메뉴 건너뛰기




Volumn 266, Issue 2, 1999, Pages 327-334

Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I

Author keywords

Cellulase; Cellulose; Hydrolysis; Simulation; Synergism

Indexed keywords

ACID; CELLULOSE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; GLUCAN SYNTHASE; MICROCRYSTALLINE CELLULOSE; CELLULASE;

EID: 0033485705     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00853.x     Document Type: Article
Times cited : (128)

References (34)
  • 1
    • 0016275528 scopus 로고
    • The structure of native cellulose
    • 1. Gardner, H.K. & Blackwell, J. (1974) The structure of native cellulose. Biopolymers 13, 1975-2001.
    • (1974) Biopolymers , vol.13 , pp. 1975-2001
    • Gardner, H.K.1    Blackwell, J.2
  • 2
    • 0003098594 scopus 로고
    • Cellulose: A random walk along its historical path
    • 2. Hon, S.-N.D. (1994) Cellulose: a random walk along its historical path. Cellulose 1, 1-25.
    • (1994) Cellulose , vol.1 , pp. 1-25
    • Hon, S.-N.D.1
  • 3
    • 0019091445 scopus 로고
    • Major chemical and physical features of cellulosic materials as substrates for enzymatic hydrolysis
    • 3. Fan, T.L., Lee, H.-Y. & Beardmore, H.D. (1980) Major chemical and physical features of cellulosic materials as substrates for enzymatic hydrolysis, Adv. Biochem. Engineering 14, 101-117.
    • (1980) Adv. Biochem. Engineering , vol.14 , pp. 101-117
    • Fan, T.L.1    Lee, H.-Y.2    Beardmore, H.D.3
  • 4
    • 0002567210 scopus 로고
    • Structure of cellulose and its relation to properties of cellulose fibres
    • (Kennedy, F.J., Phillips, G.O., Wedlock, D.J. & Williams, P.A., eds). Horwood,Chichester
    • 4. Krässig, H. ( 1985) Structure of cellulose and its relation to properties of cellulose fibres. In Cellulose and its Derivatives (Kennedy, F.J., Phillips, G.O., Wedlock, D.J. & Williams, P.A., eds), pp. 3-25. Horwood, Chichester.
    • (1985) Cellulose and its Derivatives , pp. 3-25
    • Krässig, H.1
  • 6
    • 0000551058 scopus 로고
    • The action of 1,4-β-D-glucan cellobiohydrolase on Valonia cellulose microcrystals. An electron microscopic study
    • 6. Chanzy, H., Henrissat, B., Vuong, R. & Schülein, M. (1983) The action of 1,4-β-D-glucan cellobiohydrolase on Valonia cellulose microcrystals. An electron microscopic study. FEBS Lett. 153, 113-118.
    • (1983) FEBS Lett. , vol.153 , pp. 113-118
    • Chanzy, H.1    Henrissat, B.2    Vuong, R.3    Schülein, M.4
  • 7
    • 0000028633 scopus 로고
    • Unidirectional degradation of Valonia cellulose microcrystals subjected to cellulase action
    • 7. Chanzy, H. & Henrissat, B. (1985) Unidirectional degradation of Valonia cellulose microcrystals subjected to cellulase action. FEBS Lett. 184, 285-288.
    • (1985) FEBS Lett. , vol.184 , pp. 285-288
    • Chanzy, H.1    Henrissat, B.2
  • 8
    • 0032487130 scopus 로고    scopus 로고
    • Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes
    • 8. Medve, J., Karlsson, J., Lee, D. & Tjerneld, F. (1998) Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: adsorption, sugar production pattern, and synergism of the enzymes. Biotechnol. Bioeng. 59, 621-634.
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 621-634
    • Medve, J.1    Karlsson, J.2    Lee, D.3    Tjerneld, F.4
  • 9
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50Å long tunnel of cellobiohydrolase I from Trichoderma reesei
    • 9. Divne, C., Ståhlberg, J., Teeri, T.T. & Jones, A.T. (1998) High-resolution crystal structures reveal how a cellulose chain is bound in the 50Å long tunnel of cellobiohydrolase I from Trichoderma reesei. J. Mol. Biol. 275, 309-325.
    • (1998) J. Mol. Biol. , vol.275 , pp. 309-325
    • Divne, C.1    Ståhlberg, J.2    Teeri, T.T.3    Jones, A.T.4
  • 11
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • 11. 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
  • 12
    • 0021427604 scopus 로고
    • Competitive adsorption of cellulase components and its significance in a synergistic mechanism
    • 12. Ryu, Y.D.D., Kim, C. & Mandels, M. (1984) Competitive adsorption of cellulase components and its significance in a synergistic mechanism. Biotechnol. Bioeng. 26, 488-496.
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 488-496
    • Ryu, Y.D.D.1    Kim, C.2    Mandels, M.3
  • 13
    • 0024114522 scopus 로고
    • The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose
    • 13. Woodward, J., Lima, M. & Lee, E.N. (1988) The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose. Biochem. J. 255, 895-899.
    • (1988) Biochem. J. , vol.255 , pp. 895-899
    • Woodward, J.1    Lima, M.2    Lee, E.N.3
  • 14
    • 0025605767 scopus 로고
    • Trends in biochemistry and enzymology of cellulose degradation
    • 14. Klyosov, A.A. (1990) Trends in biochemistry and enzymology of cellulose degradation. Biochemistry 29, 10577-10585.
    • (1990) Biochemistry , vol.29 , pp. 10577-10585
    • Klyosov, A.A.1
  • 15
    • 0017858361 scopus 로고
    • The cellulase of Trichoderma koningii. Purification and properties of some endoclucanase components with special reference to their action on cellulose when acting alone and in synergism with the cellobiohydrolase
    • 15. Wood, M.T. & McCrae, S.J. (1978) The cellulase of Trichoderma koningii. Purification and properties of some endoclucanase components with special reference to their action on cellulose when acting alone and in synergism with the cellobiohydrolase. Biochem. J. 171, 61-72.
    • (1978) Biochem. J. , vol.171 , pp. 61-72
    • Wood, M.T.1    McCrae, S.J.2
  • 16
    • 0000709747 scopus 로고
    • Synergism between enzymes involved in the solubilization of native cellulose
    • 16. Wood, M.T. & McCrae, S.J. (1979) Synergism between enzymes involved in the solubilization of native cellulose. Adv. Chem. Ser. 181, 181-209.
    • (1979) Adv. Chem. Ser. , vol.181 , pp. 181-209
    • Wood, M.T.1    McCrae, S.J.2
  • 17
    • 0031439510 scopus 로고    scopus 로고
    • Synergistic action of exo-type cellulases in the hydrolysis of cellulose with different crystallinities
    • 17. Hoshino, E., Shiroishi, M., Amano, Y., Nomura, M. & Kanda, T. (1997) Synergistic action of exo-type cellulases in the hydrolysis of cellulose with different crystallinities. J. Fermentation Bioengineering 4, 300-306.
    • (1997) J. Fermentation Bioengineering , vol.4 , pp. 300-306
    • Hoshino, E.1    Shiroishi, M.2    Amano, Y.3    Nomura, M.4    Kanda, T.5
  • 18
    • 0021668869 scopus 로고
    • Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414
    • 18. Bhikhabhai, R., Johansson, G. & Pettersson, G. (1984) Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414. J. Appl. Biochem. 6, 336-345.
    • (1984) J. Appl. Biochem. , vol.6 , pp. 336-345
    • Bhikhabhai, R.1    Johansson, G.2    Pettersson, G.3
  • 19
    • 10844297507 scopus 로고
    • Separation of endo-and exo-type cellulases using a new affinity chromatography method
    • 19. van Tilbeurgh, H., Bhikhabhai, R., Pettersson, G. & Claeyssens, M. (1984) Separation of endo-and exo-type cellulases using a new affinity chromatography method. FEBS Lett. 169, 215-218.
    • (1984) FEBS Lett. , vol.169 , pp. 215-218
    • Van Tilbeurgh, H.1    Bhikhabhai, R.2    Pettersson, G.3    Claeyssens, M.4
  • 20
    • 84982335188 scopus 로고
    • Bestimmung von hexosen in tryptophan-haltigen eiwesskörpern
    • 20. Hörmann, H. & Gollwitzer, R. (1962) Bestimmung von hexosen in tryptophan-haltigen eiwesskörpern. Ann. Chem. 655, 178-188.
    • (1962) Ann. Chem. , vol.655 , pp. 178-188
    • Hörmann, H.1    Gollwitzer, R.2
  • 21
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • 21. Nelson, N.J. (1944) A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153, 375-380.
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.J.1
  • 22
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • 22. Somogyi, M. (1952) Notes on sugar determination. J. Biol. Chem. 195, 19-23.
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 23
    • 0027298768 scopus 로고
    • Trichoderma reesei has no true exo-cellulase: All intact and truncated cellulases produce new reducing end groups on cellulose
    • 23. Stählberg, J., Johansson, G. & Pettersson, G. (1993) Trichoderma reesei has no true exo-cellulase: all intact and truncated cellulases produce new reducing end groups on cellulose. Biochim. Biophys. Acta 1157, 107-113.
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 107-113
    • Stählberg, J.1    Johansson, G.2    Pettersson, G.3
  • 24
    • 84948619838 scopus 로고
    • An empirical method for estimating the degree of crystallinity of native cellulose using X-ray diffractometer
    • 24. Segal, L., Creely, J.J., Martin, A.E. & Conrad, C.M. (1959) An empirical method for estimating the degree of crystallinity of native cellulose using X-ray diffractometer. Text. Res. J. 29, 786-794.
    • (1959) Text. Res. J. , vol.29 , pp. 786-794
    • Segal, L.1    Creely, J.J.2    Martin, A.E.3    Conrad, C.M.4
  • 25
    • 0032522362 scopus 로고    scopus 로고
    • The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model
    • 25. Väljamäe, P., Sild, V., Pettersson, G. & Johansson, G. (1998) The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model. Eur. J. Biochem. 253, 469-475.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 469-475
    • Väljamäe, P.1    Sild, V.2    Pettersson, G.3    Johansson, G.4
  • 27
    • 0028375029 scopus 로고
    • Acid hydrolysis of cellulose. Part II: Stochastic simulation using a Monte Carlo technique
    • 27. Dadach, E.-Z., Pinto, Q.H.-J. & Kaliaguine, S. (1994) Acid hydrolysis of cellulose. Part II: stochastic simulation using a Monte Carlo technique. Can J. Chem Engineering 72, 106-112.
    • (1994) Can J. Chem Engineering , vol.72 , pp. 106-112
    • Dadach, E.-Z.1    Pinto, Q.H.-J.2    Kaliaguine, S.3
  • 28
    • 0016079571 scopus 로고
    • Crystallite structure of cellulose
    • 28. Chang, M.M.Y. (1974) Crystallite structure of cellulose. J. Polymer Sci. 12, 1349-1374.
    • (1974) J. Polymer Sci. , vol.12 , pp. 1349-1374
    • Chang, M.M.Y.1
  • 30
    • 0026562250 scopus 로고
    • Changes in molecular size distribution of cellulose during attack by white rot and brown rot fungi
    • 30. Kleman-Leyer, K., Agosin, E., Conner, H.A. & Kirk, K.T. (1992) Changes in molecular size distribution of cellulose during attack by white rot and brown rot fungi. Appl. Env. Microbiol. 58, 1266-1270.
    • (1992) Appl. Env. Microbiol. , vol.58 , pp. 1266-1270
    • Kleman-Leyer, K.1    Agosin, E.2    Conner, H.A.3    Kirk, K.T.4
  • 31
    • 0028075432 scopus 로고
    • Changes in the molecular-size distribution of insoluble celluloses by the action of recombinant Cellutomonas-fimi cellulases
    • 31. Kleman-Leyer, K., Gilkes, R.N., Miller, C.R. Jr & Kirk, K.T. (1994) Changes in the molecular-size distribution of insoluble celluloses by the action of recombinant Cellutomonas-fimi cellulases. Biochem. J. 302, 463-469.
    • (1994) Biochem. J. , vol.302 , pp. 463-469
    • Kleman-Leyer, K.1    Gilkes, R.N.2    Miller C.R., Jr.3    Kirk, K.T.4
  • 32
    • 0029743877 scopus 로고    scopus 로고
    • The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size
    • 32. Kleman-Leyer, K., Siika-Aho, M., Teeri, T.T. & Kirk, K.T. (1996) The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size. Appl. Environ. Microbiol. 62, 2883-2887.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2883-2887
    • Kleman-Leyer, K.1    Siika-Aho, M.2    Teeri, T.T.3    Kirk, K.T.4
  • 33
    • 0019123415 scopus 로고
    • Calcufluor White ST alters in vivo assembly of cellulose microfibrils
    • 33. Haigler, H.C., Brown, M.R. Jr & Benziman, M. (1980) Calcufluor White ST alters in vivo assembly of cellulose microfibrils. Science 210, 903-906.
    • (1980) Science , vol.210 , pp. 903-906
    • Haigler, H.C.1    Brown M.R., Jr.2    Benziman, M.3
  • 34
    • 0031587296 scopus 로고    scopus 로고
    • The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 À resolution, and a comparison with related enzymes
    • 34. Kleywegt, G.J., Zou, J.-Y., Divne, C., Davies, G.J., Sinning, I., Ståhlberg, J., Reinikainen, T., Srisodsuk, M., Teeri, T. & Jones, T.A. (1997) The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 À resolution, and a comparison with related enzymes. J. Mol. Biol. 272, 383-397.
    • (1997) J. Mol. Biol. , vol.272 , pp. 383-397
    • Kleywegt, G.J.1    Zou, J.-Y.2    Divne, C.3    Davies, G.J.4    Sinning, I.5    Ståhlberg, J.6    Reinikainen, T.7    Srisodsuk, M.8    Teeri, T.9    Jones, T.A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.