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Applied and Environmental Microbiology, September 2005, p. 5098-5106, Vol. 71, No. 9
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.9.5098-5106.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Amylomaltase of Pyrobaculum aerophilum IM2 Produces Thermoreversible Starch Gels

Thijs Kaper,1,2 Boguslawa Talik,1,2 Thijs J. Ettema,3 Herman Bos,4 Marc J. E. C. van der Maarel,1,4* and Lubbert Dijkhuizen1,2

Centre for Carbohydrate Bioengineering TNO-University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands,1 Microbial Physiology Research Group, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands,2 Laboratory for Microbiology, Wageningen University, H. van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands,3 Innovative Ingredients and Products Department, TNO Quality of Life, Rouaanstraat 27, 9723 CC Groningen, The Netherlands4

Received 15 November 2004/ Accepted 2 April 2005

Amylomaltases are 4-{alpha}-glucanotransferases (EC 2.4.1.25) of glycoside hydrolase family 77 that transfer {alpha}-1,4-linked glucans to another acceptor, which can be the 4-OH group of an {alpha}-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.

* Corresponding author. Mailing address: Centre for Carbohydrate Bioengineering TNO-University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands. Phone: 31-50-3632150. Fax: 31-50-3632154. E-mail: M.J.E.C.van.der.Maarel{at}Rug.nl.

Applied and Environmental Microbiology, September 2005, p. 5098-5106, Vol. 71, No. 9
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.9.5098-5106.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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