Skip to main content

Advertisement

SpringerLink
Log in

Characterization of β-glucosidase from a strain of Penicillium purpurogenum KJS506

  • Biotechnologically Relevant Enzymes and Proteins
  • Published:
Applied Microbiology and Biotechnology Aims and scope Submit manuscript

Abstract

A novel β-glucosidase (BGL)-producing strain was isolated and identified as Penicillium purpurogenum KJS506 based on its morphology and internal transcribed spacer (ITS) rDNA gene sequence. When rice straw and corn steep powder were used as carbon and nitrogen sources, respectively, the maximal BGL activity of 12.3 U ml−1, one of the highest levels among BGL-producing microorganisms was observed. The optimum temperature and pH for BGL production were 32 °C and 4, respectively. An extracellular BGL was purified to homogeneity by sequential chromatography of P. purpurogenum culture supernatants, and the purified BGL showed higher activity (V max = 934 U mg protein–1) than most BGLs from other sources. The complete ORF of bgl3 was cloned from P. purpurogenum by a modified thermal asymmetric interlaced polymerase chain reaction. The bgl3 gene consists of a 2,571-bp ORF and encodes a putative protein containing 856 amino acids with a calculated molecular mass of 89,624 Da. The putative gene product was identified as a member of glycoside hydrolase family 3. The present results should contribute to improved industrial production of BGL by P. purpurogenum KJS506.

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

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Similar content being viewed by others

Reference

  • Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410

    CAS  Google Scholar 

  • Arja MJL, Vesa J, Raija L (2004) Three cellulases from Melanocarpus albomyces for textile treatment at neutral pH. Enzyme Microb Technol 34:332–341

    Article  Google Scholar 

  • Bahia A, Ali G (2006) Characterization of novel beta-glucosidase from a stachybotrys strain. Appl Microbiol Biotechnol 32:191–197

    Google Scholar 

  • Beguin P, Aubert JP (1994) The biological degradation of cellulose. FEMS Microbiol Rev 13:25–58

    Article  CAS  Google Scholar 

  • Bhat MK, Bhat S (1997) Cellulose degrading enzymes and their potential industrial applications. Biotechnol Adv 15:583–620

    Article  CAS  Google Scholar 

  • Coulibaly L, Naveau H, Agathos SN (2002) A tanks-in-series bioreactor to simulate macromolecule-laden wastewater pretreatment under sewer conditions by Aspergillus niger. Water Res 36:3941–3948

    Article  CAS  Google Scholar 

  • Daenen L, Saison D, Sterckx F, Delvaux FR, Verachtert H, Derdelinckx G (2008) Screening and evaluation of the glucoside hydrolase activity in Saccharomyces and Brettanomyces brewing yeasts. J Appl Microbiol 104:478–88

    CAS  Google Scholar 

  • Da-Silva R, Gomes E, Franco CML (1997) Pectinases, hemicelulase e cellulases substrate, production application no processamento de alimentos. Bol SBCTA 31:249–250

    Google Scholar 

  • de Palma-Fernandez ER, Gomes E, da Silva R (2002) Purification and characterization of two beta-glucosidases from the thermophilic fungus Thermoascus aurantiacus. Folia Microbiol (Praha) 47:685–690

    Article  Google Scholar 

  • Eriksson KE, Pettersson B, Westermark U (1974) Oxidation: an important enzyme reaction in fungal degradation of cellulose. FEBS Lett 49:282–285

    Article  CAS  Google Scholar 

  • Galas E, Romanowska I (1996) Production purification and characterization of a highly glucose-tolerant novel ß-glucosidase from Candida peltata. Appl Environ Microbiol 62:3165–3170

    Google Scholar 

  • Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A (2003) ExPASy: The proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31:3784–3788

    Article  CAS  Google Scholar 

  • Henrissat B (1998) Glycosidase families. Biochem Soc Trans 26:153–156

    CAS  Google Scholar 

  • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci U.S.A. 92:7090–7094

    Article  Google Scholar 

  • Himmel ME, Adney WS, Fox JW, Mitchell DJ, Baker JO (1993) Isolation and characterization of two forms of beta-D-glucosidase from Aspergillus niger. Appl Biochem Biotechnol 39–40:213–225

    Article  Google Scholar 

  • Joo AR et al (2009) Purification and characterization of a beta-1,4-glucosidase from a newly isolated strain of Fomitopsis pinicola. Appl Microbiol Biotechnol 83:285–294

    Article  CAS  Google Scholar 

  • Karnchanatat A et al (2007) Purification and biochemical characterization of an extracellular beta-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.:Fr.) Rehm. FEMS Microbiol Lett 270:162–170

    Article  CAS  Google Scholar 

  • Kaur J, Bhupinder SC, Badhan AK, Ghatora KS (2007) Purification and characterization of β-glucosidase from Melanocarpus sp MTCC 3922. Electron J Biotechnol 10:261–270

    Article  Google Scholar 

  • Kempton JB, Withers SG (1992) Mechanism of Agrobacterium beta-glucosidase: kinetic studies. Biochemistry 31:9961–9969

    Article  CAS  Google Scholar 

  • Kuriyama K, Tsuchiya K, Murui T (1995) Some properties of transglycosylation activity of sesame β-glucosidase. Biosci Biotechnol Biochem 59:1142–1143

    Article  CAS  Google Scholar 

  • Leclerc MAA, Ratomahenina R, Galzy P (1987) Yeast β-glucosidases. Biotechnol Genet Eng Rev 5:269–295

    CAS  Google Scholar 

  • Leite RSR, Gomes E, Da-Silva R (2007) Characterization and comparison of thermostability of purified β-glucosidases from a mesophilic Aureobasidium pullulans and thermophilic Thermoascus aurantiacus. Process Biochem 42:1101–1106

    Article  CAS  Google Scholar 

  • Lin J, Balakrishna P, Suren S (1999) Purification and biochemical characterization of β-glucosidase from a thermophilic fungus, Thermomyces lanuginosus - SSBP. Biotechnol Appl Biochem 30:81–87

    CAS  Google Scholar 

  • Liu YG, Huang N (1998) Efficient amplification of insert end sequences from bacterial artificial chromosome clones by thermal asymmetric interlaced PCR. Plant Mol Bio Rep 16:175–181

    Article  CAS  Google Scholar 

  • Liu YG, Whittier RF (1995) Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25:674–681

    Article  CAS  Google Scholar 

  • Lymar ES, Li B, Renganathan V (1995) Purification and characterization of a cellulose-binding (beta)-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium. Appl Environ Microbiol 61:2976–2980

    CAS  Google Scholar 

  • Mach R, Zeilinger S (2003) Regulation of gene expression in industrial fungi Trichoderma. Appl Microbiol biotechnol 60:515–522

    CAS  Google Scholar 

  • Magalhaes PO, Ferraz A, Milagres AF (2006) Enzymatic properties of two β-glucosidases from Ceriporiopsis subvermispora produced in biopulping conditions. J Appl Microbiol 101:480–486

    Article  CAS  Google Scholar 

  • Makoto M, Isao O, Sakuzo F, Ichiro Y (1988) Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae. Appl Microbiol Biotechnol 54:3147–3155

    Google Scholar 

  • Rashid MH, Siddiqui KS (1997) Purification and characterization of a beta-glucosidase from Aspergillus niger. Folia Microbiol (Praha) 42:544–550

    Article  CAS  Google Scholar 

  • Saha BC, Freer SN, Bothast RJ (1994) Production, purification, and properties of a thermostable beta-glucosidase from a color variant strain of Aureobasidium pullulans. Appl Environ Microbiol 60:3774–3780

    CAS  Google Scholar 

  • Saloheimo M, Nakari-Setala T, Tenkanen M, Penttila M (1997) cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast. Eur J Biochem 249:584–591

    Article  CAS  Google Scholar 

  • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68:850–858

    Article  CAS  Google Scholar 

  • Shinoyama HTV, Ando A, Fujii T, Sasaki M, Doi Y, Yasui T (1991) Enzymatic synthesis of useful alkyl-β-glucosides. Agri Biol Chem 55:1679–1681

    CAS  Google Scholar 

  • Stahl P, Klug M (1996) Characterization and differentiation of filamentous fungi based on fatty acid composition. Appl Environ Microbiol 62:4136–4146

    CAS  Google Scholar 

  • Valaskova V, Baldrian P (2006) Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus-production of extracellular enzymes and characterization of the major cellulases. Microbiology 152:3613–3622

    Article  CAS  Google Scholar 

  • Wei DL, Kirimura K, Usami S, Lin TH (1996) Purification and characterization of an extracellular beta-glucosidase from the wood-grown fungus Xylaria regalis. Curr Microbiol 33:297–301

    Article  CAS  Google Scholar 

  • Wong WK, Ali A, Chan WK, Ho V, Lee NT (1998) The cloning, expression and characterization of a cellobiase gene encoding a secretory enzyme from Cellulomonas biazotea. Gene 207:79–86

    Article  CAS  Google Scholar 

  • Workman WE, Day DF (1982) Purification and properties of beta-glucosidase from Aspergillus terreus. Appl Environ Microbiol 44:1289–1295

    CAS  Google Scholar 

  • Yan TS, Lin CL (1996) Purification and characterization of a glucose-tolerant β-glucosidase from Aspergillus niger CCRC31494. Biosci Biotechnol Biochem 61:965–970

    Article  Google Scholar 

Download references

Acknowledgment

This study was supported by a grant (code 2008A0080126) from ARPC. This subject was also supported by Korea Ministry of Environment as “The GAIA Project”.

Author information

Authors and Affiliations

  1. Department of Chemical Engineering, Konkuk University, Seoul, 143-701, South Korea

    Marimuthu Jeya, Kyoung-Mi Lee, Manish Kumar Tiwari, Kyoung-Min Lee, Sang-Hwan Kim & Jung-Kul Lee

  2. Department of Bioscience and Biotechnology, Konkuk University, Seoul, 143-701, South Korea

    Ah-Reum Joo

  3. Institute of Biomedical Science and Technology, Konkuk University, Seoul, 143-701, South Korea

    Kyoung-Mi Lee & Jung-Kul Lee

Authors
  1. Marimuthu Jeya
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ah-Reum Joo
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Kyoung-Mi Lee
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Manish Kumar Tiwari
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Kyoung-Min Lee
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Sang-Hwan Kim
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Jung-Kul Lee
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Jung-Kul Lee.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jeya, M., Joo, AR., Lee, KM. et al. Characterization of β-glucosidase from a strain of Penicillium purpurogenum KJS506. Appl Microbiol Biotechnol 86, 1473–1484 (2010). https://doi.org/10.1007/s00253-009-2395-8

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00253-009-2395-8

Keywords

Search

Navigation