Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels

T. Kaper, B. Talik, T.J.G. Ettema, H. Bos, M.J.E.C. van der Maarel, L. Dijkhuizen

Research output: Contribution to journalArticleAcademicpeer-review

65 Citations (Scopus)

Abstract

Amylomaltases are 4-¿-glucanotransferases (EC 2.4.1.25) of glycoside hydrolase family 77 that transfer ¿-1,4-linked glucans to another acceptor, which can be the 4-OH group of an ¿-1,4-linked glucan or glucose. The amylomaltase-encoding gene (PAE1209) from the hyperthermophilic archaeon Pyrobaculum aerophilum IM2 was cloned and expressed in Escherichia coli, and the gene product (PyAMase) was characterized. PyAMase displays optimal activity at pH 6.7 and 95°C and is the most thermostable amylomaltase described to date. The thermostability of PyAMase was reduced in the presence of 2 mM dithiothreitol, which agreed with the identification of two possible cysteine disulfide bridges in a three-dimensional model of PyAMase. The kinetics for the disproportionation of malto-oligosaccharides, inhibition by acarbose, and binding mode of the substrates in the active site were determined. Acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties. This thermoreversible gel has potential applications in the food industry. This is the first report on an archaeal amylomaltase.
Original languageEnglish
Pages (from-to)5098-5106
JournalApplied and Environmental Microbiology
Volume71
Issue number9
DOIs
Publication statusPublished - 2005

Keywords

  • archaeon thermococcus-litoralis
  • alpha-amylase family
  • large cyclic glucans
  • potato d-enzyme
  • cyclodextrin-glycosyltransferase
  • hyperthermophilic archaeon
  • escherichia-coli
  • crystal-structure
  • disproportionating enzyme
  • pyrococcus-furiosus

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