메뉴 건너뛰기




Volumn 13, Issue 2, 2003, Pages 313-316

Demonstration of two independent dextranase and amylase active sites on a single enzyme elaborated by Lipomyces starkeyi KSM 22

Author keywords

Active site; Amylase; Competition plot; Dextranase; Lipomyces starkeyi

Indexed keywords

AMYLASE; BACTERIAL PROTEIN; DEXTRAN; DEXTRANASE; STARCH;

EID: 0038025771     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (29)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0034839999 scopus 로고    scopus 로고
    • The competition plot: A kinetic method to assess whether an enzyme that catalyzes multiple reactions does so at a unique site
    • Cardenas, M. 2001. The competition plot: A kinetic method to assess whether an enzyme that catalyzes multiple reactions does so at a unique site. Methods 24: 175-180.
    • (2001) Methods , vol.24 , pp. 175-180
    • Cardenas, M.1
  • 4
    • 0027518532 scopus 로고
    • The competition plot: A simple test of whether two reactions occur at the same active site
    • Chevillard, C., M. Cardenas, and A. Cornish-Bowden. 1993. The competition plot: A simple test of whether two reactions occur at the same active site. Biochem. J. 289: 599-604.
    • (1993) Biochem. J. , vol.289 , pp. 599-604
    • Chevillard, C.1    Cardenas, M.2    Cornish-Bowden, A.3
  • 5
    • 0025766291 scopus 로고
    • Miniaturization of three carbohydrate analyses using a microsample plate reader
    • Fox, J. D. and J. F. Robyt. 1991. Miniaturization of three carbohydrate analyses using a microsample plate reader. Anal. Biochem. 195: 93-96.
    • (1991) Anal. Biochem. , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 6
    • 0014040209 scopus 로고
    • Synthesis of extracellular dextran by cariogenic bacteria and its presence in human dental plaque
    • Gibbons, R. J. and, S. B. Banhart. 1967. Synthesis of extracellular dextran by cariogenic bacteria and its presence in human dental plaque. Arch. Oral Biol. 12: 11-20.
    • (1967) Arch. Oral Biol. , vol.12 , pp. 11-20
    • Gibbons, R.J.1    Banhart, S.B.2
  • 7
    • 0014338990 scopus 로고
    • Synthesis of insoluble dextran and its significance in the formation of gelatinous deposits by plaque-forming Streptococci
    • Gibbons, R. J. and S. Nygaard. 1968. Synthesis of insoluble dextran and its significance in the formation of gelatinous deposits by plaque-forming Streptococci. Arch. Oral Biol. 13: 1249-1264.
    • (1968) Arch. Oral Biol. , vol.13 , pp. 1249-1264
    • Gibbons, R.J.1    Nygaard, S.2
  • 8
    • 0014515631 scopus 로고
    • Dextran-induced agglutination of Streptococcus mutans and its potential role in the formation of microbial dental plaque
    • Gibbons, R. J. and R. J. Fitzgerald. 1969. Dextran-induced agglutination of Streptococcus mutans and its potential role in the formation of microbial dental plaque. J. Bacteriol. 98: 341-353.
    • (1969) J. Bacteriol. , vol.98 , pp. 341-353
    • Gibbons, R.J.1    Fitzgerald, R.J.2
  • 10
    • 0016372813 scopus 로고
    • Morphological study of Streptococcus mutans and two extracellular polysaccharide mutants
    • Johnson, M. C., J. J. Bozzola, and I. L. Shechmeister. 1974. Morphological study of Streptococcus mutans and two extracellular polysaccharide mutants. J. Bacteriol. 118: 304-311.
    • (1974) J. Bacteriol. , vol.118 , pp. 304-311
    • Johnson, M.C.1    Bozzola, J.J.2    Shechmeister, I.L.3
  • 12
    • 0029026898 scopus 로고
    • Isolation of a dextranase constitutive mutant Lipomyces starkeyi and its use for the production of clinical size dextran
    • Kim, D. and D. F. Day. 1995. Isolation of a dextranase constitutive mutant Lipomyces starkeyi and its use for the production of clinical size dextran. Lett. Appl. Microbiol. 20: 268-270.
    • (1995) Lett. Appl. Microbiol. , vol.20 , pp. 268-270
    • Kim, D.1    Day, D.F.2
  • 13
    • 0031827710 scopus 로고    scopus 로고
    • Acarbose effect for dextran synthesis, acceptor and disproportionation reactions of Leuconostoc mesenteroides B-512FMCM dextransucrase
    • Kim, D., K. H. Park, and J. F. Robyt. 1998. Acarbose effect for dextran synthesis, acceptor and disproportionation reactions of Leuconostoc mesenteroides B-512FMCM dextransucrase. J. Microbiol. Biotechnol. 8: 287-290.
    • (1998) J. Microbiol. Biotechnol. , vol.8 , pp. 287-290
    • Kim, D.1    Park, K.H.2    Robyt, J.F.3
  • 14
    • 0032767795 scopus 로고    scopus 로고
    • Characterization of a novel carbohydrate from Lipomyces starkeyi KSM22 for dental application
    • Kim, D., S. J. Ryu, S. J. Heo, and H. S. Kim. 1999. Characterization of a novel carbohydrate from Lipomyces starkeyi KSM22 for dental application. J. Microbiol. Biotechnol. 9: 260-264.
    • (1999) J. Microbiol. Biotechnol. , vol.9 , pp. 260-264
    • Kim, D.1    Ryu, S.J.2    Heo, S.J.3    Kim, H.S.4
  • 15
    • 0033834162 scopus 로고    scopus 로고
    • Cloning and sequencing of the α-1→6 dextransucrase gene from Leuconostoc mesenteroides B-742CB
    • Kim, H. S., D. Kim, H. J. Ryu, and J. F. Robyt. 2000. Cloning and sequencing of the α-1→6 dextransucrase gene from Leuconostoc mesenteroides B-742CB. J. Microbiol. Biotechnol. 10: 559-563.
    • (2000) J. Microbiol. Biotechnol. , vol.10 , pp. 559-563
    • Kim, H.S.1    Kim, D.2    Ryu, H.J.3    Robyt, J.F.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature 227: 117-127.
    • (1970) Nature , vol.227 , pp. 117-127
    • Laemmli, U.K.1
  • 18
    • 0013331985 scopus 로고    scopus 로고
    • Effect of aeration rates on production of extracellular polysaccharides, EPS-R by marine bacterium Hahella chejuensis
    • Lee, H. S., S. H. Park, J. H. Lee, and H. K. Lee. 2001. Effect of aeration rates on production of extracellular polysaccharides, EPS-R by marine bacterium Hahella chejuensis. Biotechnol. Bioprocess Eng. 6: 359-362.
    • (2001) Biotechnol. Bioprocess Eng. , vol.6 , pp. 359-362
    • Lee, H.S.1    Park, S.H.2    Lee, J.H.3    Lee, H.K.4
  • 20
    • 0024535931 scopus 로고    scopus 로고
    • Single active site mechanism of rabbit liver acid α-glucosidase
    • Onodera, S., H. Matsui, and S. Chiba. 1998. Single active site mechanism of rabbit liver acid α-glucosidase. J. Biochem. 105: 611-618.
    • (1998) J. Biochem. , vol.105 , pp. 611-618
    • Onodera, S.1    Matsui, H.2    Chiba, S.3
  • 21
    • 0013384013 scopus 로고    scopus 로고
    • Encapsulation of whole cell CGTase from concentrated broth solution
    • Park, J. G., J. H. Sohn, H. W. Park, and Y. H. Lee. 2001. Encapsulation of whole cell CGTase from concentrated broth solution. Biotechnol. Bioprocess Eng. 6: 67-71.
    • (2001) Biotechnol. Bioprocess Eng. , vol.6 , pp. 67-71
    • Park, J.G.1    Sohn, J.H.2    Park, H.W.3    Lee, Y.H.4
  • 22
    • 0034811847 scopus 로고    scopus 로고
    • Characterization of Leuconostoc mesenteroides B-742CB dextransucrase expressed in Escherichia coli
    • Park, M. R., H. J. Ryu, D. Kim, J. Y. Choe, and J. F. Robyt. 2001. Characterization of Leuconostoc mesenteroides B-742CB dextransucrase expressed in Escherichia coli. J. Microbiol. Biotechnol. 11: 628-635.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 628-635
    • Park, M.R.1    Ryu, H.J.2    Kim, D.3    Choe, J.Y.4    Robyt, J.F.5
  • 23
    • 0015219053 scopus 로고
    • Dental plaque and oral health
    • Poole, D. F. G. and N. J. Newman. 1971. Dental plaque and oral health. Nature 234: 329-331.
    • (1971) Nature , vol.234 , pp. 329-331
    • Poole, D.F.G.1    Newman, N.J.2
  • 24
    • 0034132803 scopus 로고    scopus 로고
    • Purification and partial characterization of a novel glucanhydrolase from Lipomyces starkeyi KSM 22 and its use for inhibition of insoluble glucan formation
    • Kim, D., H. J. Ryu, S. Chiba, A. Kimura, and D. F. Day. 2000. Purification and partial characterization of a novel glucanhydrolase from Lipomyces starkeyi KSM 22 and its use for inhibition of insoluble glucan formation. Biosci. Biotechnol. Biochem. 64: 223-228.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 223-228
    • Kim, D.1    Ryu, H.J.2    Chiba, S.3    Kimura, A.4    Day, D.F.5
  • 25
    • 0031892914 scopus 로고    scopus 로고
    • The pharmacology and kinetics of ectonucleotidases in the perilymphatic compartment of the guinea-pig cochlea
    • Srdjan, M. V., R. T. Peter, D. H. Gary, J. B. M. David, and S. K. Ingrid. 1998. The pharmacology and kinetics of ectonucleotidases in the perilymphatic compartment of the guinea-pig cochlea. Hearing Res. 117: 71-80.
    • (1998) Hearing Res. , vol.117 , pp. 71-80
    • Srdjan, M.V.1    Peter, R.T.2    Gary, D.H.3    David, J.B.M.4    Ingrid, S.K.5
  • 26
    • 85004570849 scopus 로고
    • Quantitative study of the anomeric forms of isomaltose and glucose produced by isomalto-dextranase and glucodextranase
    • Takayanagi, T., G. Okada, and S. Chiba. 1987. Quantitative study of the anomeric forms of isomaltose and glucose produced by isomalto-dextranase and glucodextranase. Agric. Biol. Chem. 51: 2337-2341.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2337-2341
    • Takayanagi, T.1    Okada, G.2    Chiba, S.3
  • 27
    • 0037525964 scopus 로고    scopus 로고
    • Evidence for a single active site on isomalto-dextranase with hydrolysis activities of α-1,6- and α-1,4-glucosidic linkages
    • Takayanagi, T., A. Kimura, H. Matsui, G. Okada, and S. Chiba. 2001. Evidence for a single active site on isomalto-dextranase with hydrolysis activities of α-1,6- and α-1,4-glucosidic linkages. J. Appl. Glycosci. 48: 55-61.
    • (2001) J. Appl. Glycosci. , vol.48 , pp. 55-61
    • Takayanagi, T.1    Kimura, A.2    Matsui, H.3    Okada, G.4    Chiba, S.5
  • 28
    • 0034802384 scopus 로고    scopus 로고
    • Highly branched glucooligosaccharide and mannitol production by mixed culture fermentation of Leuconostoc mesenteroides and Lipomyces starkeyi
    • Yoo, S. K., D. Kim, and D. F. Day. 2001. Highly branched glucooligosaccharide and mannitol production by mixed culture fermentation of Leuconostoc mesenteroides and Lipomyces starkeyi. J. Microbiol. Biotechnol. 11: 700-703.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 700-703
    • Yoo, S.K.1    Kim, D.2    Day, D.F.3
  • 29
    • 0035160955 scopus 로고    scopus 로고
    • Co-production of dextran and mannitol by Leuconostoc mesenteroides
    • Yoo, S. K., D. Kim, and D. F. Day. 2001. Co-production of dextran and mannitol by Leuconostoc mesenteroides. J. Microbiol. Biotechnol. 11: 880-883.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 880-883
    • Yoo, S.K.1    Kim, D.2    Day, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.