Function of a low molecular weight peptide from trichoderma pseudokoningii S38 during cellulose biodegradation

Current Microbiology

Volumn 46, Issue 5, 2003, Pages 371-379

  Wang, Wei ^a,b   Liu, Jie ^a,c   Chen, Guanjun ^a   Zhang, Yingshu ^a   Gao, Peiji ^a  

^a SHANDONG UNIVERSITY   (China)

^b UNIVERSITY OF JINAN   (China)

^c UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLULOSE; FERRIC ION; FERROUS ION; FUNGAL PROTEIN; SHORT FIBER GENERATING FACTOR; UNCLASSIFIED DRUG; CHELATING AGENT; PEPTIDE;

ARTICLE; BIOCHEMISTRY; BIODEGRADATION; BIOPHYSICS; CHELATION; CHEMICAL BINDING; DECOMPOSITION; ENZYME ANALYSIS; HYDROGEN BOND; HYDROLYSIS; IRON CHELATION; MICROBIAL DEGRADATION; MOLECULAR WEIGHT; NONHUMAN; OXIDATION KINETICS; PEPTIDE ANALYSIS; PRIORITY JOURNAL; REACTION ANALYSIS; SCANNING ELECTRON MICROSCOPY; TRICHODERMA; TRICHODERMA PSEUDOKONINGII S38; CHEMISTRY; COTTON; CULTURE MEDIUM; ELECTRON TRANSPORT; GROWTH, DEVELOPMENT AND AGING; INFRARED SPECTROPHOTOMETRY; METABOLISM;

FUNGI; TRICHODERMA; TRICHODERMA PSEUDOKONINGII;

CELLULOSE; CHELATING AGENTS; COTTON FIBER; CULTURE MEDIA, CONDITIONED; ELECTRON TRANSPORT; FERRIC COMPOUNDS; MICROSCOPY, ELECTRON, SCANNING; MOLECULAR WEIGHT; PEPTIDES; SPECTROPHOTOMETRY, INFRARED; TRICHODERMA;

EID: 0037712959     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00284-002-3864-9     Document Type: Article

References (43)

1. Banka RR, Mishra S, Ghose TK (1998) Fibril formation from cellulose by a novel protein from Trichoderma reesei: A non-hydrolytic cellulolytic component? World J Microbiol Biotech 14:551-558
2. Beguin P, Aubert JP (1994) The biological degradation of cellulose. TEMS Microbiol Rev 13:25-28
3. Blackwell J, Marchessault RH (1971) Investigations of the structure of cellulose and its derivatives. A. Infrared spectroscopy. In: Bikales NM, Segel L (eds) Cellulose and cellulose derivatives. New York: Wiley, pp 1-18
4. Chandhoke V, Goodell B, Jellison J, Fekete FA (1992) Oxidation of 2-keto-4-thiomethylbutyric acid (KTBA) by iron-binding compounds produced by the wood-decaying fungus Glocophyllum trabeum. FEMS Microbiol Lett 90:263-266
5. Claeyssens M, Van TH, Tomme P, Wood TM, McRae SI (1989) Fungal cellulase systems: Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei. Biochem J 261:819-825
6. Enoki A, Itakuram S, Tanaka H (1997) The involvement of extra-cellular substances for reducing molecular oxygen to hydroxyl radical and ferric iron to ferrous iron in wood degradation by wood decay fungi. J Biotech 53:265-272
7. Fang J, Liu W, Gao PJ (1998) Cellobiose dehydrogenase from Schizophyllum commune: Purification and study of some catalytic, inactivation, and cellulose-binding properties. Arch Biochem Biophys 353:37-46
8. Gao PJ, Chen GJ, Wang TH, Zhang YS, Liu J (2001) Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellun. Acta Biochem Biophys Sin 33:13-18
9. Gardner KH, Blackwell J (1974) The hydrogen bonding in native cellulose. Biochim Biophys Acta 343:232-237
10. Gao J, Tong LG (1996) Cellulose science. 1st edn. Beijing: Academic Press Sinica, pp 190-194
11. Gibbs CR (1976) Characterization and application of ferrozine iron reagent as a ferrous iron indicator. Anal Chem 48:1197-1201
12. Goodell B et al. (1997) Low molecular weight chelators and phenolic compounds isolated from wood decay fungi and their role in the fungal biodegradation of wood. J Biotech 53:133-162
13. Griffin M, Dintzis FR, Krull L, Baker FL (1984) A microfibril generating factor from the enzyme complex of Trichoderma reesei. Biotech Bioeng 26:296-300
14. Halliwell G (1961) The action of cellulolytic enzyme from M. verrucaria. Biochem J 79:185-192
15. Halliwell G (1966) Solubilization of native and derived forms of cellulose by cell-free microbial enzymes. Biochem J 100:315-340
16. Halliwell G, Riaz M (1970) The formation of short fibres from native cellulose by components of Trichoderma koningii cellulase. Biochem J 116:35-42
17. Hinterstoisser B, Salmén L (2000) Application of dynamic 2D FTIR to cellulose. Vibration Spectrosc 22:111-118
18. Heyn AN (1966) The microcrystalline structure of cellulose in cell walls of cotton, ramie, and jute fibers as revealed by negative staining of sections. J Cell Biol 29:181-197
19. Jacobson E, Tinnel SS (1993) Antioxidant function of fungal melatin. J Bacteriol 175:7102-7104
20. Jeffrey GA, Saenger W (1994) Hydrogen binding in biological structure. Berlin: Springer-Verlag, pp 125-138
21. Krull H, Dintzis HL, Baker FL (1988) Microfibril-generating factor from the cellulase of Trichoderma reesei. Biotech Bioeng 31:321-327
22. Klyosov AA (1990) Trends in biochemistry and enzymology of cellulose degradation. Biochemistry 29:10577-10585
23. Liu TH, King KW (1967) Fragmentation during enzymatic degradation of cellulose. Arch Biochem Biophys 120:462-464
24. Li XZ, Zheng SF, Ren GS (1996) A low molecular weight CMCase from newly isolated Streptomyces. Bull Microbiol (in Chinese) 23:277-231
25. Li XZ, Zhang SF, Jin F, Gao PJ (1997) Production and properties of a cellobiose oxidizing enzyme from a new isolated cellulolytic bacterium Cytophage sp. LXZ. World J Microbiol Biotech 13:683-688
26. Liu J, Shen XY, Gao PJ (1996) Short fibre formation during cellulose degradation by cellulolytic fungi. Biotech Lett 11:1235-1240
27. Liu J, Gao PJ (1996) Short-fiber formation during cellulose degradation. Am Chem Soc Symp Ser 655:166-174
28. Medve T, Karlsson T, 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 enzymes. Biotech Bioeng 59:620-634
29. Michell AJ (1990) Second-derivative F.T-I.R spectra of native cellulose. Carb Res 197:53-60
30. Pennell R (1998) Cell walls: Structure and signals. Curr Opin Plant Biol 1:504-510
31. Reese ET, Siu RGH, Leyinson HS (1950) Biological degradation of soluble cellulose derivatives. J Bacteriol 59:485-497
32. Rogers MS, Jones GD, Antonini G, Wilson MT, Brunri M (1994) Electron transfer from Phanerorochate chrysosporium. Cellobiose oxidase to equine cytochrome c and Pseudomonas aeruginosa cytochrome c-551. Biochem J 298:329-334
33. Samejima M, Eriksson KE (1992) A comparison of the catalytic properties of cellobiose:quinino oxidoreductase and cellobiose oxidase from Phanerorochate chrysosporium. Eur J Biochem 207:103-107
34. Schnyn B, Neilands JB (1997) Universal chemical assay for the detection and determination of Siderophores. Anal Biochem 160:46-56
35. Sinnott ML (1998) The cellobiohydrolases of Trichoderma reesei: A review of indirect and direct evidence that their function is not just glycosidic bond hydrolysis. Biochem Soc Trans 26:160-164
36. Sugiyama T, Person J, Chanzy H (1991) Combined infrared and electron diffraction study of the polymorphism of native cellulose. Macromolecules 24:2461-2466
37. Tripp VW (1971) Measurement of crystallinity. In: Bikales NM, Segel L (eds) Cellulose and cellulose derivatives. New York: Wiley, pp 305-320
38. Wang W, Lu XM, Gao PJ (1997) Depolymerization of cellulose by low molecular weight compound from brown-rot fungi. Mycosystem (in Chinese) 16:40-46
39. Wang TH, Wang CH, Gao PJ, Ling YX (1998) Subcloning and expression of coding region for cellulose binding domain of CBHI from P. janthinelium in E. coli. Acta Microbiol Sin 38:269-275
40. Warwicker JO (1971) Swelling. In: Bikales NM, Segel L (eds) Cellulose and cellulose derivatives. New York: Wiley, pp 325-328
41. Xiao ZH, Gao PJ, Qu YN, Wang TH (2001) Cellulose-binding domain of endoglucanase III from Trichoderma reesei disrupting the structure of cellulose. Biotech Lett 23:711-715
42. Yan BX, Sun YQ (1997) Domain structure and confirmation of a cellobiohydrolase I from Trichoderma pseudokoningii S-38. J Protein Chem 16:59-66
43. Yan BX, Sun YQ, Gao PJ (1997) Intrinsic fluorescence in endoglucanase and cellobiohydrolase from Trichoderma pseudokoningii S-38. J Protein Chem 16:681-688