Dextran synthesis by immobilized dextran sucrase

López, Alfonso; Monsan, Pierre

doi:10.1016/s0300-9084(80)80161-1

Cited by 41 publications

(21 citation statements)

References 14 publications

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“…Bacterial strains, media and growth conditions L. mesenteroides ATCC 8293 (equivalent to NRRL B-1118) was cultivated in a New Brunswick incubator shaker at 30°C and 200 rpm with 20 g/l of sucrose (Lopez and Monsan 1980). For DNA isolation, glucose was used as carbon source to avoid polymer synthesis that may interfere with the extraction.…”

Section: Methodsmentioning

confidence: 99%

Structural and functional features of fructansucrases present in Leuconostoc mesenteroides ATCC 8293

Olvera

Centeno-Leija

López-Munguı́a

2006

Antonie van Leeuwenhoek

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Glycosyltransferases produced by Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293 (equivalent to NRRL B-1118) were identified. Two glucansucrases and one fructansucrases were observed in batch culture while levC and levL genes, corresponding to two fructansucrases, were isolated from information obtained from the released draft sequence of this Leuconostoc strain genome and cloned in Escherichia coli. The recombinant enzymes were shown to be fructansucrases producing a polymer identified by NMR as levan, confirming our recent report stating that these are also mosaic levansucrases bearing structural features of glucansucrases in the amino and carboxy terminal regions, as is also the case of inulosucrase (IslA) from Leuconostoc citreum CW28 and levansucrase (LevS) from L. mesenteroides NRRL B-512F. The recombinant levansucrase LevC was purified and characterized in terms of pH, temperature, and kinetic properties. The enzyme exhibits Michaelis-Menten kinetic properties with a K(m) = 27.3 mM and a k(cat) = 282.9 s(-1). This levansucrase behaves mainly as a transferase as only 30% of the substrate is hydrolyzed in a wide range of sucrose concentrations, with higher hydrolytic activities at low substrate concentrations. With this report we experimentally confirm the unusual structural pattern displayed by fructansucrases present in Leuconostoc species that group as a novel sub family of fructansucrases.

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Section: Methodsmentioning

confidence: 99%

Structural and functional features of fructansucrases present in Leuconostoc mesenteroides ATCC 8293

Olvera

Centeno-Leija

López-Munguı́a

2006

Antonie van Leeuwenhoek

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“…Each structure has its influence on the activity and stability of the immobilized enzyme. [18][19][20][21][22][23] Despite the fact that such technique has been investigated for the first time after almost 30 years 24 , the optimization of the modification and the activation steps in this technique is still needed. Recently, the same technique has been used by other authors in immobilization of Candida rugosa lipase via GA coupling onto the functionalized hydrophobic polypropylene chloride membrane, prepared by the amination of chlorinated polypropylene with hexamethylene diamine.…”

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confidence: 99%

Covalent Immobilization of β‐Galactosidase onto Amino‐Functionalized Polyvinyl Chloride Microspheres: Enzyme Immobilization and Characterization

et al. 2013

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ABSTRACT:In this study, β-galactosidase (Aspergillus oryzae) was covalently immobilized onto aminated polyvinyl chloride (PVC) via glutaraldehyde coupling. Effect of immobilization conditions was investigated. The maximum obtained immobilization yield is 27 units g −1 while the maximum expressed activity is 12 μmol minThe optimum pH of the free enzyme was observed at 5.2, whereas the optimum pH of the immobilized one was schiffed to 4.4. The optimum temperature for both the free and immobilized forms was recognized at 60• C. A change in the temperature profile of the immobilized enzyme below 60• C was observed when response to the elevation temperature was less than that to the free counterpart. The K m and V max values of the free and immobilized β-galactosidase were found to be 52.03 and 123.1 mM, and 6.12 and 9.98 μ mol/min, respectively. Lactose hydrolysis, 500 mL of 100 mM concentration, was studied using 400 units of either free or immobilized enzymes at pH 6.0 and 60• C. Almost 80% hydrolysis percentage has been obtained after 6 h hydrolysis time with immobilized enzyme compared with 63% hydrolysis percentage obtained after 2 h for the free counterpart. Investigation of the operational stability at 40• C shows that the immobilized enzyme kept its activity for 5 h over 10 successive lactose hydrolysis cycles, which provides potentials for practical application in milk and whey hydrolysis. C

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“…5). It has been previously reported that high molecular mass dextran was produced when dextransucrase enzyme was immobilized instead of cells [17]. Dextran production (gm%) Fig.…”

Section: Resultsmentioning

confidence: 89%

Continuous Production of Dextran from Immobilized Cells of Leuconostoc mesenteroides KIBGE HA1 Using Acrylamide as a Support

2011

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The cells of L. mesenteroides KIBGE HA1 were immobilized for the production of dextran on acrylamide gel and gel concentration was optimized for maximum entrapment. Sucrose at substrate concentration of 10% produced high yield of dextran at 25°C with a percent conversion of 5.82 while at 35°C it was 3.5. However, increasing levels of sucrose diminished dextran yields. The free cells stopped producing dextran after 144 h, while immobilized cells continued to produce dextran even after 480 h. Molecular mass distribution of dextran from free cells indicate that it is identical to that of blue dextran while the molecular mass of dextran from immobilized cells is lower than that of free cells.

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Dextran synthesis by immobilized dextran sucrase

Cited by 41 publications

References 14 publications

Structural and functional features of fructansucrases present in Leuconostoc mesenteroides ATCC 8293

Structural and functional features of fructansucrases present in Leuconostoc mesenteroides ATCC 8293

Covalent Immobilization of β‐Galactosidase onto Amino‐Functionalized Polyvinyl Chloride Microspheres: Enzyme Immobilization and Characterization

Continuous Production of Dextran from Immobilized Cells of Leuconostoc mesenteroides KIBGE HA1 Using Acrylamide as a Support

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