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Volumn 74, Issue 7, 1999, Pages 635-638

Stabilization of α-amylase by chemical modification with carboxymethylcellulose

Author keywords

Carboxymethylcellulose; Enzyme stability; Modified enzyme; amylase

Indexed keywords

AMYLASE; CARBOXYMETHYLCELLULOSE; DODECYL SULFATE SODIUM; PERIODATE; UREA;

EID: 0039728742     PISSN: 02682575     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4660(199907)74:7<635::AID-JCTB85>3.0.CO;2-M     Document Type: Article
Times cited : (38)

References (21)
  • 2
    • 0022444792 scopus 로고
    • Application of polyethylene glycol-modified enzymes in biotechnological processes: Organic solvent-soluble enzymes
    • Inada Y, Takahashi K, Yoshimoto T, Ajima A, Matsushima A and Saito Y, Application of polyethylene glycol-modified enzymes in biotechnological processes: organic solvent-soluble enzymes. TIBTECH 4:190-194 (1986).
    • (1986) TIBTECH , vol.4 , pp. 190-194
    • Inada, Y.1    Takahashi, K.2    Yoshimoto, T.3    Ajima, A.4    Matsushima, A.5    Saito, Y.6
  • 3
    • 0027253357 scopus 로고
    • The conjugation of proteins with polyethylene glycol and other polymers: Altering properties of proteins to enhance their therapeutics potential
    • Katre NV, The conjugation of proteins with polyethylene glycol and other polymers: altering properties of proteins to enhance their therapeutics potential. Adv Drug Deliv Rev 10:91-114 (1993).
    • (1993) Adv Drug Deliv Rev , vol.10 , pp. 91-114
    • Katre, N.V.1
  • 4
    • 0020631378 scopus 로고
    • Modification of amino groups in porcine pancreatic elastase with polyethylene glycol in relation to binding ability towards anti-serum and to enzymatic activity
    • Koide A and Kobayashi S, Modification of amino groups in porcine pancreatic elastase with polyethylene glycol in relation to binding ability towards anti-serum and to enzymatic activity. Biochem Biophys Res Commun 111:659-667 (1983).
    • (1983) Biochem Biophys Res Commun , vol.111 , pp. 659-667
    • Koide, A.1    Kobayashi, S.2
  • 5
    • 0024447080 scopus 로고
    • Modification of two amino groups with polyethylene glycol causes a unique activity change of an alkaline proteinase from alkalophilic Bacillus sp.
    • Yamagata Y and Ichishima E, Modification of two amino groups with polyethylene glycol causes a unique activity change of an alkaline proteinase from alkalophilic Bacillus sp. Curr Microbiol 19:307-311 (1989).
    • (1989) Curr Microbiol , vol.19 , pp. 307-311
    • Yamagata, Y.1    Ichishima, E.2
  • 6
    • 0028250033 scopus 로고
    • r of poly(ethylene glycol) and the stability of horseradish peroxidase-poly(ethylene glycol) adducts under various denaturing conditions
    • r of poly(ethylene glycol) and the stability of horseradish peroxidase-poly(ethylene glycol) adducts under various denaturing conditions. Biotechnol Appl Biochem 20:397-413 (1994).
    • (1994) Biotechnol Appl Biochem , vol.20 , pp. 397-413
    • Laliberté, M.1    Gayet, J.-Ch.2    Fortier, G.3
  • 7
    • 0021759913 scopus 로고
    • Chymotrypsin modified with polyethylene glycol catalyzes peptide synthesis reaction in benzene
    • Matsushima A, Okada M and Inada Y, Chymotrypsin modified with polyethylene glycol catalyzes peptide synthesis reaction in benzene. FEBS Lett 178:275-277 (1984).
    • (1984) FEBS Lett , vol.178 , pp. 275-277
    • Matsushima, A.1    Okada, M.2    Inada, Y.3
  • 8
    • 0002670074 scopus 로고
    • Chemical modification of horseradish peroxidase with ethanal-methoxypolyethylene glycol: Solubility in organic solvents, activity and properties
    • Wirth P, Souppe J, Tritsch D and Biellmann J-F, Chemical modification of horseradish peroxidase with ethanal-methoxypolyethylene glycol: solubility in organic solvents, activity and properties. Bioorg Chem 19:133-142 (1991).
    • (1991) Bioorg Chem , vol.19 , pp. 133-142
    • Wirth, P.1    Souppe, J.2    Tritsch, D.3    Biellmann, J.-F.4
  • 9
    • 0025181633 scopus 로고
    • Alteration of biopharmaceutical properties of drugs by their conjugation with water-soluble macromolecules: Uricasedextran conjugate
    • Fujita T, Yasuda Y, Takakura Y, Hashida M and Sezaki H, Alteration of biopharmaceutical properties of drugs by their conjugation with water-soluble macromolecules: uricasedextran conjugate. J Control Release 11:149-156 (1990).
    • (1990) J Control Release , vol.11 , pp. 149-156
    • Fujita, T.1    Yasuda, Y.2    Takakura, Y.3    Hashida, M.4    Sezaki, H.5
  • 11
    • 0028347317 scopus 로고
    • Synthesis of the conjugate of superoxide dismutase with the copolymer of divinyl ether and maleic anhydride retaining enzymatic activity
    • Hirano T, Todoroki T, Kato S, Yamamoto H, Caliceti P, Veronese FM, Maeda H and Ohashi S, Synthesis of the conjugate of superoxide dismutase with the copolymer of divinyl ether and maleic anhydride retaining enzymatic activity. J Control Release 28:203-209 (1994).
    • (1994) J Control Release , vol.28 , pp. 203-209
    • Hirano, T.1    Todoroki, T.2    Kato, S.3    Yamamoto, H.4    Caliceti, P.5    Veronese, F.M.6    Maeda, H.7    Ohashi, S.8
  • 12
    • 0026689937 scopus 로고
    • Chemical modification of lipase with a comb-shaped synthetic copolymer of polyoxyethylene allyl methyl diether and maleic anhydride
    • Hiroto M, Matsushima A, Kodera Y, Shibata Y and Inada Y, Chemical modification of lipase with a comb-shaped synthetic copolymer of polyoxyethylene allyl methyl diether and maleic anhydride. Biotechnol Lett 14:559-564 (1992).
    • (1992) Biotechnol Lett , vol.14 , pp. 559-564
    • Hiroto, M.1    Matsushima, A.2    Kodera, Y.3    Shibata, Y.4    Inada, Y.5
  • 13
    • 0029140579 scopus 로고
    • Stabilization of trypsin by modification with comb-shaped copolymers of poly(ethylene glycol) derivative and maleic anhydride
    • Hiroto M, Yamada M, Ueno T, Yasukohchi T, Matsushima A, Kodera Y and Inada Y, Stabilization of trypsin by modification with comb-shaped copolymers of poly(ethylene glycol) derivative and maleic anhydride. Biotechnol Techniques 9:105-110 (1995).
    • (1995) Biotechnol Techniques , vol.9 , pp. 105-110
    • Hiroto, M.1    Yamada, M.2    Ueno, T.3    Yasukohchi, T.4    Matsushima, A.5    Kodera, Y.6    Inada, Y.7
  • 14
    • 33748037939 scopus 로고
    • Amylases α- and β-
    • Bernfeld P, Amylases α- and β-. Methods Enzymol 1:149-158 (1955).
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 15
    • 0013889689 scopus 로고
    • Determination of free amino groups in protein by trinitrobenzensulphonic acid
    • Habeeb AFSA, Determination of free amino groups in protein by trinitrobenzensulphonic acid. Anal Biochem 14:328-336 (1966).
    • (1966) Anal Biochem , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 16
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois MK, Gilles A, Hamilton JK, Rebers PA and Smith F, Colorimetric method for determination of sugars and related substances. Anal Chem 28:350-356 (1956).
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.K.1    Gilles, A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 18
    • 0001241394 scopus 로고
    • Étude des O-carboxyméthylcelluloses a degré de substitution variable. I. Préparation et caractérisation des produits
    • Rinaudo M and Hudry-Clergeon G, Étude des O-carboxyméthylcelluloses a degré de substitution variable. I. Préparation et caractérisation des produits. J Chim Phys 64:1746-1752 (1967).
    • (1967) J Chim Phys , vol.64 , pp. 1746-1752
    • Rinaudo, M.1    Hudry-Clergeon, G.2
  • 19
    • 0029957475 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites
    • Alkazaz M, Desseux V, Marchis-Mouren G, Payan F, Forest E and Santimone M, The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites Eur J Biochem 241:787-796 (1996).
    • (1996) Eur J Biochem , vol.241 , pp. 787-796
    • Alkazaz, M.1    Desseux, V.2    Marchis-Mouren, G.3    Payan, F.4    Forest, E.5    Santimone, M.6
  • 20
    • 0016636113 scopus 로고
    • Enzyme stabilisation by covalent attachment of carbohydrate
    • Marshall JJ and Rabinowitz ML, Enzyme stabilisation by covalent attachment of carbohydrate. Arch Biochem Biophys 167:777-779 (1975).
    • (1975) Arch Biochem Biophys , vol.167 , pp. 777-779
    • Marshall, J.J.1    Rabinowitz, M.L.2
  • 21
    • 0023661282 scopus 로고
    • Three-dimensional structure of porcine pancreatic α-amylase at 2.9Å resolution. Role of calcium in structure and activity
    • Buisson G, Duée E, Haser R and Payan F, Three-dimensional structure of porcine pancreatic α-amylase at 2.9Å resolution. Role of calcium in structure and activity. EMBO J 6:3909-3916 (1987).
    • (1987) EMBO J , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duée, E.2    Haser, R.3    Payan, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.