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Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview. [PDF]

open access: yesMol Biol Rep
García-Paz FM   +5 more
europepmc   +1 more source

Co-Immobilization of Dextransucrase and Dextranase in Alginate

open access: yesProcess Biochemistry, 2010
Abstract Dextransucrase from Leuconostoc mesenteroides and dextranase from Penicillium lilacinum were co-immobilized and used to produce isomaltooligosaccharides from sucrose. The enzymes were co-immobilized by encapsulating soluble dextransucrase and dextranase covalently attached to Eupergit C in alginate (beads, fibers, and capsules).
Aziz Tanriseven
exaly   +3 more sources
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Dynamic reactivities of dextransucrase

Archives of Biochemistry and Biophysics, 1986
Dextransucrase, from Streptococcus sanguis ATCC 10558, was immobilized on hydroxylapatite and was "charged" in short pulses with labeled sucrose, as previously described [V. K. Parnaik, G. A. Luzio, D. A. Grahame, S. L. Ditson, and R. M. Mayer (1983) Carbohydr. Res. 121, 257-268].
S L, Ditson, S M, Sung, R M, Mayer
openaire   +2 more sources

Modelling of oligosaccharide synthesis by dextransucrase

Biotechnology and Bioengineering, 1999
Dextransucrase catalyses the formation of dextran, but also of numerous oligosaccharides from sucrose and different acceptors, if appropriate conditions are chosen. Much experimental work has been carried out and a scheme of reactions and a mathematical model have been developed to describe the complex kinetic behaviour of the enzyme.
B, Demuth, H J, Jördening, K, Buchholz
openaire   +2 more sources

The dissociation of aggregate forms of dextransucrase

Archives of Biochemistry and Biophysics, 1982
Abstract Aggregate forms of dextransucrase obtained from Streptococcus sanguis dissociate in the presence of sodium dodecyl sulfate. However, the enzyme was unstable under these conditions. Nonionic detergents such as Triton X-100 stabilize the enzyme (A. W. Miller and J. R. Robyt, (1981) Fed. Proc. Fed. Amer. Soc. Exp. Biol.
G A, Luzio, D A, Grahame, R M, Mayer
openaire   +2 more sources

Activation and inhibition of dextransucrase by calcium

Biochimica et Biophysica Acta (BBA) - General Subjects, 1986
Initial rate kinetics of dextran synthesis by dextransucrase (sucrose:1,6-alpha-D-glucan-6-alpha-D-glucosyltransferase, EC 2.4.1.5) from Leuconostoc mesenteroides NRRL B-512F showed that below 1 mM, Ca2+ activated the enzyme by increasing Vmax and decreasing the Km for sucrose. Above 1 mM, Ca2+ was a weak competitive inhibitor (Ki = 59 mM). Although it
A W, Miller, J F, Robyt
openaire   +2 more sources

Dextransucrase: Donor substrate reactions

Archives of Biochemistry and Biophysics, 1981
Abstract Previous studies have indicated that α- d -1-fluoroglucose is a glycosyl donor for glucosyl transferases (5, 6) including dextransucrases formed by Leuconostoc and Streptococcus mutans. The present report confirms these observations with dextransucrase isolated from S. sanguis and conclusively establishes the details of this reaction as well
S M, Jung, R M, Mayer
openaire   +2 more sources

Dextransucrase and the mechanism for dextran biosynthesis

Carbohydrate Research, 2008
Remaud-Simeon and co-workers [Moulis, C.; Joucla, G.; Harrison, D.; Fabre, E.; Potocki-Veronese, G.; Monsan, P.; Remaud-Simeon, M. J. Biol. Chem., 2006, 281, 31254-31267] have recently proposed that a truncated Escherichia coli recombinant B-512F dextransucrase uses sucrose and the hydrolysis product of sucrose, D-glucose, as initiator primers for the ...
John F, Robyt   +2 more
openaire   +2 more sources

Interaction of deoxyhalosucrose derivatives with dextransucrase

Carbohydrate Research, 1985
Members of a series of deoxyhalosucrose analogs substituted at one, two, or three primary carbon atoms with bromine or chlorine were prepared. Dextransucrase isolated from Streptococcus sanguis was separately treated with 6-bromo-6-deoxysucrose, 6,6'-dibromo-6,6'-dideoxysucrose, 6,1',6'-tribromotrideoxysucrose, and 6,6'-dichlorodideoxysucrose, in order
M K, Bhattacharjee, R M, Mayer
openaire   +2 more sources

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