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Food Science and Biotechnology

, Volume 28, Issue 1, pp 165–174 | Cite as

Enzymatic modification of daidzin using heterologously expressed amylosucrase in Bacillus subtilis

  • Eun-Ryoung Kim
  • Chan-Su Rha
  • Young Sung Jung
  • Jung-Min Choi
  • Gi-Tae Kim
  • Dong-Hyun Jung
  • Tae-Jip Kim
  • Dong-Ho Seo
  • Dae-Ok Kim
  • Cheon-Seok ParkEmail author
Article
  • 87 Downloads

Abstract

Amylosucrases (ASase, EC 2.4.1.4) from Deinococcus geothermalis (DGAS) and Neisseria polysaccharea (NPAS) were heterologously expressed in Bacillus subtilis. While DGAS was successfully expressed, NPAS was not. Instead, NPAS was expressed in Escherichia coli. Recombinant DGAS and NPAS were purified using nickel-charged affinity chromatography and employed to modify daidzin to enhance its water solubility and bioavailability. Analyses by LC/MS revealed that the major products of transglycosylation using DGAS were daidzein diglucoside and daidzein triglucoside, whereas that obtained by NPAS was only daidzein diglucoside. The optimal bioconversion conditions for daidzein triglucoside, which was predicted to have the highest water-solubility among the daidzin derivatives, was determined to be 4% (w/v) sucrose and 250 mg/L daidzin in sodium phosphate pH 7.0, with a reaction time of 12 h. Taken together, we suggest that the yield and product specificity of isoflavone daidzin transglycosylation may be modulated by the source of ASase and reaction conditions.

Keywords

Amylosucrase Deinococcus geothermalis Daidzin Transglycosylation Bacillus subtilis 

Notes

Acknowledgements

This work was supported by a National Research Foundation of Korea (NRF) Grant funded by the Korean Government (MEST) (No. 2017R1A2B4004218).

Compliance with ethical standards

Conflict of interest

The authors declare that there are no conflicts of interest.

References

  1. Choi CH, Kim SH, Jang JH, Park JT, Shim JH, Kim YW, Park KH. Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis. J. Sci. Food Agric. 90: 1179–1184 (2010)CrossRefGoogle Scholar
  2. Cho HK, Kim HH, Seo DH, Jung JH, Park JH, Baek NI, Kim MJ, Yoo SH, Cha J, Kim YR. Biosynthesis of (+)-catechin glycosides using recombinant amylosucrase from Deinococcus geothermalis DSM 11300. Enzyme Microb. Technol. 49: 246–253 (2011)CrossRefGoogle Scholar
  3. Delmonte P, Perry J, Rader JI. Determination of isoflavones in dietary supplements containing soy, red clover and kudzu: extraction followed by basic or acid hydrolysis. J. Chromatogr. A 1107: 59–69 (2006)CrossRefGoogle Scholar
  4. De Montalk GP, Remaud-Simeon M, Willemot R, Planchot V, Monsan P. Sequence analysis of the gene encoding amylosucrase from Neisseria polysaccharea and characterization of the recombinant enzyme. J. Bacteriol. 181: 375–381 (1999)Google Scholar
  5. Dillard CJ, German JB. Phytochemicals: nutraceuticals and human health. J. Sci. Food Agric. 80: 1744–1756 (2000)CrossRefGoogle Scholar
  6. Iwashina T. The structure and distribution of the flavonoids in plants. J. Plant Res. 113: 287–299 (2014)CrossRefGoogle Scholar
  7. Jung JH, Seo DH, Ha SJ, Song MC, Cha J, Yoo SH, Kim TJ, Baek NI, Baik MY, Park CS. Enzymatic synthesis of salicin glycosides through transglycosylation catalyzed by amylosucrases from Deinococcus geothermalis and Neisseria polysaccharea. Carbohydr. Res. 344: 1612–1619 (2009)CrossRefGoogle Scholar
  8. Kim MD, Jung DH, Seo DH, Jung JH, Seo EJ, Baek NI, Yoo SH, Park CS. Acceptor specificity of amylosucrase from Deinococcus radiopugnans and its application for synthesis of rutin derivatives. J. Microbiol. Biotechnol. 26: 1845–1854 (2016)CrossRefGoogle Scholar
  9. Kim MD, Seo DH, Jung JH, Jung DH, Joe MH, Lim S, Lee JH, Park CS. Molecular cloning and expression of amylosucrase from highly radiation-resistant Deinococcus radiopugnans. Food Sci. Biotechnol. 23: 2007–2012 (2014)CrossRefGoogle Scholar
  10. Ko JH, Kim BG, Ahn JH. Glycosylation of flavonoids with a glycosyltransferase from Bacillus cereus. FEMS Microbiol. Lett. 258: 263–268 (2006)CrossRefGoogle Scholar
  11. Ko KP. Isoflavones: chemistry, analysis, functions and effects on health and cancer. Asian Pac. J. Cancer Prev. 15: 7001–7010 (2014)CrossRefGoogle Scholar
  12. Kulkarni YA, Garud MS, Oza MJ, Barve KH, Gaikwad AB. Chapter 5—Diabetes, diabetic complications, and flavonoids A2. pp. 77–104. In: Fruits, vegetables, and herbs. Watson R and Preedy VR (eds). Academic Press, Inc., Elsevier, NY, USA.CrossRefGoogle Scholar
  13. Lee JH, Doo EH, Kwon DY, Park JB. Functionalization of isoflavones with enzymes. Food Sci. Biotechnol. 17: 228–233 (2008)Google Scholar
  14. Li D, Park JH, Park JT, Park CS, Park KH. Biotechnological production of highly soluble daidzein glycosides using Thermotoga maritima maltosyltransferase. J. Agric. Food Chem. 52: 2561–2567 (2004a)CrossRefGoogle Scholar
  15. Li D, Park SH, Shim JH, Lee HS, Tang SY, Park CS, Park KH. In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase. Carbohydr. Res. 339: 2789–2797 (2004b)CrossRefGoogle Scholar
  16. Lundemo P. Transglycosylation by glycoside hydrolases-production and modification of alkyl glycosides. PhD thesis, Lund University, Lund, Scania, Sweden (2015)Google Scholar
  17. Park HS, Choi KH, Park YD, Park CS, Cha JH. Enzymatic synthesis of polyphenol glycosides by amylosucrase. J. Life Sci. 21: 1631–1635 (2011)CrossRefGoogle Scholar
  18. Park HS, Kim JE, Park JH, Baek NI, Park CS, Lee HS, Cha JH. Bioconversion of piceid to piceid glucoside using amylosucrase from Alteromonas macleodii deep ecotype. J. Microbiol. Biotechnol. 22: 1698–1704 (2012)CrossRefGoogle Scholar
  19. Plaza M, Pozzo T, Liu J, Gulshan Ara KZ, Turner C, Nordberg Karlsson E. Substituent effects on in vitro antioxidizing properties, stability, and solubility in flavonoids. J. Agric. Food Chem. 62: 3321–3333 (2014)CrossRefGoogle Scholar
  20. Polizzi M, Bommarius A, Broering J, Chaparro-Riggers J. Stability of biocatalysts. Curr. Opin. Chem. Biol. 11: 220–225 (2007)CrossRefGoogle Scholar
  21. Rezvani AH, Overstreet DH., Perfumi M., Massi M. Plant derivatives in the treatment of alcohol dependency. Pharmacol. Biochem. Behav. 75: 593–606 (2003)CrossRefGoogle Scholar
  22. Seo DH, Jung JH, Ha SJ, Song MC, Cha JH, Yoo SH, Kim TJ, Baek NI, Park CS. Highly selective biotransformation of arbutin to arbutin-α-glucoside using amylosucrase from Deinococcus geothermalis DSM 11300. J. Mol. Catal. B-Enzym. 60: 113–118 (2009)CrossRefGoogle Scholar
  23. Seo DH, Jung JH, Ha SJ, Yoo SH, Kim TJ, Cha JH, Park CS. Molecular cloning of the amylosucrase gene from a moderate thermophilic bacterium Deinococcus geothermalis and analysis of its dual enzyme activity. Vol. I, pp. 125–140. In: Carbohydrate-active enzymes. Park KH (ed). Academic Press, Inc., Elsevier, NY, USA (2008)CrossRefGoogle Scholar
  24. Seo DH, Jung JH, Ha SJ, Cho HK, Jung DH, Kim TJ, Baek NI, Yoo SH, Park CS. High-yield enzymatic bioconversion of hydroquinone to α-arbutin, a powerful skin lightening agnet, by amylosucrase. Appl. Microbiol. Biotechnol. 94: 1189–1197 (2012)CrossRefGoogle Scholar
  25. Seo DH, Jung JH, Jung DH, Park SY, Yoo SH, Kim YR, Park CS. An unusual chimeric amylosucrase generated by domain-swapping mutagenesis. Enzyme Microb. Technol. 86: 7–16 (2016)CrossRefGoogle Scholar
  26. Shimoda K, Hamada H. Production of hesperetin glycosides by Xanthomonas campestris and cyclodextrin glucanotransferase and their anti-allergic activities. Nutrients 2: 171–180 (2010a)CrossRefGoogle Scholar
  27. Shimoda K, Hamada H. Synthesis of β-maltooligosaccharides of glycitein and daidzein and their anti-oxidant and anti-allergic activities. Molecules 15: 5153–5161 (2010b)CrossRefGoogle Scholar
  28. Shimoda K, Hamada H, Hamada H. Synthesis of xylooligosaccharides of daidzein and their anti-oxidant and anti-allergic activities. Int. J. Mol. Sci. 12: 5616–5625 (2011)CrossRefGoogle Scholar
  29. Thrane M, Paulsen PV, Orcutt MW, Krieger TM. Chapter 2—Soy Protein: Impacts, Production, and Applications A2. pp. 23-45. In: Sustainable Protein Sources. Wanasundara JPD, Scanlin L (eds). Academic Press, Inc., Elsevier, NY, USA (2017)CrossRefGoogle Scholar
  30. Vacek J, Klejdus B, Lojková L, Kubán V. Current trends in isolation, separation, determination and identification of isoflavones: a review. J. Sep. Sci. 31: 2054–2067 (2008)CrossRefGoogle Scholar
  31. Westers L, Westers H, Quax WJ. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. Biochim. Biophys. Acta-Mol. Cell. 1694: 299–310 (2004)CrossRefGoogle Scholar
  32. Wu L and Birch RG. Characterization of Pantoea dispersa UQ68 J: producer of a highly efficient sucrose isomerase for isomaltulose biosynthesis. J. Appl. Microbiol. 97: 93–103 (2004)CrossRefGoogle Scholar
  33. Wu L and Birch RG. Characterization of the highly effieient sucrose isomerase from Pantoea dispersa UQ68J and cloning of the sucrose isomerase gene. Appl. Environ. Microbiol. 71: 1581–1590 (2005)CrossRefGoogle Scholar

Copyright information

© The Korean Society of Food Science and Technology and Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  • Eun-Ryoung Kim
    • 1
  • Chan-Su Rha
    • 1
  • Young Sung Jung
    • 1
  • Jung-Min Choi
    • 1
  • Gi-Tae Kim
    • 1
  • Dong-Hyun Jung
    • 1
  • Tae-Jip Kim
    • 2
  • Dong-Ho Seo
    • 3
  • Dae-Ok Kim
    • 1
  • Cheon-Seok Park
    • 1
    Email author
  1. 1.Graduate School of Biotechnology and Institute of Life Science and ResourcesKyung Hee UniversityYonginRepublic of Korea
  2. 2.School of Food and Animal ScienceChungbuk National UniversityCheongjuRepublic of Korea
  3. 3.Research Group of HealthcareKorea Food Research InstituteWanjuRepublic of Korea

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