Novel bifunctional α-L-arabinofuranosidase/xylobiohydrolase (ABF3) from Penicillium purpurogenum

Applied and Environmental Microbiology

Volumn 76, Issue 15, 2010, Pages 5247-5253

  Cristina Ravanal, María ^a   Callegari, Eduardo ^b   Eyzaguirre, Jaime ^a  

^a UNIVERSIDAD ANDRÉS BELLO   (Chile)

^b UNIVERSITY OF SOUTH DAKOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARABINANS; ARABINOFURANOSIDE; ARABINOXYLANS; BIFUNCTIONAL; BIOCHEMICAL PROPERTIES; CARBOHYDRATE BINDING MODULES; FUNGAL SOURCES; GENOMIC DNA; GLYCOSYL HYDROLASES; GLYCOSYLATED; ISOFORMS; MASS SPECTROMETRY ANALYSIS; MATURE PROTEINS; NATURAL SUBSTRATES; OPEN READING FRAME; POLYMERIC SUBSTRATE; PUTATIVE BINDING SITES; SOFT-ROT; TWO DOMAINS; XYLANOLYTIC ENZYMES; XYLOOLIGOSACCHARIDES;

AMINO ACIDS; BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; CARBOHYDRATES; GENE ENCODING; MASS SPECTROMETRY; MOLECULAR WEIGHT; NUCLEOTIDES; ORGANIC ACIDS; PURIFICATION; SUBSTRATES; TRANSCRIPTION; TRANSCRIPTION FACTORS;

ENZYMES;

4 NITROPHENYL ALPHA L ARABINOFURANOSIDE; 4 NITROPHENYL BETA D XYLOSIDE; 4-NITROPHENYL BETA-D-XYLOSIDE; 4-NITROPHENYL-ALPHA-L-ARABINOFURANOSIDE; ALPHA N ARABINOFURANOSIDASE; ALPHA-N-ARABINOFURANOSIDASE; ARABINOSE; CELLULOSE; DRUG DERIVATIVE; EXO 1,4 BETA D XYLOSIDASE; EXO-1,4-BETA-D-XYLOSIDASE; FUNGAL DNA; FUNGAL PROTEIN; GLYCOSIDASE; GLYCOSIDE; OLIGOSACCHARIDE; XYLAN 1,4 BETA XYLOSIDASE; PROTEIN BINDING;

AMINO ACID; ENZYME ACTIVITY; FUNGUS; GENOME; GROWTH RATE; HYDROLYSIS; MASS SPECTROMETRY; SUBSTRATE;

ARTICLE; CHEMISTRY; DNA SEQUENCE; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PENICILLIUM; PROMOTER REGION; PROTEIN BINDING; ANALOGS AND DERIVATIVES;

ARABINOSE; CELLULOSE; DNA, FUNGAL; FUNGAL PROTEINS; GLYCOSIDE HYDROLASES; GLYCOSIDES; KINETICS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OLIGOSACCHARIDES; OPEN READING FRAMES; PENICILLIUM; PROMOTER REGIONS, GENETIC; PROTEIN BINDING; SEQUENCE ANALYSIS, DNA; XYLOSIDASES;

FUNGI; PENICILLIUM PURPUROGENUM;

EID: 77955569621     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00214-10     Document Type: Article

References (38)

1. Bainbridge, B. W., C. L. Spreadbury, F. G. Scalise, and J. Cohen. 1990. Improved methods for the preparation of high molecular weight DNA from large and small scale cultures of filamentous fungi. FEMS Microbiol. Lett. 54:113-117.
2. Belancic, A., J. Scarpa, A. Peirano, R. Diaz, J. Steiner, and J. Eyzaguirre. 1995. Penicillium purpurogenum produces several xylanases: purification and properties of two of the enzymes. J. Biotechnol. 41:71-79.
3. Beldman, G., H. A. Schals, S. M. Pitsan, M. J. F. Searle-van Leeuwen, and A. G. J. Voragen. 1997. Arabinans and arabinan-degrading enzymes. Adv. Macromol. Carbohydr. Res. 1:1-64.
4. Bollag, D. M., and S. J. Edelstein. 1991. Protein methods. Wiley-Liss, New York, NY.
5. Brakhage, A. A., A. Andrianopoulos, M. Kato, S. Steidl, M. A. Davis, N. Tsukagoshi, and M. J. Hynes. 1999. HAP-like CCAAT-binding complexes in filamentous fungi: implications for biotechnology. Fungal Genet. Biol. 27:243-252.
6. Brüx, C. A. Ben-David, D. Shallom-Shezifl, M. Leon, K. Niefind, G. Shoham, Y. Shoham, and D. Schomburg. 2006. The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues. J. Mol Biol. 359:97-109.
7. Carapito, R., C. Carapito, J.-M. Jeltsch, and V. Phalip. 2009. Efficient hydrolysis of hemicellulose by a Fusarium graminearum xylanase blend produced at high levels in Escherichia coli. Bioresour. Technol. 100:845-850.
8. Carvallo, M., P. De Ioannes, C. Navarro, R. Chávez, A. Peirano, P. Bull, and J. Eyzaguirre. 2003. Characterization of an α-L- arabinofuranosidase gene (abf1) from Penicillium purpurogenum and its expression. Mycol. Res. 107:388-394.
9. Cubero, B., and C. Scazzochio. 1994. Two different, adjacent and divergent zinc finger binding sites are necessary for CREA-mediated carbon catabolite repression in the proline gene cluster of Aspergillus nidulans. EMBO J. 13:407-415.
10. De Ioannes, P., A. Peirano, J. Steiner, and J. Eyzaguirre. 2000. An α-Larabinofuranosidase from Penicillium purpurogenum: production, purification and properties. J. Biotechnol. 76:253-258.
11. Diaz, J., R. Chavez, L. F. Larrondo, J. Eyzaguirre, and P. Bull. 2008. Functional analysis of the endoxylanase B (xynB) promoter from Penicillium purpurogenum. Curr. Genet. 54:133-141.
12. Filho, E. X. F., J. Puls, and M. P. Coughlan. 1996. Purification and characterization of two arabinofuranosidases from solid-state cultures of the fungus Penicillium capsulatum. Appl. Environ. Microbiol. 62:168-1753.
13. Flipphi, M. J. A., M. van Heuvel, P. van der Veen, J. Visser, and L. H. de Graaff. 1993. Cloning and characterization of the abfB gene coding for the major α-L-arabinofuranosidase (ABF B) of Aspergillus niger. Curr. Genet. 24:515-5323.
14. Flipphi, M. J. A., J. Visser, P. van der Veen, and L. de Graaff. 1994. Arabinase gene expression in Aspergillus niger: indications for coordinated regulation. Microbiology 140:2673-2682.
15. Fritz, M., M. C. Ravanal, C. Braet, and J. Eyzaguirre. 2008. A family 51 α-L-arabinofuranosidase from Penicillium purpurogenum: purification, properties and amino acid sequence. Mycol. Res. 112:933-942.
16. Gielkens, M. M. C., J. Visser, and L. H. de Graaff. 1997. Arabinoxylan degradation by fungi: characterization of the arabinoxylan- arabinofuranohydrolase encoding genes from Aspergillus niger and Aspergillus tubingensis. Curr. Genet. 31:22-29.
17. Gordillo, F., V. Caputo, A. Peirano, R. Chávez, J. Van Beeumen, I. Vandenberghe, M. Claeyssens, P. Bull, M. C. Ravanal, and J. Eyzaguirre. 2006. Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene. Mycol. Res. 110:1129-1139.
18. Henrissat, B., and G. Davies. 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:637-644.
19. Hidalgo, M., J. Steiner, and J. Eyzaguirre. 1992. β-Glucosidase from Penicillium purpurogenum: purification and properties. Biotechnol. Appl. Biochem. 15:185-191.
20. Jordan, D. B., X.-L. Li, C. A. Dunlap, T. R. Whitehead, and M. A. Cotta. 2007. Structure-function relationships of a catalytically efficient β-D-xylosidase. Appl. Biochem. Biotechnol. 141:51-76.
21. Joseleau, J. P., J. Comptat, and K. Ruel. 1992. Chemical structure of xylans and their interaction in the plant cell walls. Prog. Biotechnol. 7:1-15.
22. Kaneko, S., M. Arimoto, M. Ohba, H. Kobayashi, T. Ishi, and I. Kusakabe. 1998. Purification and substrate specificities of two α-L- arabinofuranosidases Team Aspergillus awamori IFO 4033. Appl. Environ. Microbiol. 64:4021-4027.
23. Laemmli, U. K. 1970. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227:680-685.
24. Luonteri, E., M. Siika-aho, M. Tenkanen, and L. Viikari. 1995. Purification and characterization of three α-arabinofuranosidases from Aspergillus terreus. J. Biotechnol. 38:279-291.
25. Luonteri, E., G. Beldman, and M. Tenkanen. 1998. Substrate specificities of Aspergillus terreus α-arabinofuranosidases. Carbohydr. Polym. 37:131-141 . 26.
26. Merika, M., and S. H. Orkin. 1993. DNA-binding specificity of GATA family transcription factors. Mol. Cell. Biol. 13:3999-4010.
27. Rombouts, F. M., A. G. J. Voragen, M. F. Searle-van Leeuwen, C. C. J. M. Geraeds, H.A. Schols, and W. Pilnik. 1988. The arabinanases of Aspergillus niger: purification and characterization of two α-L-arabinofuranosidases and an endo-1,5-α-L-arabinanase. Carbohydr. Polym. 9:25-47.
28. Saha, B. C. 2000. α-L-Arabinofuranosidases: biochemistry, molecular biology and application in biotechnology. Biotechnol. Adv. 18:403-423.
29. Sakamoto, T., and H. Kawasaki. 2003. Purification and properties of two type B α-L-arabinofuranosidases produced by Pénicillium chrysogenum. Biochim. Biophys. Acta 1621:204-210.
30. Sakka, K., K. Yoshikawa, Y. Kojima, S. Karita, K. Ohmiya, and K. Shimada. 1993. Nucleotide sequence of the Clostridium stercorarium xylA gene encoding a bifunctional protein with β-D-xylosidase and α-L-arabinofuranosidase activities, and properties of the translated product. Biosci. Biotechnol. Biochem. 57:268-272.
31. Sambrook, J., and D. W. Russell. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, New York, NY.
32. Scheller, H. V., J. K. Jensen, S. O. Sørensen, J. Harholt, and N. Geshi. 2007. Biosynthesis of pectin. Physiol. Plant 129:283-295.
33. Shallom, D., M. Leon, T. Bravman, A. Ben-David, G. Zaide, V. Belakhov, G. Shoham, D. Schomburg, T. Baasov, and Y. Shoham. 2005. Biochemical characterization and identification of the catalytic residues of a family 43 β-Dxylosidase from Geobacillus stearothermophilus T-6. Biochemistry 44:387-397.
34. Sinitsyna, O. A., F. E. Bukhtoyarov, A. V. Gusakov, O. N. Okunev, A. O. Bekkarevitch, Y. P. Vinetsky, and A. P. Sinitsyn. 2003. Isolation and properties of major components of Penicillium canescens extracellular enzyme complex. Biochemistry (Moscow) 68:1200-1209.
35. Utt, E. A., C. K. Eddy, K.F. Keshaw, and L. O. Ingram. 1991. Sequencing and expression of the Butyrivibrio fibrisolvens xylB gene encoding a novel bifunctional protein with β-D-xylosidase and α-L-arabinofuranosidase activities. Appl. Environ. Microbiol. 57:1227-1234.
36. van Peij, N. N., M. M. Gielkens, R. P. de Vries, J. Visser, and L. H. de Graaff. 1998. The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger. Appl. Environ. Microbiol. 64:3615-3619.
37. Whitehead, T. R., and M. A. Cotta. 2001. Identification of a broad-specificity xylosidase/arabinosidase important for xylooligosaccharide fermentation by the ruminai anaerobe Selenomonas ruminantium GA192. Curr. Microbiol. 43:293-298.
38. Whitehead, T. R., and R. B. Hespell. 1990. The genes for three xylandegrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region. J. Bacteriol. 172:2408-2412.