메뉴 건너뛰기




Volumn 133, Issue 3, 2002, Pages 351-360

Isolation, characterization and inhibition by acarbose of the α-amylase from Lactobacillus fermentum: Comparison with Lb. manihotivorans and Lb. plantarum amylases

Author keywords

Acarbose inhibition; Alpha amylase; Amylose hydrolysis kinetics; Lactobacillus fermentum; Lactobacillus manihotivorans; Lactobacillus plantarum; Maltooligosaccharides; Starch

Indexed keywords

ACARBOSE; AMYLASE; ENZYME INHIBITOR; GLYCOGEN; MALTOHEXAOSE; OLIGOSACCHARIDE; STARCH; MALTOSE; MALTOTRIOSE;

EID: 0036846703     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-4959(02)00157-4     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 0031662285 scopus 로고    scopus 로고
    • Isolation and characterization of new amylolytic strains of Lactobacillus fermentum from fermented maize doughs (mawè and ogi) from Benin
    • Agati V., Guyot J.P., Morlon-Guyot J., Talamond P., Hounhouigan D.J. Isolation and characterization of new amylolytic strains of Lactobacillus fermentum from fermented maize doughs (mawè and ogi) from Benin. J Appl. Microbiol. 85:1998;512-520.
    • (1998) J Appl. Microbiol. , vol.85 , pp. 512-520
    • Agati, V.1    Guyot, J.P.2    Morlon-Guyot, J.3    Talamond, P.4    Hounhouigan, D.J.5
  • 3
    • 0029957475 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites
    • Al Kazaz M., Desseaux V., Marchis-Mouren G., Payan F., Forest E., Santimone M. The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites. Eur. J. Biochem. 241:1996;787-796.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 787-796
    • Al Kazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Payan, F.4    Forest, E.5    Santimone, M.6
  • 4
    • 0021710691 scopus 로고
    • Rapid analysis of amino acids using pre-column derivation
    • Bidlingmeyer B.A., Cohen S.A., Tarvin T.L. Rapid analysis of amino acids using pre-column derivation. J. Chromatogr. 336:1984;93-104.
    • (1984) J. Chromatogr. , vol.336 , pp. 93-104
    • Bidlingmeyer, B.A.1    Cohen, S.A.2    Tarvin, T.L.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0025720463 scopus 로고
    • Partial purification and comparative characterization of α-amylase secreted by Lactobacillus amylovorus
    • Burgess-Cassler A., Imam S. Partial purification and comparative characterization of α-amylase secreted by Lactobacillus amylovorus. Curr. Microbiol. 23:1991;207-213.
    • (1991) Curr. Microbiol. , vol.23 , pp. 207-213
    • Burgess-Cassler, A.1    Imam, S.2
  • 8
    • 0014402263 scopus 로고
    • Sur la recherche du poids moléculaire le plus cohérent avec l'analyse des acides aminés d'une protéine
    • Delaage M. Sur la recherche du poids moléculaire le plus cohérent avec l'analyse des acides aminés d'une protéine. Biochim. Biophys. Acta. 168:1968;573-575.
    • (1968) Biochim. Biophys. Acta , vol.168 , pp. 573-575
    • Delaage, M.1
  • 9
    • 0013833244 scopus 로고
    • Determination of reducing sugar with improved precision
    • Dygert S., Li L.H., Florida D., Thoma J.A. Determination of reducing sugar with improved precision. Anal. Biochem. 13:1965;367-374.
    • (1965) Anal. Biochem. , vol.13 , pp. 367-374
    • Dygert, S.1    Li, L.H.2    Florida, D.3    Thoma, J.A.4
  • 10
    • 0034076894 scopus 로고    scopus 로고
    • Lactobacillus plantarum amylase acting on crude starch granules: Native isoforms and activity changes after limited proteolysis
    • Florêncio J.A., Eiras-Stofella D.R., Soccol C.R., Raimbault M., Guyot J.P., Fontana J.D. Lactobacillus plantarum amylase acting on crude starch granules: Native isoforms and activity changes after limited proteolysis. Appl. Biochem. Biotechnol. 84-86:2000;721-730.
    • (2000) Appl. Biochem. Biotechnol. , vol.84 , Issue.86 , pp. 721-730
    • Florêncio, J.A.1    Eiras-Stofella, D.R.2    Soccol, C.R.3    Raimbault, M.4    Guyot, J.P.5    Fontana, J.D.6
  • 11
    • 0029953633 scopus 로고    scopus 로고
    • Crystal structure of pig pancreatic α-amylase isoenzyme II in complex with carbohydrate inhibitor acarbose
    • Gilles C., Astier J.P., Marchis-Mouren G., Cambillan C., Payan F. Crystal structure of pig pancreatic α-amylase isoenzyme II in complex with carbohydrate inhibitor acarbose. Eur. J. Biochem. 238:1996;561-569.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 561-569
    • Gilles, C.1    Astier, J.P.2    Marchis-Mouren, G.3    Cambillan, C.4    Payan, F.5
  • 12
    • 0027304467 scopus 로고
    • Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6
    • Giraud E., Gosselin L., Marin B., Parada J.L., Raimbault M. Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6. J. Appl. Bacteriology. 75:1993;276-282.
    • (1993) J. Appl. Bacteriology , vol.75 , pp. 276-282
    • Giraud, E.1    Gosselin, L.2    Marin, B.3    Parada, J.L.4    Raimbault, M.5
  • 13
    • 0030724903 scopus 로고    scopus 로고
    • Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin
    • Giraud E., Cuny G. Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin. Gene. 198:1997;149-157.
    • (1997) Gene , vol.198 , pp. 149-157
    • Giraud, E.1    Cuny, G.2
  • 15
    • 2142749660 scopus 로고    scopus 로고
    • Mechanism of porcine pancreatic α-amylase. Inhibition of amylose and maltopentaose hydrolyis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose
    • Koukiekolo R., Le Berre-Anton V., Desseaux V., et al. Mechanism of porcine pancreatic α-amylase. Inhibition of amylose and maltopentaose hydrolyis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose. Eur. J. Biochem. 265:1999;20-26.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 20-26
    • Koukiekolo, R.1    Le Berre-Anton, V.2    Desseaux, V.3
  • 16
    • 0034832246 scopus 로고    scopus 로고
    • Mechanism of porcine α-amylase. Inhibition of amylose and maltopentaose hydrolysis by α-, β- and γ-cyclodextrins
    • Koukiekolo R., Desseaux V., Moreau Y., Marchis-Mouren G., Santimone M. Mechanism of porcine α-amylase. Inhibition of amylose and maltopentaose hydrolysis by α-, β- and γ-cyclodextrins. Eur. J. Biochem. 268:2001;841-848.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 841-848
    • Koukiekolo, R.1    Desseaux, V.2    Moreau, Y.3    Marchis-Mouren, G.4    Santimone, M.5
  • 17
    • 0019139168 scopus 로고
    • Renaturation of enzyme after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate
    • Lacks S.A., Springhorne S.S. Renaturation of enzyme after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. J. Biol. Chem. 225:1980;7467-7473.
    • (1980) J. Biol. Chem. , vol.225 , pp. 7467-7473
    • Lacks, S.A.1    Springhorne, S.S.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0001757520 scopus 로고
    • The glycogen-amylase complex as a means of obtaining highly purified α-amylases
    • Loyter A., Schramm M. The glycogen-amylase complex as a means of obtaining highly purified α-amylases. Biochim. Biophys. Acta. 65:1962;200-206.
    • (1962) Biochim. Biophys. Acta , vol.65 , pp. 200-206
    • Loyter, A.1    Schramm, M.2
  • 22
    • 0023473794 scopus 로고
    • Rapid isoelectric focusing in a vertical polyacrylamide minigel system
    • Robertson E.F., Dannelly H.K., Malloy P.J., Reeves H.C. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal. Biochem. 167:1987;290-294.
    • (1987) Anal. Biochem. , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 23
    • 0011287589 scopus 로고
    • Sas Institute Inc., Cary, NC, USA
    • SAS/STAT® User's Guide, V6, 4th Edition, Vol. 1, p. 643. Sas Institute Inc., 1989 Cary, NC, USA.
    • (1989) User's Guide, V6, 4th Edition , vol.1 , pp. 643
  • 25
    • 0000511865 scopus 로고    scopus 로고
    • Isoelectric focusing under denaturing conditions
    • J.M. Walker. Totowa, NJ: Human Press
    • Thurston C.F., Henley L.F. Isoelectric focusing under denaturing conditions. Walker J.M., The Protein Protocols Handbook. 1996;115-119 Human Press, Totowa, NJ.
    • (1996) The Protein Protocols Handbook , pp. 115-119
    • Thurston, C.F.1    Henley, L.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.