Skip to main content
SpringerLink
Log in

Gene Cloning and Heterologous Expression of Glycoside Hydrolase Family 55 β-1,3-Glucanase from the Basidiomycete Phanerochaete Chrysosporium

  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

The basidiomycete Phanerochaete chrysosporium produces several β-1,3-glucanases when grown on laminarin, a β-1,3/1,6-glucan, as the sole carbon source. To characterize one of the major unknown β-1, 3-glucanases with a molecular mass of 83 kDa, identification, cloning, and heterologous over-expression were carried out using the total genomic information of P. chrysosporium. The cDNA encoding this enzyme included an ORF of 2337 bp and the deduced amino acid sequence contains a predicted signal peptide of 26 amino acids and the mature protein of 752 amino acids. The amino acid sequence showed a significant similarity with glycoside hydrolase family 55 enzymes from filamentous fungi and was named Lam55A. Since the recombinant Lam55A expressed in the methylotrophic yeast Pichia pastoris degraded branched β-1,3/1,6-glucan as well as linear β-1,3-glucan, the kinetic features of the enzyme were compared with those of other β-1,3-glucanases.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • A Abbas H Koc F Liu M Tien (2005) ArticleTitleFungal degradation of wood: initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate Curr. Genet. 47 49–56 Occurrence Handle10.1007/s00294-004-0550-4 Occurrence Handle1:CAS:528:DC%2BD2cXhtFWqsLbP Occurrence Handle15551134

    Article  CAS  PubMed  Google Scholar 

  • AT Bull CG Chesters (1966) ArticleTitleThe biochemistry of laminarin and the nature of laminarinase Adv. Enzymol. Relat. Areas Mol. Biol. 28 325–364 Occurrence Handle1:STN:280:CCiD1c7jtVU%3D Occurrence Handle5334063

    CAS  PubMed  Google Scholar 

  • R Cohen-Kupiec KE Broglie D Friesem RM Broglie I Chet (1999) ArticleTitleMolecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum Gene 226 147–154 Occurrence Handle10.1016/S0378-1119(98)00583-6 Occurrence Handle1:CAS:528:DyaK1MXhtFant7s%3D Occurrence Handle9931476

    Article  CAS  PubMed  Google Scholar 

  • JL Copa-Patio F Reyes MI Perez-Leblic (1989) ArticleTitlePurification and properties of a 1,3-β-glucanase from Penicillium oxalicum autolysates FEMS Microbiol. Lett. 65 285–292

    Google Scholar 

  • J la Cruz Particlede JA Pintor-Toro T Benitez A Llobell LC Romero (1995) ArticleTitleA novel endo-β-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum J. Bacteriol. 177 6937–6945

    Google Scholar 

  • BGG Donzelli M Lorito F Scala GE Harman (2001) ArticleTitleCloning, sequence and structure of a gene encoding an antifungal glucan 1,3-β-glucosidase from Trichoderma atroviride (T.␣harzianum) Gene 277 199–208 Occurrence Handle10.1016/S0378-1119(01)00681-3 Occurrence Handle1:CAS:528:DC%2BD3MXnsFGgurw%3D Occurrence Handle11602357

    Article  CAS  PubMed  Google Scholar 

  • T Fontaine RP Hartland A Beauvais M Diaquin J-P Latge (1997) ArticleTitlePurification and characterization of an endo-1,3-β-glucanase from Aspergillus fumigatus Eur. J. Biochem. 243 315–321 Occurrence Handle10.1111/j.1432-1033.1997.0315a.x Occurrence Handle1:CAS:528:DyaK2sXhtVWitLc%3D Occurrence Handle9030754

    Article  CAS  PubMed  Google Scholar 

  • G Giczey Z Kerenyi L Fulop L Hornok (2001) ArticleTitleExpression of cmg1, an exo-β-1,3-glucanase gene from Coniothyrium minitans, increases during sclerotial parasitism Appl. Environ. Microbiol. 67 865–871 Occurrence Handle10.1128/AEM.67.2.865-871.2001 Occurrence Handle1:CAS:528:DC%2BD3MXhtFSltr0%3D Occurrence Handle11157256

    Article  CAS  PubMed  Google Scholar 

  • K Igarashi M Yoshida H Matsumura N Nakamura H Ohno M Samejima T Nishino (2005) ArticleTitleElectron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium FEBS J. 272 2869–2877 Occurrence Handle10.1111/j.1742-4658.2005.04707.x Occurrence Handle1:CAS:528:DC%2BD2MXlt1Cmsrw%3D Occurrence Handle15943818

    Article  CAS  PubMed  Google Scholar 

  • T Kamada T Fujii T Nakagawa T Takemaru (1985) ArticleTitleChanges in (1->3)-β-glucanase activities during stipe elongation in Coprinus cinereus Curr. Microbiol. 12 257–260 Occurrence Handle10.1007/BF01567974 Occurrence Handle1:CAS:528:DyaL28Xms1SmsA%3D%3D

    Article  CAS  Google Scholar 

  • S Kasahara T Nakajima C Miyamoto K Wada Y Furuichi E Ichishima (1992) ArticleTitleCharacterization and mode of action of exo-1,3-β-D-glucanase from Aspergillus saitoi J. Ferment. Bioeng. 74 238–240 Occurrence Handle1:CAS:528:DyaK3sXislOn

    CAS  Google Scholar 

  • Kawai R, Igarashi K, Yoshida M, Kitaoka M, Samejima M (2005) Hydrolysis of β-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-β-glucanase from the basidiomycete Phanerochaete chrysosporium. Appl. Microbiol. Biotechnol. (in press)

  • R Kawai M Yoshida T Tani K Igarashi T Ohira H Nagasawa M Samejima (2003) ArticleTitleProduction and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast Pichia pastoris Biosci. Biotechnol. Biochem. 67 1–7 Occurrence Handle1:CAS:528:DC%2BD3sXhtVWqtro%3D Occurrence Handle12619666

    CAS  PubMed  Google Scholar 

  • D Martinez LF Larrondo N Putnam MD Gelpke K Huang J Chapman KG Helfenbein P Ramaiya JC Detter F Larimer PM Coutinho B Henrissat R Berka D Cullen D Rokhsar (2004) ArticleTitleGenome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78 Nat. Biotechnol. 22 695–700 Occurrence Handle1:CAS:528:DC%2BD2cXksV2gtro%3D Occurrence Handle15122302

    CAS  PubMed  Google Scholar 

  • AN Nikolskaya JW Pitkin HJ Schaeffer J-H Ahn JD Walton (1998) ArticleTitleEXG1p, a novel exo-β1,3-glucanase from the fungus Cochliobolus carbonum, contains a repeated motif present in other proteins that interact with polysaccharides Biochim. Biophys. Acta 1425 632–636 Occurrence Handle1:CAS:528:DyaK1cXns1Kltbw%3D Occurrence Handle9838227

    CAS  PubMed  Google Scholar 

  • R Nobe Y Sakakibara K Ogawa M Suiko (2003a) ArticleTitleCloning and expression of a novel Trichoderma viride laminarinase AI gene (lamAI) Biosci. Biotechnol. Biochem. 68 2111–2119

    Google Scholar 

  • R Nobe Y Sakakibara N Fukuda N Yoshida K Ogawa M Suiko (2003b) ArticleTitlePurification and characterization of laminarin hydrolases from Trichoderma viride Biosci. Biotechnol. Biochem. 67 1349–1357 Occurrence Handle10.1271/bbb.67.1349 Occurrence Handle1:CAS:528:DC%2BD3sXltlensrw%3D

    Article  CAS  Google Scholar 

  • K Oda S Kasahara Y Yamagata K Abe T Nakajima (2002) ArticleTitleCloning and expression of the exo-β-D-glucanase gene (exgS) from Aspergillus saitoi Biosci. Biotechnol. Biochem. 66 1587–1590 Occurrence Handle10.1271/bbb.66.1587 Occurrence Handle1:CAS:528:DC%2BD38XlvFemsbY%3D Occurrence Handle12224649

    Article  CAS  PubMed  Google Scholar 

  • SM Pitson RJ Seviour BM McDougall (1993) ArticleTitleNoncellulolytic fungal β-glucanases: their physiology and regulation Enzyme Microb. Technol. 15 178–192 Occurrence Handle10.1016/0141-0229(93)90136-P Occurrence Handle1:CAS:528:DyaK3sXhs1Crsr4%3D Occurrence Handle7763458

    Article  CAS  PubMed  Google Scholar 

  • DJ Rigden OL Franco (2002) ArticleTitleβ-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: domain architecture, modelling and assignment of catalytic residues FEBS Lett. 530 225–232 Occurrence Handle10.1016/S0014-5793(02)03490-7 Occurrence Handle1:CAS:528:DC%2BD38XnvVOrsL8%3D Occurrence Handle12387897

    Article  CAS  PubMed  Google Scholar 

  • HJ Schaeffer J Leykam JD Walton (1994) ArticleTitleCloning and targeted gene disruption of EXG1, encoding exo-β1,3-glucanase, in the phytopathogenic fungus Cochliobolus carbonum Appl. Environ. Microbiol. 60 594–598 Occurrence Handle1:CAS:528:DyaK2cXhvVChsro%3D Occurrence Handle8135518

    CAS  PubMed  Google Scholar 

  • T Usui T Toriyama T Mizuno (1979) ArticleTitleStructural investigation of laminaran of Eisenia-Bicyclis Agric. Biol. Chem. 43 603–611 Occurrence Handle1:CAS:528:DyaE1MXktVWltr0%3D

    CAS  Google Scholar 

  • S Vazquez-Garciduenas CA Leal-Morales A Herrera-Estrella (1998) ArticleTitleAnalysis of β-1,3-glucanolytic system of the biocontrol agent. Trichoderma harzianum Appl. Environ. Microbiol. 64 1442–1446 Occurrence Handle1:CAS:528:DyaK1cXitlCisbc%3D Occurrence Handle16349547

    CAS  PubMed  Google Scholar 

  • AV Wymelenberg G Sabat D Martinez AS Rajangam TT Teeri J Gaskell PJ Kersten D Cullen (2005) ArticleTitleThe Phanerochaete chrysosporium secretome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium J. Biotechnol. 118 17–34 Occurrence Handle10.1016/j.jbiotec.2005.03.010 Occurrence Handle15888348

    Article  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan

    Rie Kawai, Kiyohiko Igarashi & Masahiro Samejima

Authors
  1. Rie Kawai
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Kiyohiko Igarashi
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Masahiro Samejima
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Masahiro Samejima.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Kawai, R., Igarashi, K. & Samejima, M. Gene Cloning and Heterologous Expression of Glycoside Hydrolase Family 55 β-1,3-Glucanase from the Basidiomycete Phanerochaete Chrysosporium. Biotechnol Lett 28, 365–371 (2006). https://doi.org/10.1007/s10529-005-6179-7

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10529-005-6179-7

Keywords

Search

Navigation