinorhizobium meliloti. FEBS Lett. 590 (2016), 1242–1252.
25. [25] Ngo, T.D., Ryu, B.H., Ju, H., Jang, E., Kim, K.K., Kim, T.D., Crystallographic analysis and biochemical applications of a novel penicillin-binding protein/β-lactamase homologue from a metagenomic library. Acta Crystallogr. D Biol. Crystallogr. 70 (2014), 2455–2466.
26. [26] Kim, K., Ryu, B.H., Kim, S.S., An, D.R., Ngo, T.D., Pandian, R., Kim, K.K., Kim, T.D., Structural and biochemical characterization of a carbohydrate acetylesterase from Sinorhizobium meliloti 1021. FEBS Lett. 589 (2015), 117–122.
27. [27] Ju, H., Ryu, B.H., Kim, T.D., Identification characterization, immobilization of a novel type hydrolase (LmH) from Listeria monocytogenes. Int. J. Biol. Macromol. 72 (2015), 63–70.
28. [28] Ngo, T.D., Ryu, B.H., Ju, H., Jang, E., Park, K., Kim, K.K., Kim, T.D., Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library. Acta Crystallogr. D Biol. Crystallogr. 69 (2013), 1726–1737.
29. [29] Sievers, F., Wilm, A., Dineen, D., Gibson, T.J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Söding, J., Thompson, J.D., Higgins, D.G., Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol., 7, 2011, 539.
30. [30] Gouet, P., Robert, X., Courcelle, E., ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31 (2003), 3320–3323.
31. [31] Tamura, K., Stecher, G., Peterson, D., Filipski, A., Kumar, S., MEGA6: molecular evolutionary genetics analysis version 6.0. Mol. Biol. Evol. 30 (2013), 2725–2729.
32. [32] Esteban-Torres, M., Mancheño, J.M., de las Rivas, B., Muñoz, R., Characterization of a cold-active esterase from Lactobacillus plantarum suitable for food fermentations. J. Agric. Food Chem. 62 (2014), 5126–5132.
33. [33] Navarro-González, I., Alvaro, S.F., Francisco, G.C., Overexpression purification, and biochemical characterization of the esterase Est0796 from Lactobacillus plantarum WCFS1. Mol. Biotechnol. 54 (2013), 651–660.
34. [34] Esteban-Torres, M., Barcenilla, J.M., Mancheño, J.M., de las Rivas, B., Muñoz, R., Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters. J. Agric. Food Chem. 62 (2014), 5118–5125.
35. [35] Siezen, R.J., van Hylckama Vlieg, J.E., Genomic diversity and versatility of Lactobacillus plantarum, a natural metabolic engineer. Microb. Cell Fact., 10, 2011, S3.
36. [36] Rodríguez, H., Curiel, J.A., Landete, J.M., de las Rivas, B., López de Felipe, F., Gómez-Cordovés, C., Mancheño, J.M., Muñoz, R., Food phenolics and lactic acid bacteria. Int. J. Food Microbiol. 132 (2009), 79–90.
37. [37] Sumby, K.M., Grbin, P.R., Jiranek, V., Characterization of EstCOo8 and EstC34 intracellular esterases, from the wine-associated lactic acid bacteria Oenococcus oeni and Lactobacillus hilgardii. J. Appl. Microbiol. 114 (2013), 413–422.
38. [38] Ryu, B.H., Ngo, T.D., Yoo, W., Lee, S., Kim, B.Y., Lee, E., Kim, K.K., Kim, T.D., Biochemical and structural analysis of a novel esterase from caulobacter crescentus related to Penicillin-Binding Protein (PBP). Sci. Rep., 6, 2016, 37978.
39. [39] Zheng, F., Huang, J., Yin, Y., Ding, S., A novel neutral xylanase with high SDS resistance from Volvariella volvacea: characterization and its synergistic hydrolysis of wheat bran with acetyl xylan esterase. J. Ind. Microbiol. Biotechnol. 40 (2013), 1083–1093.
40. [40] Zhang, J., Siika-Aho, M., Tenkanen, M., Viikari, L., The role of acetyl xylan esterase in the solubilization of xylan and enzymatic hydrolysis of wheat straw and giant reed. Biotechnol. Biofuels, 4, 2011, 60.
41. [41] Bommarius, A.S., Paye, M.F., Stabilizing biocatalysts. Chem. Soc. Rev. 42 (2013), 6534–6565.
42. [42] Sheldon, R.A., Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl. Microbiol. Biotechnol. 92 (2011), 467–477.
43. [43] Kim, S., Bae, S.Y., Lee, B.Y., Kim, T.D., Coaggregation of amyloid fibrils for the preparation of stable and immobilized enzymes. Anal. Biochem. 421 (2012), 776–778.
44. [44] Kim, S., Bae, S.Y., Kim, S.J., Ngo, T.D., Kim, K.K., Kim, T.D., Characterization amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262. Int. J. Biol. Macromol. 50 (2012), 103–111.
45. [45] Bae, S.Y., Ryu, B.H., Jang, E., Kim, S., Kim, T.D., Characterization and immobilization of a novel SGNH hydrolase (Est24) from Sinorhizobium meliloti. Appl. Microbiol. Biotechnol. 97 (2013), 1637–1647.
46. [46] Akoh, C.C., Lee, G.C., Liaw, Y.C., Huang, T.H., Shaw, J.F., GDSL family of serine esterases/lipases. Prog. Lipid Res. 43 (2004), 534–552.