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김도만,류수진,박관하,ROBYT, JOHN F. 全南大學校 觸媒硏究所 1998 觸媒硏究 論文集 Vol.20 No.-
Acarbose effectively inhibited the synthesis of dextran, and the inhibition pattern was a noncompetitive type with ?? value of 1.35mM. It also inhibited the disproport-ionation reaction of dextransucrase with isomaltotriose and decreased the efficiency of the maltose acceptor reaction. Increased concentration of dextransucrase or maltose in reaction digests, however, decreased the degree of inhibition by acarbose.
LEE, SO-YOUNG,LEE, JIN-HA,ROBYT, JOHN F.,SEO, EUN-SEONG,PARK, HYEN-JOUNG,KIM, DOMAN 한국미생물 · 생명공학회 2003 Journal of microbiology and biotechnology Vol.13 No.2
Lipomyces starkeyi KSM 22 elaborates an enzyme that has both dextranase and amylase activities in a single protein of 100 kDa. Competition studies, using different amounts of dextran and starch as substrates, gave a competition plot consistent with the hypothesis that the hydrolysis of dextran and starch occurs at two independent active sites, each specific for starch and dextran, respectively.
Cloning and Sequencing of the α-1->6 Dextransucrase Gene from Leuconostoc mensenteroides B-742CB
Kim, Ho Sang,Kim, Do Man,Ryu, Hwa Ja,John F.Robyt 한국미생물 · 생명공학회 2000 Journal of microbiology and biotechnology Vol.10 No.4
A dextransucrase gene (dsrB742) that expresses a dextransucrase to synthesize mostly α-1→6 linked dextran with a low amount (3-5%) of α-1→3 branching was cloned and sequenced from Leuconostoc mesenteroides B-742CB. The 6.1-kb PstI fragments were ligated with pGEM-3Zf(-) and transformed into E. coli DH5α. The recombinant clone (pDSRB742) synthesized dextran on an agar plate containing 2%(w/v) sucrose. The dextran synthesized was hydrolyzed with Penicillium endo-dextranase. The hydrolyzate was composed of glucose, isomaltose, isomaltotriose, and branched pentasaccharide. The nucleotide sequence of dsrB742 showed one open reading frame (ORF) composed of 4,524bp encoding dextransucrase. The deduced amino acid sequence revealed a calculated molecular mass of 168.6kDa. It also showed an activity band of 184kDa on a non-denaturing SDS-PAGE (10%). The amino acid sequence of DSRB742 exhibited a 50% similarity with DSRA from L. mesenteroides B-1299, a 70% similarity with DSRS from L. mesenteroides B-512 (F, FMCM) and a 45-56% similarity with Streptococcal GTFs.
Characterization of Leuconostoc mesenteroides B-742CB Dextransucrase Expressed in Escherichia coli
Park, Mi Ran,Ryu, Hwa Ja,Kim, Do Man,Choe, Jun Yong,Robyt, John F. 한국미생물 · 생명공학회 2001 Journal of microbiology and biotechnology Vol.11 No.4
Recombinant E. coli DH5α harboring a dextransucrase gene (dsrB742) produced an extracellular dextransucrase in a 2% sucrose medium. The enzyme was purified by DEAE-Sepharose and Phenyl-Sepharose column chromatographies upto a 142.97-fold purification with a 11.11 % recovery to near homogeneity. The enzyme had a calculated molecular mass of 168.6kDa, which was in good agreement with the activity band of 170kDa on a nondenaturing SDS-PAGE. An expression plasmid was constructed by inserting the dsrB742 into a pRSET expression vector. The activity after expression in E. coli BL21(DE3)pLysS increased about 6.7-fold compared to the extracellular dextransucrase from L. mesenteroides B-742CB. The expressed and purified enzyme from the clone showed similar biochemical properties (acceptor reaction, size of active dextransucrase, optimum pH, and temperature) to B-742CB dextransucrase, however, the ability to synthesize α-(1→3) branching decreased in comparison to that of L. mesenteroides B-742CB dextransucrase.