메뉴 건너뛰기




Volumn 63, Issue 2, 1999, Pages 154-165

Enzymatic grafting of a natural product onto chitosan to confer water solubility under basic conditions

Author keywords

Chitosan; Chlorogenic acid; Enzyme; Polymer modification; Tyrosinase

Indexed keywords

AMINES; BIOPOLYMERS; CARBOXYLIC ACIDS; CHEMICAL MODIFICATION; COMPOSITION EFFECTS; ENZYMES; GRAFTING (CHEMICAL); KETONES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH EFFECTS; SOLUBILITY; SUBSTRATES;

EID: 0033586801     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19990420)63:2<154::AID-BIT4>3.0.CO;2-R     Document Type: Article
Times cited : (179)

References (56)
  • 2
    • 84986928093 scopus 로고
    • Peroxidase-catalyzed synthesis of lign-in-phenol copolymers
    • Blinkovsky AM, Dordick JS. 1993. Peroxidase-catalyzed synthesis of lign-in-phenol copolymers. J Polym Sci 31:1839-1846.
    • (1993) J Polym Sci , vol.31 , pp. 1839-1846
    • Blinkovsky, A.M.1    Dordick, J.S.2
  • 5
    • 37049104378 scopus 로고
    • Addition of primary aliphatic amines to 1,2-benzoquinone. The absence of reaction between a secondary amide and 1,2-benzoquinone
    • Davies R, Frahn JL. 1977. Addition of primary aliphatic amines to 1,2-benzoquinone. The absence of reaction between a secondary amide and 1,2-benzoquinone. J Chem Soc, Perkin Trans I 89:2295-2297.
    • (1977) J Chem Soc, Perkin Trans I , vol.89 , pp. 2295-2297
    • Davies, R.1    Frahn, J.L.2
  • 6
    • 0000704968 scopus 로고
    • Evaluation of infrared spectroscopic techniques for analysing chitosan
    • Domszey JG, Roberts GAF. 1985. Evaluation of infrared spectroscopic techniques for analysing chitosan. Makromol Chem 186:1671-1677.
    • (1985) Makromol Chem , vol.186 , pp. 1671-1677
    • Domszey, J.G.1    Roberts, G.A.F.2
  • 7
    • 0026674982 scopus 로고
    • Enzymatic and chemoenzymatic approaches to polymer synthesis
    • Dordick JS. 1992. Enzymatic and chemoenzymatic approaches to polymer synthesis. Trends Biotechnol 10:287-293.
    • (1992) Trends Biotechnol , vol.10 , pp. 287-293
    • Dordick, J.S.1
  • 8
    • 0014939358 scopus 로고
    • Physiochemical and kinetic properties of mushroom tyrosinase
    • Duckworth HW, Coleman JE. 1970. Physiochemical and kinetic properties of mushroom tyrosinase. J Biol Chem 245:1613-1625.
    • (1970) J Biol Chem , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 9
    • 2842525944 scopus 로고    scopus 로고
    • Food browning and its prevention: An overview
    • Friedman M. 1996. Food browning and its prevention: An overview. J Agric Food Chem 44:631-653.
    • (1996) J Agric Food Chem , vol.44 , pp. 631-653
    • Friedman, M.1
  • 10
    • 0004119275 scopus 로고    scopus 로고
    • Hydrophilic polymers
    • Washington DC: American Chemical Society
    • Glass JE. 1996. Hydrophilic polymers. ACS Advances in Chemistry Series 248. Washington DC: American Chemical Society.
    • (1996) ACS Advances in Chemistry Series 248 , vol.248
    • Glass, J.E.1
  • 11
    • 0000976865 scopus 로고
    • Synthesis of N-[(3-hydroxy-2,3-dicarboxy)ethyl]chitosan: A new water-soluble chitosan derivative. Communication to the editor
    • Gruber JV, Rutar V, Bandekar J, Konish PN. 1995. Synthesis of N-[(3-hydroxy-2,3-dicarboxy)ethyl]chitosan: A new water-soluble chitosan derivative. Communication to the editor. Macromolecules 28: 8865-8867
    • (1995) Macromolecules , vol.28 , pp. 8865-8867
    • Gruber, J.V.1    Rutar, V.2    Bandekar, J.3    Konish, P.N.4
  • 13
    • 0032477983 scopus 로고    scopus 로고
    • Enzymatic tempering of a mussel adhesive protein film
    • Hansen DC, Corcoran SG, Waite JH. 1998. Enzymatic tempering of a mussel adhesive protein film. Langmuir 14:1139-1147.
    • (1998) Langmuir , vol.14 , pp. 1139-1147
    • Hansen, D.C.1    Corcoran, S.G.2    Waite, J.H.3
  • 14
    • 0016943565 scopus 로고
    • Selective N-acetylation of chitosan
    • Hirano S, Ohe Y, Ono H. 1976. Selective N-acetylation of chitosan. Carbohydr Res 47:315-320.
    • (1976) Carbohydr Res , vol.47 , pp. 315-320
    • Hirano, S.1    Ohe, Y.2    Ono, H.3
  • 15
    • 0027275812 scopus 로고
    • Solid slate NMR analysis of crosslinking in mussel protein glue
    • Holl SM, Hansen D, Waite JH, Schaefer J. 1993. Solid slate NMR analysis of crosslinking in mussel protein glue. Arch Biochem Biophys 302: 255-258.
    • (1993) Arch Biochem Biophys , vol.302 , pp. 255-258
    • Holl, S.M.1    Hansen, D.2    Waite, J.H.3    Schaefer, J.4
  • 16
    • 84948495968 scopus 로고
    • Effects of acylation and crosslinking on the material properties and cadmium ion adsorption capacity of porous chitosan heads
    • Hsien T-Y, Rorrer GR. 1995. Effects of acylation and crosslinking on the material properties and cadmium ion adsorption capacity of porous chitosan heads. Sep Sci Technol 30:2455-2475.
    • (1995) Sep Sci Technol , vol.30 , pp. 2455-2475
    • Hsien, T.-Y.1    Rorrer, G.R.2
  • 17
    • 84981890184 scopus 로고
    • Collagen-based bioadhesive barnacle cement mimic. I. Chemical and enzymatic studies
    • Kaleem K, Chertok F, Erhan S. 1987. Collagen-based bioadhesive barnacle cement mimic. I. Chemical and enzymatic studies. Angew Makromol Chem 155:31-43.
    • (1987) Angew Makromol Chem , vol.155 , pp. 31-43
    • Kaleem, K.1    Chertok, F.2    Erhan, S.3
  • 18
    • 0347600896 scopus 로고    scopus 로고
    • Enzymes in polymer science: An introduction
    • Gross RA, Kaplan DL, and Swift G, editors. Washington DC: American Chemical Society
    • Kaplan DL, Dordick JS, Gross RA, Swift, G., 1998. Enzymes in polymer science: An introduction. In Gross RA, Kaplan DL, and Swift G, editors. Enzymes in Polymer Synthesis. ACS Symposium Series 684. Washington DC: American Chemical Society, p 2-16.
    • (1998) Enzymes in Polymer Synthesis. ACS Symposium Series 684 , vol.684 , pp. 2-16
    • Kaplan, D.L.1    Dordick, J.S.2    Gross, R.A.3    Swift, G.4
  • 19
    • 0019945365 scopus 로고
    • Mammalian tyrosinase catalyzes three reactions in the biosynthesis of melanin
    • Korner A, Pawelek J. 1982. Mammalian tyrosinase catalyzes three reactions in the biosynthesis of melanin. Science 217:1163-1165.
    • (1982) Science , vol.217 , pp. 1163-1165
    • Korner, A.1    Pawelek, J.2
  • 22
    • 0000838740 scopus 로고
    • Assay of catechol oxidase: A critical comparison of methods
    • Mayer AM, Harel E, Ben-Shaul R. 1966. Assay of catechol oxidase: A critical comparison of methods. Phytochemistry 5:783-789.
    • (1966) Phytochemistry , vol.5 , pp. 783-789
    • Mayer, A.M.1    Harel, E.2    Ben-Shaul, R.3
  • 23
    • 0001839429 scopus 로고
    • Chitosan gels. 1. Study of reaction variables
    • Moore GK, Roberts GAF. 1980a. Chitosan gels. 1. Study of reaction variables. Int J Biol Macromol 2:73-77.
    • (1980) Int J Biol Macromol , vol.2 , pp. 73-77
    • Moore, G.K.1    Roberts, G.A.F.2
  • 25
    • 24744459160 scopus 로고
    • Carboxymethylated chitins and chitosan
    • Muzzarelli RAA. 1988. Carboxymethylated chitins and chitosan. Carbohydr Polym 8:1-21.
    • (1988) Carbohydr Polym , vol.8 , pp. 1-21
    • Muzzarelli, R.A.A.1
  • 26
    • 0027928653 scopus 로고
    • Chitosans carrying the methoxyphenyl functions typical of lignin
    • Muzzarelli RAA, Ilari P. 1994. Chitosans carrying the methoxyphenyl functions typical of lignin. Carbohydr Polym 23:155-160.
    • (1994) Carbohydr Polym , vol.23 , pp. 155-160
    • Muzzarelli, R.A.A.1    Ilari, P.2
  • 28
    • 0001007479 scopus 로고
    • N-(carboxymethylidene)chitosans and N-(carboxymethyl)chitosans: Novel chelating polyampholytes obtained from chitosan glyoxalate
    • Muzzarelli RAA, Taniani F, Emanuelli M, Marioth S. 1982. N-(Carboxymethylidene)chitosans and N-(carboxymethyl)chitosans: Novel chelating polyampholytes obtained from chitosan glyoxalate. Carbohydr Res 107:199-214.
    • (1982) Carbohydr Res , vol.107 , pp. 199-214
    • Muzzarelli, R.A.A.1    Taniani, F.2    Emanuelli, M.3    Marioth, S.4
  • 30
    • 0019304566 scopus 로고
    • Covalent binding of aromatic amines to humates. 1. Reaction with carbonyls and quinones
    • Parris GE. 1980. Covalent binding of aromatic amines to humates. 1. Reaction with carbonyls and quinones. Environ Sci Technol 14: 1099-1106.
    • (1980) Environ Sci Technol , vol.14 , pp. 1099-1106
    • Parris, G.E.1
  • 31
    • 0004773996 scopus 로고
    • Enzymes in polymer chemistry. 6. Lipase-catalyzed acylation of comb-like methacrylic polymers containing OH groups in the side chain
    • Pavel K, Ritter H. 1992. Enzymes in polymer chemistry. 6. Lipase-catalyzed acylation of comb-like methacrylic polymers containing OH groups in the side chain. Makromol Chem 193:323-328.
    • (1992) Makromol Chem , vol.193 , pp. 323-328
    • Pavel, K.1    Ritter, H.2
  • 32
    • 0030231079 scopus 로고    scopus 로고
    • Enzyme-catalyzed polymer modification: Reaction of phenolic compounds with chitosan films
    • Payne GF, Chaubal MV, Barbari TA. 1996. Enzyme-catalyzed polymer modification: Reaction of phenolic compounds with chitosan films. Polymer 37:4643-4648.
    • (1996) Polymer , vol.37 , pp. 4643-4648
    • Payne, G.F.1    Chaubal, M.V.2    Barbari, T.A.3
  • 33
    • 0024662764 scopus 로고
    • Chemcial modifications of biopolymers by quinones and quinone methides
    • Peter MG. 1989. Chemcial modifications of biopolymers by quinones and quinone methides. Angew Chem, Int Ed Engl 28:555-570.
    • (1989) Angew Chem, Int Ed Engl , vol.28 , pp. 555-570
    • Peter, M.G.1
  • 34
    • 0026409547 scopus 로고
    • Incorporation of p-cresol into lignins via peroxidase-catalyzed copolymerization in nonaqueous media
    • Popp JL, Kirk TK, Dordick JS. 1991. Incorporation of p-cresol into lignins via peroxidase-catalyzed copolymerization in nonaqueous media. Enzyme Microb Technol 13:964-968.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 964-968
    • Popp, J.L.1    Kirk, T.K.2    Dordick, J.S.3
  • 35
    • 0004739025 scopus 로고
    • Enzymatisch katalysierte peptidknupfung von alanin an phenylalaninhaltige methacrylpolmere mittels α-chymotrypsin
    • Rehse H, Ritter H. 1988. Enzymatisch katalysierte Peptidknupfung von Alanin an phenylalaninhaltige Methacrylpolmere mittels α-Chymotrypsin. Makromol Chem 189:529-539.
    • (1988) Makromol Chem , vol.189 , pp. 529-539
    • Rehse, H.1    Ritter, H.2
  • 36
    • 0000120206 scopus 로고
    • Oxidation of chlorogenic acid, catechins. And 4-methylcatechol in model solutions by apple polyphenol oxidase
    • Richard-Forget FC, Rouet-Mayer M-A, Goupy PM, Philippon P, Nicolas JJ. 1992. Oxidation of chlorogenic acid, catechins. and 4-methylcatechol in model solutions by apple polyphenol oxidase. J Agric Food Chem 40:2114-2122.
    • (1992) J Agric Food Chem , vol.40 , pp. 2114-2122
    • Richard-Forget, F.C.1    Rouet-Mayer, M.-A.2    Goupy, P.M.3    Philippon, P.4    Nicolas, J.J.5
  • 38
    • 0000793343 scopus 로고
    • Chitosan gels. 3. (a) the formation of gels by reaction of chitosan with glutaraldehyde
    • Roberts GAF, Taylor KE. 1989. Chitosan gels. 3. (a) The formation of gels by reaction of chitosan with glutaraldehyde. Makromol Chem 190: 951-960.
    • (1989) Makromol Chem , vol.190 , pp. 951-960
    • Roberts, G.A.F.1    Taylor, K.E.2
  • 40
    • 49349124836 scopus 로고
    • Studies on chitin. 7. IR spectroscopic determination of degree of deacetylation. Notes to the editor
    • Sannan T, Kurita K, Ogura K, Iwakura Y. 1978. Studies on chitin. 7. IR spectroscopic determination of degree of deacetylation. Notes to the editor. Polymer 19:458-459.
    • (1978) Polymer , vol.19 , pp. 458-459
    • Sannan, T.1    Kurita, K.2    Ogura, K.3    Iwakura, Y.4
  • 42
    • 0029875759 scopus 로고    scopus 로고
    • Evaluation of different absorbance ratios from infrared spectroscopy for analyzing the degree of deacetylation in chitin
    • Shigemasa Y, Matsuura H, Sashiwa H, Saimoto H. 1996. Evaluation of different absorbance ratios from infrared spectroscopy for analyzing the degree of deacetylation in chitin. Int J Biol Macromol 18:237-242.
    • (1996) Int J Biol Macromol , vol.18 , pp. 237-242
    • Shigemasa, Y.1    Matsuura, H.2    Sashiwa, H.3    Saimoto, H.4
  • 44
    • 0024490109 scopus 로고
    • Oxidative co-oligomerization of guaiacol and 4-chloroaniline
    • Simmons KE, Minard RD, Bollag J-M. 1989. Oxidative co-oligomerization of guaiacol and 4-chloroaniline. Environ Sci Technol 23: 115-121.
    • (1989) Environ Sci Technol , vol.23 , pp. 115-121
    • Simmons, K.E.1    Minard, R.D.2    Bollag, J.-M.3
  • 46
    • 77956776805 scopus 로고
    • Molecular mechanisms for cuticular sclerotization
    • Sugumaran M. 1988. Molecular mechanisms for cuticular sclerotization. Adv Insect Physiol 21:179-231.
    • (1988) Adv Insect Physiol , vol.21 , pp. 179-231
    • Sugumaran, M.1
  • 47
    • 0025764070 scopus 로고
    • Quinone methide as a new intermediate in eumelanin biosynthesis
    • Sugumaran M, Semensi V. 1991. Quinone methide as a new intermediate in eumelanin biosynthesis. J Biol Chem 266:6073-6078.
    • (1991) J Biol Chem , vol.266 , pp. 6073-6078
    • Sugumaran, M.1    Semensi, V.2
  • 48
    • 0030570418 scopus 로고    scopus 로고
    • Tyrosinase containing chitosan gels: A combined catalyst and sorbent for selective phenol removal
    • Sun W-Q, Payne GF. 1996. Tyrosinase containing chitosan gels: A combined catalyst and sorbent for selective phenol removal. Biotechnol Bioeng 51:79-86.
    • (1996) Biotechnol Bioeng , vol.51 , pp. 79-86
    • Sun, W.-Q.1    Payne, G.F.2
  • 49
    • 0001587318 scopus 로고
    • Directions for environmentally biodegradable polymer research
    • Swift G. 1993. Directions for environmentally biodegradable polymer research. Acc Chem Res 26:105-110.
    • (1993) Acc Chem Res , vol.26 , pp. 105-110
    • Swift, G.1
  • 50
    • 0027955317 scopus 로고
    • Enzyme-mediated coupling of 3,4-dichloroaniline with ferulic acid: A model for pollutant binding to humic materials
    • Tatsumi K, Freyer A, Minard RD, Bollag JM. 1994. Enzyme-mediated coupling of 3,4-dichloroaniline with ferulic acid: A model for pollutant binding to humic materials. Environ Sci Technol 28:210-215.
    • (1994) Environ Sci Technol , vol.28 , pp. 210-215
    • Tatsumi, K.1    Freyer, A.2    Minard, R.D.3    Bollag, J.M.4
  • 52
    • 0029659995 scopus 로고    scopus 로고
    • Covalent binding of aniline to humic substances. 1. Kinetic studies
    • Weber EJ, Spidle DL, Thorn KA. 1996. Covalent binding of aniline to humic substances. 1. Kinetic studies. Environ Sci Technol 30: 2755-2763.
    • (1996) Environ Sci Technol , vol.30 , pp. 2755-2763
    • Weber, E.J.1    Spidle, D.L.2    Thorn, K.A.3
  • 54
    • 0030572089 scopus 로고    scopus 로고
    • Chitosan film acylation and effects on biodegradability
    • Xu J, McCarthy SP, Gross RA, Kaplan DL. 1996. Chitosan film acylation and effects on biodegradability. Macromolecules 29:3436-3440.
    • (1996) Macromolecules , vol.29 , pp. 3436-3440
    • Xu, J.1    McCarthy, S.P.2    Gross, R.A.3    Kaplan, D.L.4
  • 55
    • 16344366954 scopus 로고
    • Some chemical and analytical aspects of polysaccharide modifications. Formation of branched-chain, soluble chitosan derivatives
    • Yalpani M, Hall LD. 1984. Some chemical and analytical aspects of polysaccharide modifications. Formation of branched-chain, soluble chitosan derivatives. Macromolecules 17:272-281.
    • (1984) Macromolecules , vol.17 , pp. 272-281
    • Yalpani, M.1    Hall, L.D.2
  • 56
    • 0031898225 scopus 로고    scopus 로고
    • Trypsin purification by p-aminobenzamidine immobilized on macroporous chitosan membranes
    • Zeng X, Ruckenstein E. 1998. Trypsin purification by p-aminobenzamidine immobilized on macroporous chitosan membranes. Ind Eng Chem Res 37:159-165.
    • (1998) Ind Eng Chem Res , vol.37 , pp. 159-165
    • Zeng, X.1    Ruckenstein, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.