Engineering endoglucanase II from Trichoderma reesei to improve the catalytic efficiency at a higher pH optimum

Journal of Biotechnology

Volumn 135, Issue 2, 2008, Pages 190-195

  Qin, Yuqi ^a   Wei, Xiaomin ^a   Song, Xin ^a   Qu, Yinbo ^a  

^a SHANDONG UNIVERSITY   (China)

Author keywords

Catalytic efficiency; DNA shuffling; Endoglucanase II; pH optimum; Saturation mutation; Trichoderma reesei

Indexed keywords

CHARACTERIZATION; COULOMB INTERACTIONS; MUTAGENESIS; PH EFFECTS; PROTEINS; PURIFICATION;

CATALYTIC EFFICIENCY; DNA SHUFFLING; ENDOGLUCANASE II; SATURATION MUTATION; TRICHODERMA REESEI;

CATALYST ACTIVITY;

ENZYME VARIANT; GLUCAN SYNTHASE; GLUCAN SYNTHASE II;

ARTICLE; CATALYSIS; DNA SHUFFLING; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME STRUCTURE; MOLECULAR MODEL; MUTAGENESIS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ENGINEERING; TRICHODERMA REESEI; WILD TYPE;

AMINO ACID SUBSTITUTION; CATALYSIS; CELLULASE; DIRECTED MOLECULAR EVOLUTION; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; MUTATION; STRUCTURE-ACTIVITY RELATIONSHIP; TRICHODERMA;

HYPOCREA JECORINA;

EID: 43849110605     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2008.03.016     Document Type: Article

References (49)

1. Anish R., Rahman M.S., and Rao M. Application of cellulases from an alkalothermophilic Thermomonospora sp. in biopolishing of denims. Biotechnol. Bioeng. 96 (2007) 48-56
2. Bailey M.J., and Nevalainen K.M.H. Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubilizing cellulase. Enzyme Microb. Technol. 3 (1981) 153-157
3. Barbesgaard, P.O., Jensen, G.W., Holm, P., 1984. Detergent cellulase. United States Patent 4,435,307.
4. Becker D., Braet C., Brumer H., Claeyssens M., Divne C., Fagerström B.R., Harris M., Jones T.A., Kleywegt G.J., Koivula A., Mahdi S., Piens K., Sinnott M.L., Ståhlberg J., Teeri T.T., Underwood M., and Wohlfahrt G. Engineering of a glycosidase family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/A224H/L225V/T226A/D262G mutant. Biochem. J. 356 (2001) 19-30
5. Boer H., and Koivula A. The relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A. Eur. J. Biochem. 270 (2003) 841-848
6. Davies G.J., Dauter M., Brzozowski A.M., Bjornvad M.E., Andersen K.V., and Schülein M. Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution. Biochemistry 37 (1998) 1926-1932
7. Domínguez R., Souchon H., and Alzari P.M. Characterization of two crystal forms of Clostridium thermocellum endoglucanase CelC. Protein Struct. Funct. Genet. 19 (1994) 158-160
8. Domínguez R., Souchon H., Lascombe M., and Alzari P.M. The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J. Mol. Biol. 257 (1996) 1042-1051
9. Ducros V., Czjzek M., Belaich A., Gaudin C., Fierobe H.P., Belaich J.P., Davies G.J., and Haser R. Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5. Structure 3 (1995) 939-949
10. Fang T.Y., and Ford C. Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum. Protein Eng. 11 (1998) 383-388
11. Fierobe H.P., Gaudin C., Belaich A., Loutfi M., Faure E., Bagnara C., Baty D., and Belaich J.P. Characterization of endoglucanase A from Clostridium cellulolyticum. J. Bacteriol. 173 (1991) 7956-7962
12. Hirasawa K., Uchimura K., Kashiwa M., Grant W.D., Ito S., Kobayashi T., and Horikoshi K. Salt-activated endoglucanase of a strain of alkaliphilic Bacillus agaradhaerens. Antonie Van Leeuwenhoek 89 (2006) 211-219
13. Höcker B. Directed evolution of (beta-alpha)(8)-barrel enzymes. Microbiol. Mol. Biol. Rev. 69 (2005) 373-392
14. Horikoshi K., Nakao M., Kurono Y., and Sashihara N. Cellulases of an alkalophilic Bacillus strain isolated from soil. Can. J. Microbiol. 39 (1984) 774-779
15. Jenkins J., Lo-Leggio L., Harris G., and Pickersgill R. Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven. FEBS Lett. 362 (1995) 281-285
16. Kleywegt G.J., Zou J.Y., Divne C., Davies G.J., Sinning I., Ståhlberg J., Reinikainen T., Srisodsuk M., Teeri T.T., and Jones T.A. The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes. J. Mol. Biol. 272 (1997) 383-397
17. Knowles J., Lehtovaara P., and Teeri T.T. Cellulase families and their genes. Trends Biotechnol. 5 (1987) 255-261
18. Le-Nours J., Ryttersgaard C., Lo-Leggio L., Østergaard P.R., Borchert T.V., Christensen L.L., and Larsen S. Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. Protein Sci. 12 (2003) 1195-1204
19. Lo-Leggio L., and Larsen S. The 1.62 A structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5. FEBS Lett. 523 (2002) 103-108
20. Macarrón R., Henrissat B., and Claeyssens M. Family A cellulases: two essential tryptophan residues in endoglucanase III from Trichoderma reesei. Biochim. Biophys. Acta 1245 (1995) 187-190
21. Medve J., Karlsson J., Lee D., and Tjerneld F. 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 (1998) 621-634
22. Meurisse R., Brasseur R., and Thomas A. Aromatic side-chain interactions in proteins. Near- and far-sequence His-X pairs. Biochim. Biophys. Acta 26 (2003) 85-96
23. Miettinen-Oinonen A., and Suominen P. Enhanced production of Trichoderma reesei endoglucanases and use of the new cellulase preparations in producing the stonewashed effect on denim fabric. Appl. Environ. Microbiol. 68 (2002) 3956-3964
24. Murray P.G., Grassick A., Laffey C.D., Cuffe M.M., Higgins T., Savage A.V., Planas A., and Tuohy M.G. Isolation and characterization of a thermostable endo-beta-glucanase active on 1,3-1,4-beta-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70. Enzyme Microb. Technol. 29 (2001) 90-98
25. Nakamura A., Fukumori F., Horinouchi S., Masaki H., Kudo T., Uozumi T., Horikoshi K., and Beppu T. Construction and characterization of the chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase. J. Biol. Chem. 266 (1991) 1579-1583
26. Ozaki K., Hayashi Y., Sumitomo N., Kawai S., and Ito S. Construction, purification, and properties of a truncated alkaline endoglucanase from Bacillus sp. KSM-635. Biosci. Biotechnol. Biochem. 59 (1995) 1613-1618
27. Parry N.J., Beever D.E., Owen E., Nerinckx W., Claeyssens M., Van-Beeumen J., and Bhat M.K. Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus. Arch. Biochem. Biophys. 404 (2002) 243-253
28. Qin Y., Wei X., Liu X., Wang T., and Qu Y. Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability. Protein Expr. Purif. 58 (2008) 162-167
29. Qin, Y., Wei, X., Song, X., Qu, Y., 2008b. The role of the site 342 in catalytic efficiency and pH optima of endoglucanase II from Trichoderma reesei as probed by saturation mutagenesis. Biocatal. Biotransfor, in press.
30. Roberge M., Shareck F., Morosoli R., Kluepfel D., and Dupont C. Site-directed mutagenesis study of a conserved residue in family 10 glycanases: histidine 86 of xylanase A from Streptomyces lividans. Protein Eng. 11 (1998) 399-404
31. Rui L., Kwon Y.M., Fishman A., Reardon K.F., and Wood T.K. Saturation mutagenesis of toluene ortho-monooxygenase of Burkholderia cepacia G4 for enhanced 1-naphthol synthesis and chloroform degradation. Appl. Environ. Microbiol. 70 (2004) 3246-3252
32. Saloheimo M., Lehtovaara P., Penttila M., Teeri T.T., Ståhlberg J., Johansson G., Pettersson G., Claeyssens M., Tomme P., and Knowles J.K. EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme. Gene 63 (1988) 11-22
33. Schülein M. Enzymatic properties of cellulases from Humicola insolens. J. Biotechnol. 57 (1997) 71-81
34. In: Schulz G.E., and Schirmer R.H. (Eds). Principles of Protein Structure (1979), Springer-Verlag, New York 4-11
35. Schwarz W.H., Schimming S., Rucknagel K.P., Burgschwaiger S., Kreil G., and Staudenbauer W.L. Nucleotide sequence of the celC gene encoding endoglucanase C of Clostridium thermocellum. Gene 63 (1988) 23-30
36. Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Hitomi J., and Ito S. High-resolution crystal structure of M-protease: phylogeny aided analysis of the high-alkaline adaptation mechanism. Protein Eng. 10 (1997) 627-634
37. Shirai T., Ishida H., Noda J., Yamane T., Ozaki K., Hakamada Y., and Ito S. Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme. J. Mol. Biol. 310 (2001) 1079-1087
38. Shiraki K., and Sakiyama F. Histidine 210 mutant of a trypsin-type Achromobacter protease I shows broad optimum pH range. J. Biosci. Bioeng. 93 (2002) 331-333
39. Shiraki K., Norioka S., Li S., Yokota K., and Sakiyama F. Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease, Achromobacter protease I. Eur. J. Biochem. 269 (2002) 4152-4158
40. Sterner R., and Höcker B. Catalytic versatility, stability, and evolution of the (beta alpha)8-barrel enzyme fold. Chem. Rev. 105 (2005) 4038-4055
41. Suominen P.L., Mäntylä A.L., Karhunen T., Hakola S., and Nevalainen H. Trichoderma reesei. II. Effects of deletions of individual cellulase genes. Mol. Gen. Genet. 241 (1993) 523-530
42. Tao H., and Cornish V.W. Milestones in directed enzyme evolution. Curr. Opin. Chem. Biol. 6 (2002) 858-864
43. Teixeira S., Lo-Leggio L., Pickersgill R.W., and Cardin C. Anisotropic refinement of the structure of Thermoascus aurantiacus xylanase I. Acta Crystallogr. D: Biol. Crystallogr. 57 (2001) 385-392
44. Turunen O., Vuorio M., Fenel F., and Leisola M. Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH. Protein Eng. 15 (2002) 141-145
45. Urban A., Neukirchen S., and Jaeger K.E. A rapid and efficient method for site-directed mutagenesis using one-step overlap extension PCR. Nucleic Acids Res. 1 (1997) 2227-2228
46. Wang T., Liu X., Yu Q., Zhang X., Qu Y., Gao P., and Wang T. Directed evolution for engineering pH profile of endoglucanase III from Trichoderma reesei. Biomol. Eng. 22 (2005) 89-94
47. White A., and Rose D.R. Mechanism of catalysis by retaining beta-glycosyl hydrolases. Curr. Opin. Struct. Biol. 7 (1997) 645-651
48. Wohlfahrt G., Pellikka T., Boer H., Teeri T.T., and Koivula A. Probing pH-dependent functional elements in proteins: modification of carboxylic acid pairs in Trichoderma reesei cellobiohydrolase Cel6A. Biochemistry 42 (2003) 10095-10103
49. Zhao H., and Arnold F.H. Optimization of DNA shuffling for high fidelity recombination. Nucleic Acids Res. 25 (1997) 1307-1308