Biotechnology and Bioprocess Engineering

, Volume 8, Issue 2, pp 106–111 | Cite as

Transglycosylation reaction and raw starch hydrolysis by novel carbohydrolase fromLipomyces starkeyi

  • Jin Ha Lee
  • Sun Ok Lee
  • Gwang Ok Lee
  • Eun Seong Seo
  • Suk Sang Chang
  • Sun Kyun Yoo
  • Do Won Kim
  • Donal F. Day
  • Doman Kim


A novel carbohydrolase, which is a DXAMase, containing both dextranase and amylase equivalent activities, was purified fromLipomyces starkeyi KSM22. The purified DXAMase was also found to hydrolyze cellobiose, gentiobiose, trehalose and melezitose, while disproportionation reactions were exhibited with various di-and tri-saccharides, such as maltose, isomaltose, gentiobiose, kojibiose, sophorose, panose, maltotriose, and isomaltotriose with various kinds of oligosaccharides produced as acceptor reaction products. Furthermore, the purified DXAMase hydrolyzed raw waxy rice starch and produced maltodextrin to the extent of 50% as a glucose equivalent.


carbohydrolase Lipomyces starkeyi disproportionation oligosaccharide raw starch 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. [1]
    Barrett, J. F., T. A. Barrett, and R. Curtiss (1987) Purification and partial characterization of the multicomponent dextranase complex ofStreptococcus sorbrinus and the cloning of the dextranase gene.Infect. Immun. 55: 729–802.Google Scholar
  2. [2]
    Koenig, D. and D. F. Day (1988) The purification and characterization of a dextranase fromLipomyces starkeyi.Eur. J. Biochem. 183: 161–167.CrossRefGoogle Scholar
  3. [3]
    Kim, D. and D. F. Day (1995) Isolation of a dextranase constitutive mutant ofLipomyces starkeyi and its use for the production of clinical size dextran.Lett. Appl. Microbiol. 20: 268–270.CrossRefGoogle Scholar
  4. [4]
    Kim, D., H. C. Seo, and D. F. Day (1996) Dextran production byLeuconostoc mesenteroides in the presence of a dextranase producing yeastLipomyces starkeyi.Biotechnol. Tech. 10: 227–232.Google Scholar
  5. [5]
    Kim, D. and D. F. Day (1994) A new process for the production of clinical dextran by mixed-culture fermentation ofLipomyces starkeyi andLeuconostoc mesenteroides.Enzyme Microb. Technol. 16: 844–848.CrossRefGoogle Scholar
  6. [6]
    Ryu, S. J., D. Kim, H. J. Ryu, S. Chiba, A. Kimura, and D. F. Day (2000) Purification and partial characterization of a novel glucanhydrolase fromLipomyces starkeyi KSM 22 and its use for inhibitionof insoluble formation.Biosci. Biotechnol. Biochem. 64: 223–228.CrossRefGoogle Scholar
  7. [7]
    Phaff, H. J. and C. P. Kortzaman (1984) Genus 14.Lipomyces, pp. 252–262. In: R. Kreger-van (ed.),The Yeast: A Taxonomic Study. Elsevier, Amsterdam, The Netherlands.Google Scholar
  8. [8]
    Binder, T. P., G. L. Cote, and J. F. Robyt (1983) Disproportionation reactions catalyzed byLeuconostoc mesenteroides andStreptococcus glucansucrases.Carbohydr. Res. 124: 275–286.CrossRefGoogle Scholar
  9. [9]
    Albenne, C., LK. Skov, O. Mirza, M. Gajhede, G. Potocki-Véronèse, P. Monsan, and M. Remaud-Simound (2002) Maltooligoscaccharide disproportionation reaction: an intrinstic property of amylosucrase fromNeisseria polysaccaharea.FEBS Lett. 527: 67–70.CrossRefGoogle Scholar
  10. [10]
    Oguma, T., K. Tobe, and M. Kobayashi (1994) Purification and properties of a novel enzyme fromBacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosccharides.FEBS Lett. 345: 135–138.CrossRefGoogle Scholar
  11. [11]
    Fox, J. D. and J. F. Robyt (1991) Miniaturization of three carbohydrate analyses using a microsample plate reader.Anal. Biochem. 195: 93–96.CrossRefGoogle Scholar
  12. [12]
    Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 72: 248–254.CrossRefGoogle Scholar
  13. [13]
    Laemmli, U. K. (1970) Cleavage of Structural Proteins During the assembly of the head of bacteriophage T4.Nature 227: 680–685.CrossRefGoogle Scholar
  14. [14]
    Ohnishi, Y., S. Kubo, Ono. Yoshiaki, M. Nozaki, Y. Gonda, H. Okano, T. Matsuya, A. Matsushiro, and T. Morita (1995) Cloning and sequencing of the gene coding for dextranase fromStreptococcus salivaeius.Gene 156: 93–96.CrossRefGoogle Scholar
  15. [15]
    Mukerjea, H., Kim, D., and J. F. Robyt (1996) Simplified and improved methylation analysis of saccharide, using a modified procedure and thin-layer chromatography.Carbohydr. Res. 292: 11–20.Google Scholar
  16. [16]
    Tanirseven, A. and J. F. Robyt (1993) Interpretation of dextransucrase inhibition at high sucrose concentration.Carbohydr. Res. 245: 97–104.CrossRefGoogle Scholar
  17. [17]
    Cho, H. Y., Y. W. Kim, T. J. Kim, H. S. Lee, D. Y. Kim, J. W. Kim, W. Kim, Y. W. Lee, S. B. Lee, and K. H. Park (2000) Molecular characterization of a dimeric intracellular maltogenic amylase ofBacillus SUH4-2.Biochim. Biophys. Acta 1478: 333–340.Google Scholar
  18. [18]
    Gatehouse, J. A., J. Gilroy, M. S. Hoque, and R. R. Croy (1985) Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea (Pisum sativum L.).Biochem. J. 225: 239–247.Google Scholar
  19. [19]
    Yook, C. and J. F. Robyt (2002) Reactions of alpha amylases with starch granules in a aqueous suspension giving products in solution and in a minimum amount of water giving products inside the granule.Carbohydr. Res. 337: 1113–1117.CrossRefGoogle Scholar
  20. [20]
    Koenig, D. W. and D. F. Day (1989) Induction ofLipomyces starkeyi dextranase.Appl. Environ. Microbiol. 23: 2079–2081.Google Scholar

Copyright information

© The Korean Society for Biotechnology and Bioengineering 2003

Authors and Affiliations

  • Jin Ha Lee
    • 1
  • Sun Ok Lee
    • 2
  • Gwang Ok Lee
    • 2
  • Eun Seong Seo
    • 2
  • Suk Sang Chang
    • 4
  • Sun Kyun Yoo
    • 5
  • Do Won Kim
    • 6
  • Donal F. Day
    • 7
  • Doman Kim
    • 1
    • 3
  1. 1.Engineering Research InstituteChonnam National UniversityGwangjuKorea
  2. 2.Department of Material and Biochemical EngineeringChonnam National UniversityGwangjuKorea
  3. 3.Faculty of Applied Chemical Engineering and Research Institute for CatalysisChonnam National UniversityGwangjuKorea
  4. 4.Pohang Accelerator LaboratoryPohang University of Science and TechnologyPohangKorea
  5. 5.Department of Food and BiotechnologyJoong Bu UniversityChungnamKorea
  6. 6.Department of PhysicsKangnung National UniversityKangnungKorea
  7. 7.Audubon Sugar InstituteLouisiana State UniversityBaton RougeUSA

Personalised recommendations