Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 63, 1999 - Issue 2
Journal homepage
196
Views
10
CrossRef citations to date
0
Altmetric
Original Articles

Isolation and Properties of an Extracellular β-Glucosidase from a Filamentous Fungus, Cladosporium resinae, Isolated from Kerosene

Ki-Bong OHDepartment of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology
,
Kazu HAMADADepartment of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology
,
Mikako SAITODepartment of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology
,
Hun-Jun LEEMicrobiological Test & Research Center
&
Hideaki MATSUOKADepartment of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology
Pages 281-287 | Received 11 Aug 1998, Accepted 29 Oct 1998, Published online: 22 May 2014

  • 1) Gueguen, Y., Chemardin, P., Arnaud, A., and Galzy, P., Purification and characterization of an intracellular β-glucosidases from Botrytis cinerea. Enzyme Microb. Technol., 78, 900-906 (1995).
  • 2) Saha, B. C., and Bothast, R. J., Production, purification, and characterization of a highly glucose-tolerant novel β-glucosidase from Candida peltata. Appl. Environ. Microbiol., 62, 3165-3170 (1996).
  • 3) Kwon, K.-S., Kang, H.-G., and Hah, Y.-C., Purification and characterization of two extracellular β-glucosidase from Aspergillus nidulans. FEMS Microbiol. Lett., 97, 149-154 (1992).
  • . 1995. p. 197- 207.
  • 5) Srivastava, S. K., Gopalakrishnan, K. S., and Ramachandran, K. B., Kinetic characterization of a crude β-D-glucosidase from Aspergillus wentii Pt 2804. Enzyme Microb. Technol., 6, 508-511 (1984).
  • 6) Rapp, P., Grote, E., and Wagner, F., Formation and location of 1,4-β-glucanases and β-glucosidases from Penicillium janthinellum. Appl. Environ. Microbiol., 41, 857-866 (1981).
  • 7) Schmid, G., and Wandrey, C., Purification and partial characterization of a cellodextrin glucohydrolase (β-glucosidase) from Trichoderma reesei strain QM 9414. Biotechnol. Bioeng., 30, 571-585 (1987).
  • 8) Parbery, D. G., The natural occurrence of Cladosporium resinae. Trans. Brit. Mycol. Soc., 53, 15-23 (1969).
  • 9) McCleary, B. V., and Anderson, M. A., Hydrolysis of α-D-glucans and α-D-gluco-oligosaccharides by Cladosporium resinae glucoamylases. Carbohydr. Res., 86, 77-96 (1980).
  • 10) Parbery, D. G., Amorphotheca resinae gen. nov., sp. nov.: The perfect stage of Cladosporium resinae. Aust. J. Bot., 17, 331-357 (1969).
  • 11) Bushnell, L. D., and Haas, H. F., The utilization of certain hydrocarbons by microorganisms. J. Bacteriol., 41, 653-673 (1941).
  • 12) Ahluwalia, A., Gupta, J. K., Vadehra, D. V., and Sharma, P., Production of β-glucosidase by Cladosporium resinae. MIRCEN J., 5, 205-215 (1989).
  • 13) Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
  • 14) Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
  • 15) Hugget, A. S. C., andNixon, D. A., Glucose oxidase method for measurement of glucose. Biochem. J., 6, 12-19 (1957).
  • 16) Lineweaver, H., and Burk, D., The determination of enzyme dissociation constants. J. Am. Chem. Soc., 56, 658-666 (1934).
  • 17) Sternberg, D., Vijayakumar, P., and Reese, E. T., β-Glucosidase: microbial production and effect on enzymatic hydrolysis of cellulose. Can. J. Microbiol., 23, 139-147 (1977).
  • 18) Jermyn, M. A., Fungal cellulases-the nature of the inductive process for aryl-β-glucosidase in Stachybotrys atra. Aust. J. Biol. Sci., 18, 387-415 (1965).
  • 19) Lusis, A. J., and Becker, R. R., β-Glucosidase of Chaetomium thermophile var. coprophile-N-VAR. Biochim. Biophys. Acta, 329, 5-16 (1973).
  • 20) Deshpande, V., Eriksson, K. E., and Pettersson, B., Production, purification and partial characterization of β-glucosidase enzyme from Sporotrichum pulverulentum. Eur. J. Biochem., 90, 191-198 (1978).
  • 21) Marchin, G. L., and Duerksen, J. D., Purification of β-glucosidase from Saccharomyces lactis strain Y-14 and Y-1057A. J. Bacteriol., 96, 1181-1186 (1968).
  • 22) Ait, N., Creuzet, N., and Cattaneo, J., Properties of β-glucosidase purified from Clostridium thermocellum. J. Gen. Microbiol., 128, 569-577 (1982).
  • 23) Freer, S. N., Purification and characterization of the extracellular β-glucosidase produced by Candida wickerhamii. Arch. Biochem. Biophys., 243, 515-522 (1985).
  • 24) Li, X., and Calza, R. E., Purification and characterization of an extracellular β-glucosidase from the rumen fungus Neocallimastix frontalis EB188. Enzyme Microb. Technol., 13, 622-628 (1991).
  • 25) Watanabe, T., Sato, T., Yoshioka, S., Koshijima, T., and Kuwahara, M., Purification and properties of Aspergillus niger β-glucosidase. Eur. J. Biochem., 209, 651-659 (1992).
  • 26) Lymar, E. S., Li, B., and Renganathan, V., Purification and characterization of a cellulose-binding β-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium. Appl. Environ. Microbiol., 61, 2976-2980 (1995).
  • 27) Teunissen, M. J., Lahaye, D. H. T. P., Tveld, J. H. J. H. I., and Vogels, G. D., Purification and characterization of an extracellular β-glucosidase from the anaerobic fungus Piromyces sp. strain E2. Arch. Microbiol., 158, 276-281 (1992).
  • 28) Li, X., and Calza, R. E., Kinetic study of a cellobiase purified from Neocallimastix frontalis EB188. Biochim. Biophys. Acta, 1080, 148-154 (1991).
  • 29) Herbaud, M., and Fevre, M., Purification and characterization of an aspecific glucoside hydrolase from the anaerobic ruminal fungus Neocallimastix frontalis. Appl. Environ. Microbiol., 56, 3164-3169 (1990).
  • 30) Dekker, R. F. H., Induction, localization and characterization of β-glucosidases produced by a species of Monilia. J. Gen. Microbiol., 127, 177-184 (1981).
  • 31) Wood, T. M., and McCrae, S. I., Purification and some properties of the extracellular β-glucosidase of the cellulolytic fungus Trichoderma koningii. J. Gen. Microbiol., 128, 2973-2982 (1982).
  • 32) Coughlan, M. P., The properties of fungal and bacterial cellulases with comments on their production and application. Biotechnol. Genet. Eng. Rev., 3, 39-109 (1985).
  • 33) Kengen, S. W. M., Leusink, E. J., Stams, A. J. M., and Zehnder, A. J. B., Purification and characterization of an extremely thermostable β-glucosidase from hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem., 213, 305-312 (1993).
  • 34) Woodward, J., and Wiseman, A., Fungal and other β-glucosidases-their properties and applications. Enzyme Microb. Technol., 4, 73-79 (1982).
  • 35) Saha, B. C., Freer, S. N., and Bothast, R. J., Production, purification, and properties of a thermostable β-glucosidase from a color variant strain of Aureobasidium pullulans. Appl. Environ. Microbiol., 60, 3774-3780 (1994).
  • 36) Sanyal, A., Kundu, R. K., Dube, S., and Dube, D. K., Extracellular cellulolytic system of Aspergillus japonicus: purification and characterization of an inducible extracellular β-glucosidase. Enzyme Microb. Technol., 10, 91-99 (1988).
  • 37) Ozaki, H., and Yamada, K., Isolation of Streptomyces sp. producing glucose-tolerant β-glucosidases and properties of the enzymes. Agric. Biol. Chem., 55, 979-987 (1992).
  • 38) Christakopoulos, P., Goodenough, P. W., Kekos, D., Macris, B. J., Claeyssens, M., and Bhat, M. K., Purification and characterization of an extracellular β-glucosidase with transglycosylation and exo-glucosidase activities from Fusarium oxysporum. Eur. J. Biochem., 224, 376-385 (1994).
  • 39) Wright, W. M., Yablonsky, M. D., Ahalita, Z. P., Goyal, A. K., and Eveleigh, D. E., Cloning, characterization, and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli. Appl. Environ. Microbiol., 58, 3455-3465 (1992).
  • 40) Yan, T. S., and Lin, C. H., Purification and characterization of a glucose-tolerant β-glucosidase from Aspergillus niger CCRC 31494. Biosci. Biotechnol. Biochem., 61, 965-970 (1997).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.