Identification of a novel alpha-galatosidase from the hyperthermophilic archaeon Sulfolobus solfataricus

S.J.J. Brouns, N. Smits, H. Wu, P.C. Wright, A.P.L. Snijders, W.M. de Vos, J. van der Oost

Research output: Contribution to journalArticleAcademicpeer-review

39 Citations (Scopus)

Abstract

Sulfolobus solfataricus is an aerobic crenarchaeon that thrives in acidic volcanic pools. In this study, we have purified and characterized a thermostable -galactosidase from cell extracts of S. solfataricus P2 grown on the trisaccharide raffinose. The enzyme, designated GalS, is highly specific for -linked galactosides, which are optimally hydrolyzed at pH 5 and 90°C. The protein consists of 74.7-kDa subunits and has been identified as the gene product of open reading frame Sso3127. Its primary sequence is most related to plant enzymes of glycoside hydrolase family 36, which are involved in the synthesis and degradation of raffinose and stachyose. Both the galS gene from S. solfataricus P2 and an orthologous gene from Sulfolobus tokodaii have been cloned and functionally expressed in Escherichia coli, and their activity was confirmed. At present, these Sulfolobus enzymes not only constitute a distinct type of thermostable -galactosidases within glycoside hydrolase clan D but also represent the first members from the Archaea.
Original languageEnglish
Pages (from-to)2392-2399
JournalJournal of Bacteriology
Volume188
Issue number7
DOIs
Publication statusPublished - 2006

Keywords

  • catalytic nucleophile
  • phanerochaete-chrysosporium
  • thermoacidophilic archaeon
  • functional expression
  • glycosyl hydrolases
  • crystal-structure
  • escherichia-coli
  • genus sulfolobus
  • complete genome
  • melon fruit

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