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Levan fructotransferase (DFA-IV-forming)

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Last Updated: 05 December 2020

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Levan fructotransferase (DFA-IV-forming)

Databases
BRENDABRENDA entry
ExPASyNiceZyme view
IntEnzIntEnz view
KEGGKEGG entry
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
PRIAMprofile
Identifiers
EC number4.2.2.16

Di d fructofuranose 2 6: 2 6dianhydride, kind of cyclic disaccharide, was first isolated as a byproduct, when inulin was treated with sulphuric acid to prepare fructose syrup. DFA is nondigestive and nonfermentative subsaccharide, which is indigestible to animals. In addition to its utility as a lowcalorie sweetener, DFA plays a role in inhibiting tooth decay, and also functions as a productive factor for Bifidobacterium. It has also been reported that DFA can be used as an absorption factor for minerals in the body. DFA consists of two fructose residues, with the reducing end of each residue linked to the nonreducing - hydroxyl group of counter residue. DFA can be synthesize chemically or enzymatically from fructans, inulin and levan-all naturally occurring fructose homopolysaccharides. So far, five kinds of difructose dianhydrides have been discover, namely, DFA I-V. DFA II and V can be synthesize only by chemical processes, while others can be produced enzymatically: DFA I and III are produced from inulin by action of inulin fructotransferase; and DFA IV is produced from levan by action of levan fructotransferase. However, chemical synthesis of DFA from natural fructans is fraught with significant disadvantages, most notably low reaction selectivity and complicated separation and purification procedures. An even more distressing aspect is environmental pollution resulting from this process. Consequently, these problems contraindicate chemical synthesis of DFA in terms of economical production value. In contrast, enzymatic synthesis using biocatalysts, such as microbes or enzymes, is now regarded as being very economically favourable in preparation of DFA from natural fructans. Since the discovery of inulin fructotransferase in microbes, DFAproducing enzymes have been isolated from several microbial sources. LFTases that catalyse formation of DFA IV from levan were found in microorganisms, such as Arthrobacter nicotinovorans GS9, Arthrobacter ureafaciens, Arthrobacter oxydans and Microbacterium sp. However, because only a very small amount of LFTase can be isolated from these bacteria and, it is still technically and economically unfeasible to apply these enzymes for production of DFA IV. In this study, we clone LFTase gene from. Ureafaciens K2032 which was previously reported to produce this enzyme and overexpressed in Escherichia coli. Furthermore, we demonstrate biochemical conversion of levan into DFA IV by recombinant enzyme and test crystallizationbased product purification method.

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* Please keep in mind that all text is machine-generated, we do not bear any responsibility, and you should always get advice from professionals before taking any actions

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* Please keep in mind that all text is machine-generated, we do not bear any responsibility, and you should always get advice from professionals before taking any actions

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