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Trichoderma reesei cellobiohydrolase

Cellulomonas fimi Endoglucanase A (i7) Microbispora bispora Endoglucanase I (5) Streptomyces sp. Cellulase A (72) Trichoderma reesei Cellobiohydrolase II (75)... [Pg.294]

Trichoderma reesei Cellulase A (26) Trkhoderma reesei Cellulase (25) Trichoderma reesei Cellobiohydrolase II 13) Trichoderma reesei Cellobiohydrolase I (55) Phanerochaete chrysosporium Exocellobiohydrolase I 34)... [Pg.296]

Okada, H., Sekiya, T., Yokoyama, K.,Tohda, H., Kumagai, H., and Morikawa, Y. 1998. Efficient secretion of Trichoderma reesei cellobiohydrolase II in Schizosaccharomy-ces pombe and characterization of its products. Appl. Microbiol. Biotechnol., 49, 301-308. [Pg.227]

Linder M, Mattinen M-L, Konttelli M, Lindeberg G, Stdhlberg J, Drakenberg T, Reinikainen T, Pettersson G, Annila A (1995) Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase 1. Protein Science 4 1056-1064... [Pg.39]

Rouvinen J, Bergfors T, Teeri T, Knowles JKC, Jones TA (1990) Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science 249 380-385 Srisodsuk M, Reinikainen T, PenttUa M, Teeri TT (1993) Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose. Journal of Biological Chemistry 268 20,756-20,761... [Pg.40]

M. Srisodsuk, J. Lehtio, M. Linder, E. Margolles-Clark, T. Reinikainen, and T. T. Teeri, Trichoderma reesei cellobiohydrolase I with an endoglucanase... [Pg.206]

Sandra, K. et al.. Combining gel and capillary electrophoresis, nano-LC and mass spectrometry for the elucidation of posttranslational modifications of Trichoderma reesei cellobiohydrolase I., J. Chromatogr. A, 1058, 263, 2004. [Pg.702]

Structure-Reactivity Studies of Trichoderma reesei Cellobiohydrolase Cel7A... [Pg.207]

Koivula A, Kinnari T, Harjunpaa V, Ruohonen L, Teleman A, Drakenberg T, Rouvinen J, Jones TA, Teeri TT (1998) Tryptophan 272 an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A. FEBS Lett 429 341-346... [Pg.70]

Srisodsuk, M Lehtio, JML Msrgolles-Clark, E Reinikainen, T Teeri, TT. Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain action on bacterial microcrystalline cellulose. Journal of Bacteriology, 1997, 57, 49-57. [Pg.913]

Cellulase-Negative Xylanase-Positive Mutants. There are two reports concerning the selection of such mutants from filamentous fungi, one on Pofyporus adm-tus (32) and the other cmi Trichoderma reesei (Durand, H. et al. Society CAYLA, Toulouse, France, unpublished results). An analysis of the eliminated cellulase genes has not been done, so it is not known if the mutants negative in endo(l- 4)-p-glucan-ase were deficient also in cellobiohydrolases. [Pg.410]

Figure 1. Fractionation of proteins in the culture filtrate of Trichoderma reesei according to their pi values Xyl, xylanase Ara, arabinosidase AE, acetyl esterase / X, /3-xylosidase aG, a-glucuronidase / G, / -glucosidase CBH, cellobiohydrolase EG, endoglucanase. Chromatofocusing was performed in a PBE-94 anion exchange resin (Pharmacia) with a pH-gradient created by ampholyte buffers (Pharmacia). Solid line, A dotted line, pH. (Reproduced with permission from ref. 24. Copyright 1988.)... Figure 1. Fractionation of proteins in the culture filtrate of Trichoderma reesei according to their pi values Xyl, xylanase Ara, arabinosidase AE, acetyl esterase / X, /3-xylosidase aG, a-glucuronidase / G, / -glucosidase CBH, cellobiohydrolase EG, endoglucanase. Chromatofocusing was performed in a PBE-94 anion exchange resin (Pharmacia) with a pH-gradient created by ampholyte buffers (Pharmacia). Solid line, A dotted line, pH. (Reproduced with permission from ref. 24. Copyright 1988.)...
Compound (44 g, NHAc form) (Scheme 14) was found to be a competitive inhibitor for CBHI cellulase (family 7) from Trichoderma reesei, when 4-methyl-umbelliferyl / -lactoside was used as substrate. Therefore (44 g, NHj form) was coupled to CH-Sepharose 4B, and the affinity gel was very effective for the purification of cellobiohydrolases from a crude commercial cellulolytic extract of T. reesei [40c]. Using the same approach aryl 1,4-dithioxylobioside and l,4,4 -trithioxylotrioside (44 h, NH2 form) were coupled to CH-Sepharose 4B to give affinity gels which were used for the purification of xylanases [40a,b]. [Pg.112]

Figure 5 shows the results of inhibition experiments involving the D-gluco-sides 37 (n = 1-3) and a cellobiohydrolase from Trichoderma reesei. The best inhibition was achieved with the epoxypentyl /J-D-C-glucoside, a result which corresponds nicely to the 0-glycoside series where the epoxybutyl -o-gluco-side 6 (n = 2) was the most effective inhibitor. [Pg.211]

Divne, C., Stahlberg.J., Reinikainen, T., Ruohonen, L., Pettersson, G., KnowlesJ., et al. (1994) The three-dimensional crystal stractme of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science, 265, 524-528. [Pg.59]

Divne, C., Stahlberg, J., Teeri, T. and Jones, T. (1998) High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Angstrom long tuimel of cellobiohydrolase I from Trichoderma reesei. J. Mol. Biol., 275, 309-325. [Pg.60]

El-Gogary, S., Leite, A., Crivellaro, O., Eveleigh, D., and El-Dorry, H. 1989. Mechanism by which cellulose triggers cellobiohydrolase I gene expresion in Trichoderma reesei. Proc. Natl. Acad. Sci.,86, 6138-6141. [Pg.223]

Kleman-Leyer, K. M., Siika-Aho, M., Teeri, T. T., and Kirk, T. K. 1996. The Cellulases Endoglucanase I and Cellobiohydrolase II of Trichoderma Reesei act synergistically to solubilize native cotton cellulose but not to decrease its moleculare size. Appl. Environ. Microbiol., 62,2883-2887. [Pg.225]

Linder, M., and Teeri, T. T. 1996. The Cellulose-Binding Domain of the Major Cellobiohydrolase of Trichoderma reesei Exhibits True Reversibility and a High Exchange Rate on Crystalline Cellulose. Proc. Natl. Acad. Sci., 93,12251-12255. [Pg.225]

Medve, J., Karlsson, J., Lee, D., and 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. Biotech. Bioeng.,59, 621-634. [Pg.226]

Reinikainen, T. 1994. The Cellulose-Binding Domain of Cellobiohydrolase I from Trichoderma reesei (pg. 206). Espoo, Finland VTT publications. [Pg.227]

Reinikainen, T., Teleman, O., and Teeri, T. T. 1995. Effects of Ph and High Ionic-Strength on the Adsorption and Activity of Native and Mutated Cellobiohydrolase-I from Trichoderma-Reesei. Proteins-Structure Function and Genetics, 22, 392-403. [Pg.228]

Vrsanska, M. and Biely, P., The cellobiohydrolase I from Trichoderma reesei QM 9414 Action on cello-oligosaccharides. Carbohydrate Res 1992, 227, 19 27. [Pg.1531]


See other pages where Trichoderma reesei cellobiohydrolase is mentioned: [Pg.268]    [Pg.268]    [Pg.301]    [Pg.314]    [Pg.350]    [Pg.570]    [Pg.576]    [Pg.237]    [Pg.238]    [Pg.262]    [Pg.81]    [Pg.289]    [Pg.390]    [Pg.234]    [Pg.268]    [Pg.268]   


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Cellobiohydrolase I from Trichoderma reesei

Cellobiohydrolases from Trichoderma reesei

Trichoderma

Trichoderma reesei cellobiohydrolase A from

Trichoderma reesei cellobiohydrolase B from

Trichoderma reesei cellobiohydrolase enzymes

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