470-69-9

Usage

Uses

Used in Pharmaceutical Industry:
1-Kestose is used as a prebiotic agent for promoting gut health and improving the balance of gut microbiota. Its prebiotic properties help in enhancing the growth of beneficial bacteria, which in turn supports overall health and well-being.
Used in Diabetes Treatment:
1-Kestose is used as an antihyperglycemic agent for treating diabetes. Its ability to lower blood sugar levels makes it a potential therapeutic option for managing diabetes and its associated complications.
Used in Functional Foods and Supplements:
1-Kestose can be used as an ingredient in functional foods and dietary supplements due to its prebiotic and antihyperglycemic properties. It can be incorporated into products aimed at promoting gut health, managing blood sugar levels, and supporting overall well-being.
Used in Agriculture:
1-Kestose can be utilized as a prebiotic additive in the agricultural industry, particularly in animal feed, to improve the gut health and overall health of livestock. This can lead to better growth, reduced disease incidence, and improved productivity in the animals.

InChI:InChI=1/C18H32O16/c19-1-6-9(23)12(26)13(27)16(31-6)34-18(15(29)11(25)8(3-21)33-18)5-30-17(4-22)14(28)10(24)7(2-20)32-17/h6-16,19-29H,1-5H2/t6-,7-,8-,9-,10-,11-,12+,13-,14+,15+,16-,17-,18+/m1/s1

Upstream product

• 57-50-1 Sucrose 
• 13133-07-8 nystose 
• 57-50-1 sucrose 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 25101-98-8 1′′,2,3,3′,3′′,4,4′,4′′,6,6′,6′′-undeca-O-acetyl-deoxy-1-kestose 

Downstream Products

• 25101-98-8 1′′,2,3,3′,3′′,4,4′,4′′,6,6′,6′′-undeca-O-acetyl-deoxy-1-kestose 
• 13133-07-8 nystose 

Relevant academic research and scientific papers

Molecular insight into regioselectivity of transfructosylation catalyzed by GH68 levansucrase and β-fructofuranosidase

Glycoside hydrolase family 68 (GH68) enzymes catalyze β-fructosyltransfer from sucrose to another sucrose, the so-called transfructosylation. Although regioselectivity of transfructosylation is divergent in GH68 enzymes, there is insufficient information available on the structural factor(s) involved in the selectivity. Here, we found two GH68 enzymes, β-fructofuranosidase (FFZm) and levansucrase (LSZm), encoded tandemly in the genome of Zymomonas mobilis, displayed different selectivity: FFZm catalyzed the β-(2→1)-transfructosylation (1-TF), whereas LSZm did both of 1-TF and β-(2→6)-transfructosylation (6-TF). We identified His79FFZm and Ala343FFZm and their corresponding Asn84LSZm and Ser345LSZm respectively as the structural factors for those regioselectivities. LSZm with the respective substitution of FFZm-type His and Ala for its Asn84LSZm and Ser345LSZm (N84H/S345A-LSZm) lost 6-TF and enhanced 1-TF. Conversely, the LSZm-type replacement of His79FFZm and Ala343FFZm in FFZm (H79N/A343SFFZm) almost lost 1-TF and acquired 6-TF. H79N/A343S-FFZm exhibited the selectivity like LSZm but did not produce the β-(2→6)-fructoside-linked levan and/or long levanooligosaccharides that LSZm did. We assumed Phe189LSZm to be a responsible residue for the elongation of levan chain in LSZm and mutated the corresponding Leu187FFZm in FFZm to Phe. An H79N/L187F/A343S-FFZm produced a higher quantity of long levanooligosaccharides than H79N/A343S-FFZm (or H79NFFZm), although without levan formation, suggesting that LSZm has another structural factor for levan production. We also found that FFZm generated a sucrose analog, β-D-fructofuranosyl α-D-mannopyranoside, by β-fructosyltransfer to D-mannose and regarded His79FFZm and Ala343FFZm as key residues for this acceptor specificity. In summary, this study provides insight into the structural factors of regioselectivity and acceptor specificity in transfructosylation of GH68 enzymes.

Inulinase immobilisation in PAA/PEG composite for efficient fructooligosaccharides production

Inulinase was immobilised by entrapment method in polyacrylamide/polyethylene glycol composite and evaluated for its efficiency for short-chain fructooligosaccharides (3–6 degrees of polymerisation) production in batch hydrolysis system. Aqueous two-phase

Application of appel reaction to the primary alcohol groups of fructooligosaccharides: Synthesis of 6,6′,6′′-trihalogenated 1-kestose derivatives

1-kestose (O-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-α-D-glucopyranoside) is a potential short chain fructooligosaccharide with an inulin-type skeleton. Halogenation of 1-kestose was conducted via the Appel reaction with the use of carbon tetrahalide (CBr4 or CCl4) and triphenylphosphine, which was then followed by conventional acetylation. The per-O-acetylated form of 6,6’,6’’-trihalogenated derivatives of 1-kestose were conveniently isolated. Further deprotection of the per-O-acetylated form resulted in 6-, 6’-, and 6’’-trihalogenated derivatives. The structure elucidation by one- and two-dimensional nuclear magnetic resonance established that halogenations are specific at the 6-, 6’-, and 6’’-position of 1-kestose primary alcohols.

Separation and purification of fructo-oligosaccharide by high-speed counter-current chromatography coupled with precolumn derivatization

High-speed counter-current chromatography (HSCCC) coupled with precolumn derivatization was developed for isolating and purifying fructo-oligosaccharides (FOSs). Firstly, the total FOSs were precolumn derivatized and then separated by high-speed counter-current chromatography (HSCCC) with two-phase solvent system petroleum ether-n-butanol-methanol-water (3:2:1:4, v/v). Secondly, the obtained compounds were deacetylated and the fructo-oligosaccharides (FOSs) with high purity were obtained. Their structures were identified by mass spectrometry (MS) and nuclear magnetic resonance (NMR). This research successfully established a novel strategy for separation and purification of FOS. There is no doubt that the application of the research will be beneficial for the quantitative and qualitative analysis of products containing FOSs.

Enhancing fructooligosaccharides production by genetic improvement of the industrial fungus Aspergillus niger ATCC 20611

Aspergillus niger ATCC20611 is one of the most potent filamentous fungi used commercially for production of fructooligosaccharides (FOS), which are prospective components of functional food by stimulating probiotic bacteria in the human gut. However, current strategies for improving FOS yield still rely on production process development. The genetic engineering approach hasn't been applied in industrial strains to increase FOS production level. Here, an optimized polyethylene glycol (PEG)-mediated protoplast transformation system was established in A. niger ATCC 20611 and used for further strain improvement. The pyrithiamine resistance gene (ptrA) was selected as a dominant marker and protoplasts were prepared with high concentration (up to 108?g?1 wet weight mycelium) by using mixed cell wall-lysing enzymes. The transformation frequency with ptrA can reach 30–50 transformants per μg of DNA. In addition, the efficiency of co-transformation with the EGFP reporter gene (egfp) was high (approx. 82%). Furthermore, an activity-improved variant of β-fructofuranosidase, FopA(A178P), was successfully overexpressed in A. niger ATCC 20611 by using the transformation system. The transformant, CM6, exhibited a 58% increase in specific β-fructofuranosidase activity (up to 507?U/g), compared to the parental strain (320?U/g), and effectively reduced the time needed for completion of FOS synthesis. These results illustrate the feasibility of strain improvement through genetic engineering for further enhancement of FOS production level.

Fructo-oligosaccharide synthesis by whole cells of Microbacterium paraoxydans

The synthesis of fructo-oligosaccharides was carried out using whole cells of Microbacterium paraoxydans. Reactions were carried out using un-induced, inulin-induced and sucrose-induced cells displaying different amounts of invertase and inulinase activities out of which the best transfructosylation occurred using sucrose-induced cells displaying 12 I.U. invertase/0.75 I.U. inulinase activities. Using 40% w/v sucrose and in the sucrose-induced cells, a maximum fructo-oligosaccharide yield of 155 g/l (corresponding to product yield of 0.38 g/g initial substrate) was obtained. The major products synthesized were the tri-saccharide, 1-kestose [1F(1-β-D-fructofuranosyl)sucrose] and the tetrasaccharide, nystose [1F(1-β-D-fructofuranosyl)kestose]. A Box–Behnken design was used to optimize the factors affecting the fructo-oligosaccharide synthesis and these were at 31.5% sucrose, 10.96 I.U. invertase/0.69 I.U. inulinase and 14.32 h incubation time leading to an overall yield of 0.44 g/g initial substrate. The synthesized 1-kestose and nystose were purified to homogeneity by preparative TLC and structurally characterized by ESI-MS and 2D NMR.

Continuous production of fructooligosaccharides and invert sugar by chitosan immobilized enzymes: Comparison between in fluidized and packed bed reactors

In this work, β-fructofuranosidase and β-fructosyltransferase were covalently immobilized on chitosan spheres, using glutaraldehyde as a coupling agent, in order to produce invert sugar and fructooligosaccharides (FOS). Maxinvert L was used to make β-fructofuranosidase biocatalyst yielding 7000 HU/g. A partial purified β-fructosyltransferase from Viscozyme L was used to prepare the other biocatalyst yielding 2100 TU/g. The production of invert sugar and FOS was evaluated using different continuous enzymatic reactors: two packed bed reactors (PBR) and two fluidized bed reactors (FBR). The invert sugar production achieved a yield of 98% (grams of product per grams of initial sucrose) in the PBR and 94% in the FBR, whereas FOS production achieved a yield of 59% in the PBR and 54% in the FBR. It was also observed in both cases that varying the flow rate it is possible to modulate the FOS composition in terms of nystose and kestose concentrations. The operational stability of FOS produced in the PBR was evaluated for 40 days showing no reductions in yields.

Optimization of levansucrase/endo-inulinase bi-enzymatic system for the production of fructooligosaccharides and oligolevans from sucrose

A bi-enzymatic system based on the combined use of levansucrase (LS) from Bacillus amyloliquefaciens and endo-inulinase from Aspergillus niger in a one-step reaction was investigated for the synthesis of fructooligosaccharides (FOSs) and oligolevans using sucrose as the sole substrate. Sucrose concentration was the most important independent variable, whilst LS to endo-inulinase ratio exhibited significant effects on the end-product profiles. The interaction between sucrose concentration and reaction time exhibited significant effect on all responses. At the initial stage of time course, short chain FOSs (scFOSs, 1-kestose, nystose, 1F-fructosylnystose) were the major products, whilst 6-kestose, medium chain fructooligosaccharides (mcFOSs, levanohexaose, levanopentaose) and oligolevans became the dominant ones at the late stage. The optimal conditions leading to a high yield of scFOSs (1:1 ratio, 0.5 h, 0.6 M) were different from those resulting in a high yield of mcFOSs and oligolevans (1.85:1 ratio, 1.77 h, 0.6 M). The bi-enzymatic system has a great potential for the production of FOSs and oligolevans at a large scale because of its high yield (57-65%, w/w) and productivity (65.8-266.8 g/L h), and its uses of low temperature (35 °C) and low concentration of sucrose. To the best of our knowledge, this is the first study on the optimization of a LS/endo-inulinase bi-enzymatic system.

Biomolecular characterization of the levansucrase of erwinia amylovora, a promising biocatalyst for the synthesis of fructooligosaccharides

Erwinia amylovora is a plant pathogen that affects Rosaceae, such as apple and pear. In E. amylovora the fructans, produced by the action of a levansucrase (EaLsc), play a role in virulence and biofilm formation. Fructans are bioactive compounds, displaying health-promoting properties in their own right. Their use as food and feed supplements is increasing. In this study, we investigated the biomolecular properties of EaLsc using HPAEC-PAD, MALDI-TOF MS, and spectrophotometric assays. The enzyme, which was heterologously expressed in Escherichia coli in high yield, was shown to produce mainly fructooligosaccharides (FOSs) with a degree of polymerization between 3 and 6. The kinetic properties of EaLsc were similar to those of other phylogenetically related Gram-negative bacteria, but the good yield of FOSs, the product spectrum, and the straightforward production of the enzyme suggest that EaLsc is an interesting biocatalyst for future studies aimed at producing tailor-made fructans.

Screening of biocatalysts for transformation of sucrose to fructooligosaccharides

Twenty microorganisms comprising of sixteen molds, two yeasts and two bacteria were evaluated for their ability to produce fructosyltransferase (FTase) and generate fructooligosaccharides (FOS) from sucrose. FTase production by these microorganisms was studied over a period of 120 h on medium containing 20% (w/v) sucrose as the sole carbon source. High FTase levels (35-31 U/ml) were observed in culture filtrates of Aspergillus flavus, Aspergillus niger, Aspergillus terreus and Penicillium islandicum. Higher concentrations of FOS were generated from 50% (w/v) sucrose using culture filtrates of A. flavus NFCCI 2364 (63.40%, w/w), A. niger SI 19 (54.94%, w/w), A. flavus NFCCI 2785 (44.61%, w/w), P. islandicum MTCC 4926 (43.56%, w/w), A. terreus NFCCI 2347 (24.17%, w/w) and Fusarium solani NFCCI 2315 (15.25%, w/w). Kestose, nystose and 1-fructofuranosyl nystose were the predominant oligosaccharides as revealed by HPLC analysis.