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Research article

References

  1. Almog J, Cohen Y, Azoury M, Hahn TR. 2004. Genipin - a novel fingerprint reagent with colorimetric and fluorogenic activity. J. Forensic Sci. 49: 255-257.
    CrossRef
  2. Bowers EM, Ragland LO, Byers LD. 2007. Salt effects on βglucosidase: pH-profile narrowing. Biochim. Biophys. Acta 1774: 1500-1507.
    CrossRef
  3. Bradford MM. 1 976. A r apid a nd s ensitive m ethod for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72: 248-254.
    CrossRef
  4. Chen M, Qin YQ, Liu ZY, Liu K, Wang FS, Qu YB. 2010. Isolation and characterization of a β-glucosidase from Penicillium decumbens and improving hydrolysis of corncob residue by using it as cellulase supplementation. Enzyme Microb. Technol. 46: 444–449.
    CrossRef
  5. Chen SC, Wu YC, Mi FL, Lin YH, Yu LC, Sung HW. 2004. A novel pH-sensitive hydrogel composed of N,O-carboxymethyl chitosan and alginate cross-linked by genipin for protein drug delivery. J. Control. Release 96: 285-300.
    CrossRef
  6. Chiono V, Pulieri E, Vozzi G, Ciardelli G, Ahluwalia A, Giusti P. 2008. Genipin-crosslinked chitosan/gelatin blends for biomedical applications. J. Mater. Sci. Mater. Med. 19:889-898.
    CrossRef
  7. Diao JS, Wang L, Chen Z, Liu H, Nie GJ, Zheng ZM. 2010. Strain improvement and optimization for β-glucosidase production in Aspergillus niger by low-energy N+ implantation. J. Radiat. Res. Radiat. Process. 28: 345-351. [In Chinese]
  8. Djerassi C, Gray JD, Kincl FA. 1960. Naturally occurring oxygen heterocyclics. IX. Isolation and characterization of genipin. J. Org. Chem. 25: 2174-2177.
    CrossRef
  9. Djerassi C, Nakano T, James AN, Zalkow LH, Eisenbraun EJ, Shoolery JN. 1961. Terpenoids. XLVII. The structure of genipin. J. Org .Chem. 26: 1192-1206.
    CrossRef
  10. Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280:309-316.
  11. Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293: 781-788.
  12. Koo HJ, Song YS, Kim HJ, Lee YH, Hong SM, Kim SJ, et al. 2004. Antiinflammatory effects of genipin, an active principle of gardenia. Eur. J. Pharmacol. 495: 201-208.
    CrossRef
  13. Lee SW, Lim JM, Bhoo SH, Paik YS, Hahn TR. 2003. Colorimetric determination of amino acids using genipin from Gardenia jasminoides. Anal. Chim. Acta 480: 267-274.
    CrossRef
  14. Lineweaver H, Burk D. 1934. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56: 658-666.
    CrossRef
  15. Pei JJ, Pang Q, Zhao LG, Fan S, Shi H. 2012. Thermoanaerobacterium thermosaccharolyticum β-glucosidase: a glucose-tolerant enzyme with high specific activity for cellobiose. Biotechnol. Biofuels 5: 31-40.
    CrossRef
  16. Saibi W, Gargouri A. 2011. Purification and biochemical characterization of an atypical β-glucosidase from Stachybotrys microspora. J. Mol. Catal. B Enzym. 72: 107-115.
    CrossRef
  17. Wang JF, Chen JZ, L iang HZ, Rao J , Li J . 201 0. Purification and characterization of geniposide-hydrolyzing β-glucosidase from Aspergillus niger. Mycosystema 29: 683-690. [In Chinese]
  18. Xu MM, Sun Q, Su J, Wang JF, Xu C, Zhang T, Sun QL. 2008. Microbial transformation of geniposide in Gardenia jasminoides Ellis into genipin by Penicillium nigricans. Enzyme Microb. Technol. 42: 440-444.
    CrossRef
  19. Yang YS, Zhang T, Yu SC, Ding Y, Zhang LY, Qiu C, Jin D. 2011. Transformation of geniposide into genipin by immobilized β-glucosidase in a two-phase aqueous-organic system. Molecules 16: 4295-4304.
    CrossRef
  20. Yuan Y, Chesnutt BM, Utturkar G, Haggard WO, Yang Y, Ong JL, Bumgardner JD. 2007. The effect of cross-linking of chitosan microspheres with genipin on protein release. Carbohyd. Polym. 68: 561-567.
    CrossRef
  21. Zhang CY, Parton LE, Ye CP, Krauss S, Shen R, Lin CT, et al. 2006. Genipin inhibits UCP2-mediated proton leak and acutely reverses obesity- and high glucose-induced beta cell dysfunction in isolated pancreatic islets. Cell Metab. 3: 417-427.
    CrossRef

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Article

Research article

J. Microbiol. Biotechnol. 2014; 24(6): 788-794

Published online June 28, 2014 https://doi.org/10.4014/jmb.1401.01053

Copyright © The Korean Society for Microbiology and Biotechnology.

Purification and Characterization of a β-Glucosidase from Aspergillus niger and Its Application in the Hydrolysis of Geniposide to Genipin

Guohong Gong 1*, Zhiming Zheng 1, Hui Liu 1, Li Wang 1, Jinshan Diao 1, Peng Wang 1 and Genhai Zhao 1

Key Laboratory of Ion Beam Bioengineering, Chinese Academy of Sciences, Hefei 230031, P. R. China

Received: January 27, 2014; Accepted: March 8, 2014

Abstract

An extracellular β-glucosidase from Aspergillus niger Au0847 was purified to homogeneity by
precipitation with ammonium sulfate, anion exchange, and gel filtration. The purified
protein was composed of two subunits with molecular masses of 110 and 120 kDa. Au0847
β-glucosidase exhibited relatively high thermostability and pH stability, and its highest
activity was obtained at 65°C and pH 4.6, respectively. As a potential metalloprotein, its
enzymatic activity was potently stimulated by manganese ion and DTT. The β-glucosidase
displayed avid affinity and high catalytic efficiency for geniposide. Au0847 β-glucosidase has
potential value as an industrial enzyme for the hydrolysis of geniposide to genipin.

Keywords: Aspergillus niger, β-glucosidase, Affinity, Geniposide, Genipin

References

  1. Almog J, Cohen Y, Azoury M, Hahn TR. 2004. Genipin - a novel fingerprint reagent with colorimetric and fluorogenic activity. J. Forensic Sci. 49: 255-257.
    CrossRef
  2. Bowers EM, Ragland LO, Byers LD. 2007. Salt effects on βglucosidase: pH-profile narrowing. Biochim. Biophys. Acta 1774: 1500-1507.
    CrossRef
  3. Bradford MM. 1 976. A r apid a nd s ensitive m ethod for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72: 248-254.
    CrossRef
  4. Chen M, Qin YQ, Liu ZY, Liu K, Wang FS, Qu YB. 2010. Isolation and characterization of a β-glucosidase from Penicillium decumbens and improving hydrolysis of corncob residue by using it as cellulase supplementation. Enzyme Microb. Technol. 46: 444–449.
    CrossRef
  5. Chen SC, Wu YC, Mi FL, Lin YH, Yu LC, Sung HW. 2004. A novel pH-sensitive hydrogel composed of N,O-carboxymethyl chitosan and alginate cross-linked by genipin for protein drug delivery. J. Control. Release 96: 285-300.
    CrossRef
  6. Chiono V, Pulieri E, Vozzi G, Ciardelli G, Ahluwalia A, Giusti P. 2008. Genipin-crosslinked chitosan/gelatin blends for biomedical applications. J. Mater. Sci. Mater. Med. 19:889-898.
    CrossRef
  7. Diao JS, Wang L, Chen Z, Liu H, Nie GJ, Zheng ZM. 2010. Strain improvement and optimization for β-glucosidase production in Aspergillus niger by low-energy N+ implantation. J. Radiat. Res. Radiat. Process. 28: 345-351. [In Chinese]
  8. Djerassi C, Gray JD, Kincl FA. 1960. Naturally occurring oxygen heterocyclics. IX. Isolation and characterization of genipin. J. Org. Chem. 25: 2174-2177.
    CrossRef
  9. Djerassi C, Nakano T, James AN, Zalkow LH, Eisenbraun EJ, Shoolery JN. 1961. Terpenoids. XLVII. The structure of genipin. J. Org .Chem. 26: 1192-1206.
    CrossRef
  10. Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280:309-316.
  11. Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293: 781-788.
  12. Koo HJ, Song YS, Kim HJ, Lee YH, Hong SM, Kim SJ, et al. 2004. Antiinflammatory effects of genipin, an active principle of gardenia. Eur. J. Pharmacol. 495: 201-208.
    CrossRef
  13. Lee SW, Lim JM, Bhoo SH, Paik YS, Hahn TR. 2003. Colorimetric determination of amino acids using genipin from Gardenia jasminoides. Anal. Chim. Acta 480: 267-274.
    CrossRef
  14. Lineweaver H, Burk D. 1934. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56: 658-666.
    CrossRef
  15. Pei JJ, Pang Q, Zhao LG, Fan S, Shi H. 2012. Thermoanaerobacterium thermosaccharolyticum β-glucosidase: a glucose-tolerant enzyme with high specific activity for cellobiose. Biotechnol. Biofuels 5: 31-40.
    CrossRef
  16. Saibi W, Gargouri A. 2011. Purification and biochemical characterization of an atypical β-glucosidase from Stachybotrys microspora. J. Mol. Catal. B Enzym. 72: 107-115.
    CrossRef
  17. Wang JF, Chen JZ, L iang HZ, Rao J , Li J . 201 0. Purification and characterization of geniposide-hydrolyzing β-glucosidase from Aspergillus niger. Mycosystema 29: 683-690. [In Chinese]
  18. Xu MM, Sun Q, Su J, Wang JF, Xu C, Zhang T, Sun QL. 2008. Microbial transformation of geniposide in Gardenia jasminoides Ellis into genipin by Penicillium nigricans. Enzyme Microb. Technol. 42: 440-444.
    CrossRef
  19. Yang YS, Zhang T, Yu SC, Ding Y, Zhang LY, Qiu C, Jin D. 2011. Transformation of geniposide into genipin by immobilized β-glucosidase in a two-phase aqueous-organic system. Molecules 16: 4295-4304.
    CrossRef
  20. Yuan Y, Chesnutt BM, Utturkar G, Haggard WO, Yang Y, Ong JL, Bumgardner JD. 2007. The effect of cross-linking of chitosan microspheres with genipin on protein release. Carbohyd. Polym. 68: 561-567.
    CrossRef
  21. Zhang CY, Parton LE, Ye CP, Krauss S, Shen R, Lin CT, et al. 2006. Genipin inhibits UCP2-mediated proton leak and acutely reverses obesity- and high glucose-induced beta cell dysfunction in isolated pancreatic islets. Cell Metab. 3: 417-427.
    CrossRef