Characterization of the multiple forms and main component of dextransucrase from Leuconostoc mesenteroides NRRL B-512F

Kobayashi, Mikihiko; Matsuda, Kazuo

doi:10.1016/0005-2744(80)90166-7

Cited by 67 publications

(42 citation statements)

References 22 publications

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“…Dextransucrase from Leuconostoc mesenteroides NRRL B-512F was purified as described previously. 3) Glucosyltransferase (GTF) from Streptococcus mutans IFO 13955 was prepared by the method described by Kitao and Sekine. 4 ) Assay of dextransucrase.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Dextran and Mutan Synthesis by Cycloisomaltooligosaccharides

Kobayashi

Funane

Oguma

1995

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Inhibition of Dextran and Mutan Synthesis by Cycloisomaltooligosaccharides

Kobayashi

Funane

Oguma

1995

Bioscience, Biotechnology, and Biochemistry

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“…Several workers have reported that dextransucrase exists in single or multiple forms having molecular weight in the range 64,000 -245,000 8,11,12,14,15,23 . The enzyme remains in an aggregated form in the presence of dextran resulting in high molecular weight.…”

Section: Structural Characteristics Of Dextransucrasementioning

confidence: 99%

“…The enzyme remains in an aggregated form in the presence of dextran resulting in high molecular weight. The aggregated forms disassociate into low molecular weight forms by endodextranase treatment 8 . The purifi ed enzyme is stable and active only in the presence of dextran and in the absence of dextran dextransucrase loses activity and this loss could be prevented by adding dextran 24 .…”

Section: Structural Characteristics Of Dextransucrasementioning

confidence: 99%

“…A series of reports appeared on various methods of purifi cation since then. A wide variety of techniques have been used for the purifi cation of Leuconostoc mesenteroides dextransucrase [6][7][8][9][10][11][12][13][14][15] . A recent report describes the production of recombinant dextransucrase of L. mesenteroides B-512F with a histidine tag at the C-terminal using E. coli TOP10 cells for expression and purifi cation of the recombinant enzyme by affi nity chromatography using Ni 2+ ion immobilized column 16 .…”

Section: Introductionmentioning

confidence: 99%

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An overview of purification methods of glycoside hydrolase family 70 dextransucrase

2007

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The enzyme dextransucrase (sucrose:1, 6-α-D-glucan 6-α-glucosyltransferase, EC 2.4.1.5) catalyses the synthesis of exopolysaccharide, dextran from sucrose. This class of polysaccharide has been extensively exploited in pharmaceutical industry as blood volume expander, as stabiliser in food industry and as a chromatographic medium in fi ne chemical industry because of their nonionic nature and stability. Majority of the dextrans are synthesized from sucrose by dextransucrase secreted mainly by bacteria belonging to genera Leuconostoc, Streptococcus and Lactobacillus. Bulk of the information on purifi cation of extracellular dextransucrase has been generated from Leuconostoc species. Various methods such as precipitation by ammonium sulphate, ethanol or polyethylene glycol, phase partitioning, ultrafi ltration and chromatography have been used to purify the enzyme. Purifi cation of dextransucrase is rendered diffi cult by the presence of viscous dextran in the medium. However, processes like ultra-fi ltration, salt and PEG precipitation, chromatography and phase partitioning have been standardized and successfully used for higher scale purifi cation of the enzyme. A recombinant dextransucrase from Leuconostoc mesenteroides B-512F with a histidine tag has been expressed in E. coli cells and purifi ed by immobilized metal ion chromatography. This review reports the available information on purifi cation methods of dextransucrase from Leuconostoc mesenteroides strains.

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“…The removal of dextran was necessary to compare the electrophoretic patterns of the enzyme from each strain, because dextransucrase tends to aggregate in the presence of an excess of dextran. 5 ) The enzyme from the culture supernatant of six strains was precipitated by 36% ethanol and adsorbed on hydroxyapatite. A gluconolactone-Sepharose column was used for the subsequent removal of dextran.…”

Section: Partial Purification Of Dextransucrasesmentioning

confidence: 99%