Antonie van Leeuwenhoek

, Volume 92, Issue 4, pp 399–404 | Cite as

Multiple dextranases from the yeast Lipomyces starkeyi

  • Stefan H. Millson
  • Ivor Howell Evans
Original Paper


The soil yeast Lipomyces starkeyi (NCYC 1436) secretes dextranase activity into the growth medium. Resolution of a dextranase-active protein fraction by SDS-PAGE produced three protein bands, of 66 kDa, 68 kDa and 78 kDa, and isoelectric focusing of the same fraction resulted in seven protein bands, of pIs 3.50, 3.85, 4.20, 4.80, 4.85, 5.00 and 5.30. Dextranase activity was demonstrated for all the isoelectric forms, and for the 78 kDa species in the presence of SDS. Amino acid compositions of the 66 kDa, 68 kDa and 78 kDa protein bands were determined, and the N-termini of the 66 kDa and 78 kDa protein bands were sequenced: the first two amino acids at the N-terminus of each protein were alanine and valine, respectively; an alanine-valine pair is seen early in the N-terminal coding sequences of the dextranases and the isopullulanase produced by the phylogenetically disparate organisms contributing to glycosyl hydrolase family 49.


Dextranase GH family 49 Isoforms Lipomyces starkeyi N-terminal sequences Yeast 


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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  1. 1.Department of Molecular Biology and BiotechnologyUniversity of SheffieldSheffieldUK
  2. 2.School of ScienceUniversity of Greenwich at MedwayChatham Maritime, KentUK

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