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Products Released from Structurally Different Dextrans by Bacterial and Fungal Dextranases.
Pittrof, Silke L; Kaufhold, Larissa; Fischer, Anja; Wefers, Daniel.
  • Pittrof SL; Department of Food Chemistry and Phytochemistry, Karlsruhe Institute of Technology, 76131 Karlsruhe, Germany.
  • Kaufhold L; Department of Food Chemistry and Phytochemistry, Karlsruhe Institute of Technology, 76131 Karlsruhe, Germany.
  • Fischer A; Department of Food Chemistry and Phytochemistry, Karlsruhe Institute of Technology, 76131 Karlsruhe, Germany.
  • Wefers D; Department of Food Chemistry and Phytochemistry, Karlsruhe Institute of Technology, 76131 Karlsruhe, Germany.
Foods ; 10(2)2021 Jan 26.
Article en En | MEDLINE | ID: mdl-33530339
ABSTRACT
Dextran hydrolysis by dextranases is applied in the sugar industry and the medical sector, but it also has a high potential for use in structural analysis of dextrans. However, dextranases are produced by several organisms and thus differ in their properties. The aim of this study was to comparatively investigate the product patterns obtained from the incubation of linear as well as O3- and O4-branched dextrans with different dextranases. For this purpose, genes encoding for dextranases from Bacteroides thetaiotaomicron and Streptococcus salivarius were cloned and heterologously expressed in Escherichia coli. The two recombinant enzymes as well as two commercial dextranases from Chaetomium sp. and Penicillium sp. were subsequently used to hydrolyze structurally different dextrans. The hydrolysis products were investigated in detail by HPAEC-PAD. For dextranases from Chaetomium sp., Penicillium sp., and Bacteroides thetaiotaomicron, isomaltose was the end product of the hydrolysis from linear dextrans, whereas Penicillium sp. dextranase led to isomaltose and isomaltotetraose. In addition, the latter enzyme also catalyzed a disproportionation reaction when incubated with isomaltotriose. For O3- and O4-branched dextrans, the fungal dextranases yielded significantly different oligosaccharide patterns than the bacterial enzymes. Overall, the product patterns can be adjusted by choosing the correct enzyme as well as a defined enzyme activity.
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