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Improving the Acid Resistance of Tannase TanBLp (AB379685) from Lactobacillus plantarum ATCC14917T by Site-Specific Mutagenesis

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Abstract

Tannin acyl hydrolase referred commonly as tannase catalyzes the hydrolysis of the galloyl ester bond of tannin to release gallic acid. The tannase TanBLp which cloned from Lactobacillus plantarum ATCC14917T has high activity in the pH range (7.0–9.0) at 40 °C, it would be detrimental to the utilization at acidic environment. The catalytic sites and stability of TanBLp were analyzed using bioinformatics and site-specific mutagenesis. The results reiterated that the amino acid residues Ala164, Lys343, Glu357, Asp421 and His451 had played an important role in maintaining the activity. The optimum pH of mutants V75A, G77A, N94A, A164S and F243A were shifted from 8.0 to 6.0, and mutant V75A has the highest pH stability and activity at acidic conditions than other mutants, which was more suitable for industrial application to manufacture gallic acid. This study was of great significance to promote the industrialization and efficient utilization of tannase TanBLp.

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References

  1. Zhu X, Hou X, Ma B, Xu H, Yang Y (2019) Chitosan/gallnut tannins composite fiber with improved tensile, antibacterial and fluorescence properties. Carbohydr Polym 226:115311

    Article  CAS  Google Scholar 

  2. Watrelot AA, Guernevé CL, Halle H, Meudec E, Cheynier V (2017) Multimethod approach for extensive characterization of gallnut tannin extracts. J Agric Food Chem 68:13426–13438

    Article  Google Scholar 

  3. Wu Y, Xia X, Dong S, Zhou K (2017) Industrial scale extraction and stripping devices for continuous recovery of gallic acid from Chinese nutgall processing wastewater. Environ Eng Res 22:288–293

    Article  Google Scholar 

  4. Chávez-González M, Rodríguez-Durán LV, Balagurusamy N, Prado-Barragán A, Rodríguez R, Contreras JC, Aguilar CN (2012) Biotechnological advances and challenges of tannase: an overview. Food Bioprocess Technol 5:445–459

    Article  Google Scholar 

  5. Jana A, Halder SK, Banerjee A, Paul T, Pati BR, Mondal KC, Mohapatra PKD (2014) Biosynthesis, structural architecture and biotechnological potential of bacterial tannase: a molecular advancement. Bioresour Technol 157:327–340

    Article  CAS  Google Scholar 

  6. Abdel-Naby MA, El-Tanash AB, Sherief ADA (2016) Structural characterization, catalytic, kinetic and thermodynamic properties of Aspergillus oryzae tannase. Int J Biol Macromol 92:803–811

    Article  CAS  Google Scholar 

  7. Aguilar CN, Rodríguez R, Gutiérrez-Sánchez G, Augur C, Favela-Torres E, Prado-Barragan LA, Ramírez-Coronel A, Contreras-Esquivel JC (2007) Microbial tannases: advances and perspectives. Appl Microbiol Biotechnol 76:47–59

    Article  CAS  Google Scholar 

  8. Begovic S, Duzic E (1977) Purifying of tannase from the mucous membrane of the rumen and small intestines of bovines and a comparison of activity. Vetenaria (Yugoslavia) 26:227–233

    CAS  Google Scholar 

  9. Govindarajan RK, Revathi S, Rameshkumar N, Krishnan M, Kayalvizhi N (2016) Microbial tannase: current perspectives and biotechnological advances. Biocatal Agric Biotechnol 6:168–175

    Article  Google Scholar 

  10. Dai XL, Liu YJ, Zhuang JH, Yao SB, Liu L, Jiang XL, Zhou K, Wang YS, Xie DY, Bennetzen JL, Gao LP, Xia T (2020) Discovery and characterization of tannase genes in plants: roles in hydrolysis of tannins. New Phytol 226:1104–1116

    Article  CAS  Google Scholar 

  11. Chhokar V, Sharma J, Kumar A, Beniwal V (2013) Recent advances in industrial application of tannases: a review. Recent Patents Biotechnol 7:228–233

    Article  Google Scholar 

  12. Sharma KP, John PJ, Goswami P, Soni M (2017) Enzymatic synthesis of gallic acid from tannic acid with an inducible hydrolase of Enterobacter spp. Biocatal Biotransform 35:177–184

    Article  CAS  Google Scholar 

  13. Yao J, Guo GS, Ren GH, Liu YH (2014) Production, characterization and applications of tannase. J Mol Catal B Enzym 101:137–147

    Article  CAS  Google Scholar 

  14. Govindarajan RK, Mathivanan K, Rameshkumar N, Shyu DJH, Krishnan M, Kayalvizhi N (2019) Purification, structural characterization and biotechnological potential of tannase enzyme produced by Enterobacter cloacae strain 41. Process Biochem 77:37–47

    Article  Google Scholar 

  15. Fuentes-Garibay JA, Aguilar CN, Rodríguez-Herrera R, Guerrero-Olazarán M, Viader-Salvadó JM (2015) Tannase sequence from a xerophilic Aspergillus niger strain and production of the enzyme in Pichia pastoris. Mol Biotechnol 57:439–447

    Article  CAS  Google Scholar 

  16. Venu Gopal KS, Cherita C, Anu Appaiah KA (2016) Yeast as a potential candidate for tannase production: a review. Curr Biochem Eng 3:82–88

    Article  Google Scholar 

  17. Matoba Y, Tanaka N, Noda M, Higashikawa F, Sugiyama M (2013) Crystallographic and mutational analyses of tannase from Lactobacillus plantarum. Proteins 81:2052–2058

    Article  CAS  Google Scholar 

  18. Aguilar-Zarate P, Cruz-Hernandez MA, Montanez JC, Belmares-Cerda RE, Aguilar CN (2014) Enhancement of tannase production by Lactobacillus plantarum CIR1: validation in gas-lift bioreactor. Bioprocess Biosyst Eng 37:2305–2316

    Article  CAS  Google Scholar 

  19. Aishwarya SS, Selvarajan E, Iyappan S, Rajnish KN (2019) Recombinant l -asparaginase ii from Lactobacillus casei subsp. casei ATCC 393 and its anticancer activity. Indian J Microbiol 59:313–320

    Article  CAS  Google Scholar 

  20. Zhang L, Zhao B, Liu CJ, Yang E (2020) Optimization of biosynthesis conditions for the production of exopolysaccharides by lactobacillus plantarum sp8 and the exopolysaccharides antioxidant activity test. Indian J Microbiol 60:334–345

    Article  CAS  Google Scholar 

  21. Rivas BDL, Rodríguez H, Anguita J, Muoz R (2019) Bacterial tannases: classification and biochemical properties. Appl Microbiol Biotechnol 103:603–623

    Article  Google Scholar 

  22. Ueda S, Nomoto R, Yoshida K, Osawa R (2014) Comparison of three tannases cloned from closely related Lactobacillus species: L. plantarum, L. paraplantarum, and L. pentosus. BMC Microbiol 14:87

    Article  Google Scholar 

  23. Iwamoto K, Tsuruta H, Nishitaini Y, Osawa R (2008) Identification and cloning of a gene encoding tannase (tannin acylhydrolase) from Lactobacillus plantarum ATCC 14917T. Syst Appl Microbiol 31:269–277

    Article  CAS  Google Scholar 

  24. Ren B, Wu M, Qin W, Peng X, Chen Q (2013) Crystal structure of tannase from Lactobacillus plantarum. J Mol Biol 425:2737–2751

    Article  CAS  Google Scholar 

  25. Seeliger D, Groot BLD (2010) Ligand docking and binding site analysis with PyMOL and Autodock/Vina. J Comput Aided Mol Des 24:417–422

    Article  CAS  Google Scholar 

  26. Mahmoud AE, Fathy SA, Rashad MM (2018) Purification and characterization of a novel tannase produced by Kluyveromyces marxianus using olive pomace as solid support, and its promising role in gallic acid production. Int J Biol Macromol 107:2342–2350

    Article  CAS  Google Scholar 

  27. Tseng YH, Hsieh CC, Kuo TY, Liu JR, Hsu TY, Hsieh SC (2019) Construction of a lactobacillus plantarum strain expressing the capsid protein of porcine circovirus type 2d (pcv2d) as an oral vaccine. Indian J Microbiol 59:490–499

    Article  Google Scholar 

  28. Chaitanyakumar A, Anbalagan M (2016) Expression, purification and immobilization of tannase from Staphylococcus lugdunensis MTCC 3614. AMB Express 6:89

    Article  Google Scholar 

  29. Miyazaki K, Takenouchi M (2002) Creating random mutagenesis libraries using megaprimer PCR of whole plasmid. Biotechniques 33:1036–1038

    Article  Google Scholar 

  30. Pulido RP, Omar NB, Abriouel H, López RL, Gálvez A (2007) Characterization of lactobacilli isolated from caper berry fermentations. J Appl Microbiol 102:583–590

    Article  CAS  Google Scholar 

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Funding

National Key R&D Program of China (2019YFC1604903, 2019YFC1604905), National Natural Science Foundation of China (21808052, 31971042), Science and Technology Department of Hunan Province (2020NK4194, 2018RS3086, 2019GK4018), Open Research Project of State Key Laboratory Breeding Base of Crop Germplasm Innovation and Resource Utilization (18KFXM11), Training Program for Excellent Young Innovators of Changsha (kq2009019) and “Double First-Class” construction project of Hunan Agricultural University (SYL201802002) funded this work.

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Author notes

  1. Hu Pan, Jingjing Zhan and Hui Yang contributed equally to this article.

Authors and Affiliations

  1. College of Bioscience and Biotechnology, Hunan Agricultural University, Changsha, China

    Hu Pan, Jingjing Zhan, Hui Yang, Chong Wang, Huhu Liu, Haiyan Zhou, Xiangyang Lu & Yun Tian

  2. Institute of Agricultural Product Quality Standard and Testing Research, Tibet Academy of Agricultural and Animal Husbandry Sciences, Lhasa, China

    Hu Pan

  3. College of Food Science and Technology, Hunan Agricultural University, Changsha, China

    Hui Zhou & Xiaojun Su

Authors
  1. Hu Pan
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  2. Jingjing Zhan
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  10. Yun Tian
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Contributions

HP, JZ and HY conducted most of the experiments and contributed equally to this work. YT and HZ conceived and designed the study. CW and HL designed the primer by site-directed mutagenesis. HZ, XS and XL predicted the catalytic sites of tannase TanBLp using bioinformatics. HP, JZ and HY wrote the paper. All authors discussed the data and commented on the manuscript.

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Correspondence to Yun Tian.

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Pan, H., Zhan, J., Yang, H. et al. Improving the Acid Resistance of Tannase TanBLp (AB379685) from Lactobacillus plantarum ATCC14917T by Site-Specific Mutagenesis. Indian J Microbiol 62, 96–102 (2022). https://doi.org/10.1007/s12088-021-00983-x

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