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Volumn 66, Issue 1, 1999, Pages 35-41

Substrate heterogeneity causes the nonlinear kinetics of insoluble cellulose hydrolysis

Author keywords

Cellulase; Cellulose hydrolysis; Enzyme inactivation; Nonlinear kinetics; Substrate heterogeneity; Thermomonospora fusca

Indexed keywords

ACTIVATION ENERGY; BIODEGRADATION; CATALYSIS; CATALYST ACTIVITY; ENZYMES; HYDROLYSIS; REACTION KINETICS;

EID: 0033230682     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(1999)66:1<35::AID-BIT3>3.0.CO;2-G     Document Type: Article
Times cited : (93)

References (26)
  • 2
    • 0032580960 scopus 로고    scopus 로고
    • Activesite binding of glycosides by Thermomonospora fusca endocellulase E2
    • Barr BK, Wolfgang DE, Piens K, Claeyssens M, Wilson DB. 1998. Activesite binding of glycosides by Thermomonospora fusca endocellulase E2. Biochemistry. 37:9220-9229.
    • (1998) Biochemistry , vol.37 , pp. 9220-9229
    • Barr, B.K.1    Wolfgang, D.E.2    Piens, K.3    Claeyssens, M.4    Wilson, D.B.5
  • 3
    • 0025908702 scopus 로고
    • The endo-1,4-β-glucanase I from Trichoderma reesei: Action of β-1,4-oligomers and polymers derived from D-glucose and D-xylose
    • Biely P, Vrsanska M, Claeysens M. 1991. The endo-1,4-β-glucanase I from Trichoderma reesei: Action of β-1,4-oligomers and polymers derived from D-glucose and D-xylose. Eur J Biochem 200:157-163.
    • (1991) Eur J Biochem , vol.200 , pp. 157-163
    • Biely, P.1    Vrsanska, M.2    Claeysens, M.3
  • 4
    • 0031148766 scopus 로고    scopus 로고
    • Binding capacities for Thermomonospora fusca E3, E4 and E5, the E3 binding domain, and Trichoderma reesei CBHI on Avicel and bacterial microcrystalline cellulose
    • Bothwell M, Daughhetee S, Chaua G, Wilson DB, Walker L. 1997. Binding capacities for Thermomonospora fusca E3, E4 and E5, the E3 binding domain, and Trichoderma reesei CBHI on Avicel and bacterial microcrystalline cellulose. Bioresource Technol 60:169-178.
    • (1997) Bioresource Technol , vol.60 , pp. 169-178
    • Bothwell, M.1    Daughhetee, S.2    Chaua, G.3    Wilson, D.B.4    Walker, L.5
  • 5
    • 0026792646 scopus 로고
    • Influence of β-glucosidase on the filter paper activity and hydrolysis of lignocellulosic substrates
    • Breuil C, Chan M, Gilbert M, Saddler JN. 1991. Influence of β-glucosidase on the filter paper activity and hydrolysis of lignocellulosic substrates. Bioresource Technol 39:139-142.
    • (1991) Bioresource Technol , vol.39 , pp. 139-142
    • Breuil, C.1    Chan, M.2    Gilbert, M.3    Saddler, J.N.4
  • 6
    • 0022311468 scopus 로고
    • Purification and characterization of two β-1,4-endoglucanases from Thermomonospora fusca
    • Calza RE, Irwin DC, Wilson DB. 1985. Purification and characterization of two β-1,4-endoglucanases from Thermomonospora fusca. Biochemistry 24:7797-7804.
    • (1985) Biochemistry , vol.24 , pp. 7797-7804
    • Calza, R.E.1    Irwin, D.C.2    Wilson, D.B.3
  • 7
    • 0002831168 scopus 로고
    • Fogarty WM, Kelley CT, editors. London: Elsevier Applied Science
    • Coughlan M. 1990. In: Fogarty WM, Kelley CT, editors. Microbial Enzymes and Biotechnology. London: Elsevier Applied Science. p 1-36.
    • (1990) Microbial Enzymes and Biotechnology , pp. 1-36
    • Coughlan, M.1
  • 8
    • 0343487590 scopus 로고    scopus 로고
    • Substrate reactivity as a function of the extent of reaction in the enzymatic hydrolysis of cellulose
    • Desai SC, Converse AO. 1997. Substrate reactivity as a function of the extent of reaction in the enzymatic hydrolysis of cellulose. Biotechnol Bioeng 56:650-655.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 650-655
    • Desai, S.C.1    Converse, A.O.2
  • 9
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin D, Walker L, Spezio M, Wilson D. 1993. Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects. Biotechnol Bioeng 42:1002-1013.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 1002-1013
    • Irwin, D.1    Walker, L.2    Spezio, M.3    Wilson, D.4
  • 11
    • 0027909738 scopus 로고
    • A new approach for modeling cellulase-cellulose adsorption and the kinetics of hydrolysis of cellulose
    • Nidetzky B, Steiner W. 1993. A new approach for modeling cellulase-cellulose adsorption and the kinetics of hydrolysis of cellulose. Biotechnol Bioeng 42:469-479.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 469-479
    • Nidetzky, B.1    Steiner, W.2
  • 12
    • 0002348686 scopus 로고
    • Synergistic interaction of cellulases from Trichoderma reesei during cellulose degradation
    • Saddler JN, MHP, editor. Washington DC: American Chemical Society
    • Nidetzky B, Steiner W, Claeyssens M. 1995. Synergistic interaction of cellulases from Trichoderma reesei during cellulose degradation. In: Saddler JN, MHP, editor. Enzymatic degradation of insoluble carbohydrate. Washington DC: American Chemical Society. p 90-112.
    • (1995) Enzymatic Degradation of Insoluble Carbohydrate , pp. 90-112
    • Nidetzky, B.1    Steiner, W.2    Claeyssens, M.3
  • 13
    • 0028353231 scopus 로고
    • Cellulose hydrolysis by the cellulases from Trichoderma reesei: A new model for synergistic interaction
    • Nidetzky B, Steiner W, Hayn M, Claeyssens, M. 1994. Cellulose hydrolysis by the cellulases from Trichoderma reesei: A new model for synergistic interaction. Biochem J 298:705-710.
    • (1994) Biochem J , vol.298 , pp. 705-710
    • Nidetzky, B.1    Steiner, W.2    Hayn, M.3    Claeyssens, M.4
  • 14
    • 0024641809 scopus 로고
    • The effect of enzyme concentration on the rate of the hydrolysis of cellulose
    • Sattler W, Esterbauer H, Glatter O, Steiner W. 1989. The effect of enzyme concentration on the rate of the hydrolysis of cellulose. Biotechnol Bioeng 33:1221-1234.
    • (1989) Biotechnol Bioeng , vol.33 , pp. 1221-1234
    • Sattler, W.1    Esterbauer, H.2    Glatter, O.3    Steiner, W.4
  • 15
    • 0027381121 scopus 로고
    • Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases
    • Schou C, Rasmussen G, Katoft MB, Henrissat B, Schulein M. 1993. Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases. Eur J Biochem FEBS 217:947-953.
    • (1993) Eur J Biochem FEBS , vol.217 , pp. 947-953
    • Schou, C.1    Rasmussen, G.2    Katoft, M.B.3    Henrissat, B.4    Schulein, M.5
  • 17
    • 0027385038 scopus 로고
    • Crystal structure of the catalytic domain of a thermophilic endocellulase
    • Spezio M, Wilson DB, Karplus PA. 1993. Crystal structure of the catalytic domain of a thermophilic endocellulase. Biochemistry 32:9906-9916.
    • (1993) Biochemistry , vol.32 , pp. 9906-9916
    • Spezio, M.1    Wilson, D.B.2    Karplus, P.A.3
  • 18
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • Teeri T. 1997. Crystalline cellulose degradation: New insight into the function of cellobiohydrolases. Trends Biotechnol 15:160-167.
    • (1997) Trends Biotechnol , vol.15 , pp. 160-167
    • Teeri, T.1
  • 19
    • 0027910079 scopus 로고
    • Engineering cellulase mixtures by varying the mole fraction of Thermomonospora fusca E5 and E3, Trichoderma reesei CBHI, and Caldocellulosiruptor saccharotyticum β-glucosidase
    • Walker LP, Belair CD, Wilson DB, Irwin DC. 1993. Engineering cellulase mixtures by varying the mole fraction of Thermomonospora fusca E5 and E3, Trichoderma reesei CBHI, and Caldocellulosiruptor saccharotyticum β-glucosidase. Biotechnol Bioeng 42:1019-1028.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 1019-1028
    • Walker, L.P.1    Belair, C.D.2    Wilson, D.B.3    Irwin, D.C.4
  • 20
    • 0029843079 scopus 로고    scopus 로고
    • Microbial hydrolysis of polysaccharides
    • Warren RAJ. 1996. Microbial hydrolysis of polysaccharides. Annu Rev Microbiol 50:183-212.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 183-212
    • Warren, R.A.J.1
  • 21
    • 0001434836 scopus 로고
    • Cellulases of Thermomonospora fusca
    • Wilson DB. 1988. Cellulases of Thermomonospora fusca. Methods Enzymol 160:314-323.
    • (1988) Methods Enzymol , vol.160 , pp. 314-323
    • Wilson, D.B.1
  • 22
  • 24
    • 0025881549 scopus 로고
    • Synergism in cellulase systems
    • Woodward J. 1991. Synergism in cellulase systems. Bioresource Technol 36:67-75.
    • (1991) Bioresource Technol , vol.36 , pp. 67-75
    • Woodward, J.1
  • 25
    • 0002556081 scopus 로고
    • Ethanol and methanol from cellulosic biomass
    • RL, Johannson TE, Kelly H, Reddy AKN, Williams RA, editors. Washington, DC: Island Press
    • Wyman DKB, RL, Hinman ND, Stevens DJ. 1993. Ethanol and methanol from cellulosic biomass. In: Johannson TE, Kelly H, Reddy AKN, Williams RA, editors. Renewable energy: Sources for fuels and electricity. Washington, DC: Island Press. p 865-923.
    • (1993) Renewable Energy: Sources for Fuels and Electricity , pp. 865-923
    • Wyman, D.K.B.1    Hinman, N.D.2    Stevens, D.J.3
  • 26
    • 0343472021 scopus 로고    scopus 로고
    • Surface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2
    • Zhang S, Wilson DB. 1997. Surface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2. J Biotechnol 57: 101-113.
    • (1997) J Biotechnol , vol.57 , pp. 101-113
    • Zhang, S.1    Wilson, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.