Transglycosylation Reaction and Raw Starch Hydrolysis by Novel Carbohydrolase from Lipomyces starkeyi

  • Lee, Jin-Ha (Engineering Research Institute, Chonnam National University) ;
  • Lee, Sun-Ok (Department of Material and Biochemical Engineering, Chonnam National University) ;
  • Lee, Gwang-Ok (Department of Material and Biochemical Engineering, Chonnam National University) ;
  • Seo, Eun-Seong (Department of Material and Biochemical Engineering, Chonnam National University) ;
  • Chang, Suk-Sang (Pohang Accelerator Laboratory, Pohang University of Science and Technology) ;
  • Yoo, Sun-Kyun (Department of Food and Biotechnology, Joong Bu University) ;
  • Kim, Do-Won (Department of Physics, Kangnung National University) ;
  • Donal F. Day (Audubon Sugar Institute, Louisiana State University) ;
  • Kim, Doman (Engineering Research Institute, Faculty of Applied Chemical Engineering and Research Institute for Catalysis, Chonnam National University)
  • Published : 2003.04.01

Abstract

A novel carbohydrolase, which is a DXAMase, containing both dextranase and amylase equivalent activities, was purified from Lipomyces 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.

Keywords

References

  1. Infect. Immun. v.55 Purification and partial characterization of the multicomponent dextranase complex of Streptococcus sorbrinus and the cloning of the dextranase gene Barrett,J.F.;T.A.Barrett;R.Curtiss
  2. Eur. J. Biochem. v.183 The purification and characterization of a dextranase from Lipomyces starkeyi Koenig,D.;D.F.Day
  3. Lett. Appl. Microbiol. v.20 Isolation of a dextranase constitutive mutant of Lipomyces starkeyi and its use for the production of clinical size dextran Kim,D.;D.F.Day https://doi.org/10.1111/j.1472-765X.1995.tb00443.x
  4. Biotechnol. Tech. v.10 Dextran production by Leuconostoc mesenteroides in the presence of a dextranase producing yeast Lipomyces starkeyi Kim,D.;H.C.Seo;D.F.Day
  5. Enzyme Microb. Technol. v.16 A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides Kim,D.;D.F.Day https://doi.org/10.1016/0141-0229(94)90058-2
  6. Biosci. Biotechnol. Biochem. v.64 Purification and partial characterization of a novel glucanhydrolase from Lipomyces starkeyi KSM 22 and its use for inhibition of insoluble formation Ryu,S.J.;D.Kim;H.J.Ryu;S.Chiba;A.Kimura;D.F.Day https://doi.org/10.1271/bbb.64.223
  7. The Yeast: A Taxonomic Study Genus 14. Lipomyces Phaff,H.J.;C.P.Kortzaman;R.Kreger-van(ed.)
  8. Carbohydr. Res. v.124 Disproportionation reactions catalyzed by Leuconostoc mesenteroides and Streptococcus glucansucrases Binder,T.P.;G.L.Cote;J.F.Robyt https://doi.org/10.1016/0008-6215(83)88463-8
  9. FEBS Lett. v.527 Maltooligoscaccharide disproportionation reaction: an intrinstic property of amylosucrase from Neisseria polysaccaharea Albenne,C.;L.K.Skov;O.Mirza;M.Gajhede;G.Potocki-Veronese;P.Monsan;M.Remaud-Simound https://doi.org/10.1016/S0014-5793(02)03168-X
  10. FEBS Lett. v.345 Purification and properties of a novel enzyme from Bacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosccharides Oguma,T.;K.Tobe;M.Kobayashi https://doi.org/10.1016/0014-5793(94)00418-8
  11. Anal. Bichem. v.195 Miniaturization of three carbohydrate analyses using a microsample plate reader Fox.J.D.;J.F.Robyt https://doi.org/10.1016/0003-2697(91)90300-I
  12. Anal. Biochem. v.72 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Bradford,M.M. https://doi.org/10.1016/0003-2697(76)90527-3
  13. Nature v.227 Cleavage of Structural Proteins During the assembly of the head of bacteriophage T4 Laemmli,U.K. https://doi.org/10.1038/227680a0
  14. Gene v.156 Cloning and sequencing of the gene coding for dextranase from Streptococcus salivaeius Ohnishi,Y.;S.Kubo;Ono Yoshiaki;M.Nozaki;Y.Gonda;H.Okano;T.Matsuya;A.Matsushiro;T.Morita https://doi.org/10.1016/0378-1119(95)00071-D
  15. Carbohydr. Res. v.292 Simplified and improved methylation analysis of saccharide, using a modified procedure and thin-layer chromatography Mukerjea,H.;Kim,D;J.F.Robyt https://doi.org/10.1016/S0008-6215(96)91017-4
  16. Carbohydr. Res. v.245 Interpretation of dextransucrase inhibition at high sucrose concentration Tanirseven,A.;J.F.Robyt https://doi.org/10.1016/0008-6215(93)80062-J
  17. Biochim. Biophys. Acta v.1478 Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus SUH4-2 Cho,H.Y.;Y.W.Kim;T.J.Kim;H.S.Lee;D.Y.Kim;J.W.Kim;Y.W.Lee;S.B.Lee;K.H.Park https://doi.org/10.1016/S0167-4838(00)00037-6
  18. Biochem. J. v.225 Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea(Pisum sativum L.) Gatehouse,J.A.;J.Gilroy;M.S.Hoque;R.R.Croy https://doi.org/10.1042/bj2250239
  19. Carbohydr. Res. v.337 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 Yook,C.;J.F.Robyt https://doi.org/10.1016/S0008-6215(02)00107-6
  20. Appl. Environ. Microbiol. v.23 Induction of Lipomyces starkeyi dextranase Koenig,D.W.;D.F.Day