Reactor optimization for α‐1,2 glucooligosaccharide synthesis by immobilized dextransucrase

Dols‐Lafargue, Marguerite; Willemot, René‐Marc; Monsan, Pierre; Remaud‐Siméon, Magali

doi:10.1002/bit.1183

Cited by 10 publications

(6 citation statements)

References 25 publications

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“…In addition, another group of 10 mice was fed a α1-2-GlucoOligoSaccharide17 (O-α-D-glc p (1-2)-O-α-D-glc p (1-6)n-O-α-D-glc p (1–4) where (2<n<7), GOS)-supplemented HFD (500 mg/mouse/day, 10% of daily intake) (HFD+GOS) for 3 months. Mice were group-housed (five mice per cage) in a controlled environment (inverted 12 h daylight-cycle, light off at 10:00 h).…”

Section: Methodsmentioning

confidence: 99%

Metabolic adaptation to a high-fat diet is associated with a change in the gut microbiota

Sérino

Luche

Grès

et al. 2011

Gut

550

431

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ObjectiveThe gut microbiota, which is considered a causal factor in metabolic diseases as shown best in animals, is under the dual influence of the host genome and nutritional environment. This study investigated whether the gut microbiota per se, aside from changes in genetic background and diet, could sign different metabolic phenotypes in mice.MethodsThe unique animal model of metabolic adaptation was used, whereby C57Bl/6 male mice fed a high-fat carbohydrate-free diet (HFD) became either diabetic (HFD diabetic, HFD-D) or resisted diabetes (HFD diabetes-resistant, HFD-DR). Pyrosequencing of the gut microbiota was carried out to profile the gut microbial community of different metabolic phenotypes. Inflammation, gut permeability, features of white adipose tissue, liver and skeletal muscle were studied. Furthermore, to modify the gut microbiota directly, an additional group of mice was given a gluco-oligosaccharide (GOS)-supplemented HFD (HFD+GOS).ResultsDespite the mice having the same genetic background and nutritional status, a gut microbial profile specific to each metabolic phenotype was identified. The HFD-D gut microbial profile was associated with increased gut permeability linked to increased endotoxaemia and to a dramatic increase in cell number in the stroma vascular fraction from visceral white adipose tissue. Most of the physiological characteristics of the HFD-fed mice were modulated when gut microbiota was intentionally modified by GOS dietary fibres.ConclusionsThe gut microbiota is a signature of the metabolic phenotypes independent of differences in host genetic background and diet.

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Section: Methodsmentioning

confidence: 99%

Metabolic adaptation to a high-fat diet is associated with a change in the gut microbiota

Sérino

Luche

Grès

et al. 2011

Gut

550

431

View full text Add to dashboard Cite

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“…This polymer layer is also the reason for limited operational stability of the biocatalyst and its lower productivity when it is used in continuous operation. Beyond that, the enzyme can be leaked out of the beads, as result of swelling, and their remaining enzymatic activity is considerably reduced [255,262,263].…”

Section: The Gh 70 Family Of Enzymesmentioning

confidence: 99%

“…Another advantage of dextransucrase encapsulation relates to the simplification of the segregation of products, namely dextran and oligosaccharides, since dextran is limited to the bead microenvironment owing to its molecular size, whereas the smaller oligosaccharides are released to the reaction medium. Furthermore, the alginate matrix possibly acts as a protection for the biocatalyst, with the half-life of the entrapped dextransucrase, which is always reported as being higher than that of the free enzyme [244,258,262]. Moreover, glucose and maltose could be added as additional stabilizers [256,265], and soluble starch as viscosity modulator, protecting the enzyme [266].…”

Section: The Gh 70 Family Of Enzymesmentioning

confidence: 99%

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

et al. 2016

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Glycoside hydrolases (GH) are enzymes capable to hydrolyze the glycosidic bond between two carbohydrates or even between a carbohydrate and a non-carbohydrate moiety. Because of the increasing interest for industrial applications of these enzymes, the immobilization of GH has become an important development in order to improve its activity, stability, as well as the possibility of its reuse in batch reactions and in continuous processes. In this review, we focus on the broad aspects of immobilization of enzymes from the specific GH families. A brief introduction on methods of enzyme immobilization is presented, discussing some advantages and drawbacks of this technology. We then review the state of the art of enzyme immobilization of families GH1, GH13, and GH70, with special attention on the enzymes β-glucosidase, α-amylase, cyclodextrin glycosyltransferase, and dextransucrase. In each case, the immobilization protocols are evaluated considering their positive and negative aspects. Finally, the perspectives on new immobilization methods are briefly presented.

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“…These oligosaccharides can also interact with beneficial lactic acid bacteria of the skin (7). Isomaltooligosaccharides (8) and glucooligosaccharides containing α(1→2) bonds (9) [commercialized with the name of BioEcolia; http://www.solabia.fr] are examples of such prebiotic products synthesized by dextransucrases.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Dextransucrase from Leuconostoc mesenteroides NRRL B-512F on Eupergit C Supports

et al. 2004

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Dextransucrase from Leuconostoc mesenteroides B-512F was immobilized on epoxy-activated acrylic polymers with different textural properties (Eupergit C and Eupergit C 250L). Prior to immobilization, dextransucrase was treated with dextranase to remove the dextran layer covering the enzyme surface, thus increasing the accessibility of its reactive groups to the epoxide centers of the support. Elimination of 99% of the initial carbohydrate content was determined by the anthrone method. To prevent enzyme inactivation, the immobilization was carried out at pH 5.4, at which the coupling to the support took place through the carboxylic groups of the enzyme. The effects of the amount (mg) of dextransucrase added per gram of support (from 0.2:1 to 30:1), temperature and contact time were studied. Maximum activity recovery of 22% was achieved using Eupergit C 250L. Using this macroporous support, the maximum specific activity (710 U/g biocatalyst) was significantly higher than that obtained with the less porous Eupergit C (226 U/g biocatalyst). The dextransucrase immobilized on Eupergit C 250L showed similar optimal temperature (30 degrees C) and pH (5-6) compared with the native enzyme. In contrast, a notable stabilization effect at 30 degrees C was observed as a consequence of immobilization. After a fast partial inactivation, the dextransucrase immobilized on Eupergit C 250L maintained more than 40% of the initial activity over the following 2 days. The features of this immobilized system are very attractive for its application in batch and fixed-bed bioreactors.

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Reactor optimization for α‐1,2 glucooligosaccharide synthesis by immobilized dextransucrase

Cited by 10 publications

References 25 publications

Metabolic adaptation to a high-fat diet is associated with a change in the gut microbiota

Metabolic adaptation to a high-fat diet is associated with a change in the gut microbiota

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

Immobilization of Dextransucrase from Leuconostoc mesenteroides NRRL B-512F on Eupergit C Supports

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