Skip to main content
SpringerLink
Log in

Functional classification of the microbial feruloyl esterases

  • Mini-Review
  • Published:
Applied Microbiology and Biotechnology Aims and scope Submit manuscript

Abstract

Feruloyl esterases have potential uses over a broad range of applications in the agri-food industries. In recent years, the number of microbial feruloyl esterase activities reported has increased and, in parallel, even more related protein sequences may be discerned in the growing genome databases. Based on substrate utilisation data and supported by primary sequence identity, four sub-classes have been characterised and termed type-A, B, C and D. The proposed sub-classification scheme is discussed in terms of the evolutionary relationships existing between carbohydrate esterases.

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

Similar content being viewed by others

References

  • Andreasen MF, Kroon P, Williamson G, Garcia-Conesa MT (2001) Esterase activity able to hydrolyze dietary antioxidant hydroxycinnamates is distributed along the intestine of mammals. J Agric Food Chem 49:5679–5684

    Article  CAS  PubMed  Google Scholar 

  • Bartolome B, Faulds CB, Kroon PA, Waldron K, Gilbert HJ, Hazlewood G, Williamson G (1997) An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (XylD) release a 5-5′-ferulic dehydrodimer (diferulic acid) from barley and wheat cell walls. Appl Environ Microbiol 63:208–212

    PubMed  Google Scholar 

  • Basaran P, Hang YD (2000) Purification and characterization of acetyl esterase from Candida guilliermondii. Lett Appl Microbiol 30:167–171

    Article  CAS  PubMed  Google Scholar 

  • Blum DL, Li XL, Chen H, Ljungdahl LG (1999) Characterization of an acetyl xylan esterase from the anaerobic fungus Orpinomyces sp. strain PC-2. Appl Environ Microbiol 65:3990–3995

    CAS  PubMed  Google Scholar 

  • Blum DL, Kataeva IA, Li XL, Ljungdahl LG (2000) Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ. J Bacteriol 182:1346–1351

    Article  CAS  PubMed  Google Scholar 

  • Borneman WS, Ljungdahl LG, Hartley RD, Akin DE (1992) Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2. Appl Environ Microbiol 58:3762–3766

    CAS  PubMed  Google Scholar 

  • Castanares A, McCrae SI, Wood TM (1992) Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum. Enzyme Microb Technol 14:875–884

    Article  CAS  Google Scholar 

  • Coutinho PM, Henrissat B (1999) Carbohydrate-active enzymes: an integrated database approach. In: Gilbert HJ, Davies GJ, Svensson B, Henrissat B (eds), Recent advances in carbohydrate engineering. Royal Society of Chemistry, Cambridge, pp 3–12

  • Crepin VF, Faulds CB, Connerton IF (2003a) A non-modular type-B feruloyl esterase from Neurospora crassa exhibits concentration dependent substrate inhibition. Biochem J 370:417–427

    Article  CAS  PubMed  Google Scholar 

  • Crepin VF, Faulds CB, Connerton IF (2003b) Production and characterisation of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: identification of the nucleophilic serine. Protein Express Purif 29:176–184

    CAS  Google Scholar 

  • Dalrymple BP, Swadling Y, Cybinski DH, Xue GP (1996) Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminal bacterium Butyrivibrio fibrisolvens E14 by a novel method. FEMS Microbiol Lett 143:115–120

    Article  PubMed  Google Scholar 

  • De Vries RP, Visser J (1999) Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger. Appl Environ Microbiol 65:5500–5503

    PubMed  Google Scholar 

  • De Vries RP, Visser J (2001) Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol Mol Biol Rev 65:497–522

    PubMed  Google Scholar 

  • De Vries RP, Michelsen B, Poulsen CH, Kroon PA, Heuvel RH van den, Faulds CB, Williamson G, Hombergh JP van den, Visser J (1997) The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides. Appl Environ Microbiol 63:4638–4644

    PubMed  Google Scholar 

  • De Vries RP, Visser J, Graaff LH de (1999) CreA modulates the XlnR-induced expression on xylose of Aspergillus niger genes involved in xylan degradation. Res Microbiol 150:281–285

    PubMed  Google Scholar 

  • De Vries RP, Jansen J, Aguilar G, Parenicova l, Joosten V, Wulfert F, Benen JAE, Visser J (2002a) Expression profiling of pectinolytic genes from Aspergillus niger. FEBS Lett 530:41–47

    Article  PubMed  Google Scholar 

  • De Vries RP, Kuyk PA van, Kester HC, Visser J (2002b) The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem J 363:377–386

    PubMed  Google Scholar 

  • Degrassi G, Kojic M, Ljubijankic G, Venturi V (2000) The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. Microbiology 146:1585–1591

    CAS  PubMed  Google Scholar 

  • Donaghy JA, Bronnenmeier K, Soto-Kelly PF, McKay AM (2000) Purification and characterization of an extracellular feruloyl esterase from the thermophilic anaerobe Clostridium stercorarium. J Appl Microbiol 88:458–466

    Article  CAS  PubMed  Google Scholar 

  • Dowzer CEA, Kelly JM (1991) Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans. Mol Cell Biol 11:5701–5709

    CAS  PubMed  Google Scholar 

  • Ebbole DJ (1998) Carbon catabolic repression of gene expression and conidiation in Neurospora crassa. Fungal Genet Biol 25:15–21

    Article  CAS  PubMed  Google Scholar 

  • Faulds CB, Williamson G (1991) The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes. J Gen Microbiol 137:2339–2345

    CAS  PubMed  Google Scholar 

  • Faulds CB, Williamson G (1994) Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: Specificity for the phenolic moiety and binding to microcrystalline cellulose. Microbiology 140:779–787

    CAS  Google Scholar 

  • Faulds CB, Williamson G (1995) Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger. Appl Microbiol Biotechnol 43:1082–1087

    Google Scholar 

  • Faulds CB, Williamson G (1999) Effect of hydroxycinnamates and benzoates on the production of feruloyl esterases by Aspergillus niger. J Sci Food Agric 79:450–452

    Article  CAS  Google Scholar 

  • Faulds CB, De Vries RP, Kroon PA, Visser J, Williamson G (1997) Influence of ferulic acid on the production of feruloyl esterases by Aspergillus niger. FEMS Microbiol Lett 157:239–244

    Article  CAS  PubMed  Google Scholar 

  • Ferreira LMA, Wood TM, Williamson G, Faulds C, Hazlewood GP, Black GW, Gilbert HJ (1993) A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain. Biochem J 294:349–355

    CAS  PubMed  Google Scholar 

  • Fillingham IJ, Kroon PA, Williamson G, Gilbert HJ, Hazlewood GP (1999) A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex. Biochem J 343:215–224

    CAS  PubMed  Google Scholar 

  • Gutierrez R, Cederlund E, Hjelmqvist L, Peirano A, Herrera F, Ghosh D, Duax W, Jornvall H, Eyzaguirre J (1998) Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain. FEBS Lett 423:35–38

    Article  CAS  PubMed  Google Scholar 

  • Henikoff S, Henikoff J (1992) Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci USA 89:10915–10919

    CAS  Google Scholar 

  • Kroon PA, Williamson G (1996) Release of ferulic acid from sugar-beet pulp by using arabinanase, arabinofuranosidase and an esterase from Aspergillus niger. Biotechnol Appl Biochem 23:263–267

    Google Scholar 

  • Kroon PA, Faulds CB, Williamson G (1996) Purification and characterization of a novel esterase induced by growth of Aspergillus niger on sugar-beet pulp. Biotechnol Appl Biochem 23:255–262

    Google Scholar 

  • Kroon PA, Faulds CB, Brezillon C, Williamson G (1997) Methyl phenylalkanoates as substrates to probe the active site of esterases. Eur J Biochem 248:245–251

    CAS  PubMed  Google Scholar 

  • Kroon PA, Garcia-Conesa MT, Fillingham IJ, Hazlewood GP, Williamson G (1999) Release of ferulic acid dehydrodimers from plant cell walls by feruloyl esterases. J Sci Food Agric 79:428–434

    CAS  Google Scholar 

  • Kroon PA, Williamson G, Fish NM, Archer DB, Belshaw NJ (2000) A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module. Eur J Biochem 267:6740–6752

    CAS  PubMed  Google Scholar 

  • Linden J, Samara M, Decker S, Johnson E, Boyer M, Pecs M, Adney W, Himmel M (1994) Purification and characterization of an acetyl esterase from Aspergillus niger. Appl Biochem Biotechnol 383:45–46

    Google Scholar 

  • McCrae SI, Leith KM, Gordon AH, Wood TM (1994) Xylan-degrading enzyme system produced by the fungus Aspergillus awamori: isolation and characterization of a feruloyl esterase and a p-coumaroyl esterase. Enzyme Microb Technol 16:826–834

    Article  CAS  Google Scholar 

  • McDermid KP, Forsberg CW, MacKenzie CR (1990) Purification and properties of an acetyl xylan esterase from Fibrobacter succinogenes S85. Appl Environ Microbiol 56:3805–3810

    CAS  PubMed  Google Scholar 

  • Orejas M, MacCabe AP, Perez-Gonzalez JA, Kumar S, Ramon D (2001) The wide-domain carbon catabolite repressor CreA indirectly controls expression of the Aspergillus nidulans xlnB gene, encoding the acidic endo-β-(1,4)-xylanase X24. J Bacteriol 183:1517–1523

    Article  CAS  PubMed  Google Scholar 

  • Peij NNME van, Visser J, Graaff LH de (1998) Isolation and analysis of xlnR, encoding a transcriptional activator co-ordinating xylanolytic expression in Aspergillus niger. Microbiology 27:131–142

    Google Scholar 

  • Prates JAM, Tarbouriech N, Charnock SJ, Fontes CMGA, Ferreira LMA, Davies GJ (2001) The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition. Structure 9:1183–1190

    Article  CAS  PubMed  Google Scholar 

  • Ralet MC, Faulds CB, Williamson G, Thibault, JF (1994) Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger. Carbohydr Res 263:257–269

    CAS  PubMed  Google Scholar 

  • Ruijter GJG, Visser J (1997) Carbon repression in Aspergilli. FEMS Microbiol Lett 151:103–114

    PubMed  Google Scholar 

  • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406–425

    CAS  PubMed  Google Scholar 

  • Sancho AI, Faulds CB, Bartolomé B, Williamson G (1999) Characterisation of feruloyl esterase activity in barley. J Sci Food Agric 79:447–449

    Article  CAS  Google Scholar 

  • Schubot FD, Kataeva IA, Blum DL, Shah AC, Ljungdahl LG, Rose JP, Wang BC (2001) Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum. Biochemistry 40:12524–12532

    Article  CAS  PubMed  Google Scholar 

  • Shoham Y, Lamed R, Bayer EA (1999) The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol 7:275–281

    CAS  PubMed  Google Scholar 

  • Strauss J, Mach RL, Zeilinger S, Hartler G, Stoffler G, Wolschek M, Kubicek CP (1995) Cre1, the carbon catabolic repressor protein from Trichoderma reesei. FEBS Lett 376:103–107

    CAS  PubMed  Google Scholar 

  • Tenkanen M, Schuseil J, Puls J, Poutanen K (1991) Production, purification and characterization of an esterase liberating phenolic-acids from lignocellulosics. J Biotechnol 18:69–84

    CAS  Google Scholar 

  • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673–4680

    PubMed  Google Scholar 

  • Williamson G, Faulds CB, Kroon PA (1998a) Specificity of ferulic acid (feruloyl) esterases. Biochem Soc Trans 26:205–209

    CAS  PubMed  Google Scholar 

  • Williamson G, Kroon PA, Faulds CB (1998b) Hairy plant polysaccharides: a close shave with microbial esterases. Microbiology 144:2011–2023

    CAS  PubMed  Google Scholar 

Download references

Acknowledgements

We would like to thank the Biotechnology and Biological Sciences Research Council (BBSRC), UK, and the Department of Trade and Industry, UK, for their support through the LINK Applied Biocatalysts programme (Grant number BTL/27/12).

Author information

Authors and Affiliations

  1. Division of Food Sciences, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, UK

    V. F. Crepin & I. F. Connerton

  2. Food Materials Science Division, Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, UK

    C. B. Faulds

Authors
  1. V. F. Crepin
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. C. B. Faulds
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. I. F. Connerton
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to I. F. Connerton.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Crepin, V.F., Faulds, C.B. & Connerton, I.F. Functional classification of the microbial feruloyl esterases. Appl Microbiol Biotechnol 63, 647–652 (2004). https://doi.org/10.1007/s00253-003-1476-3

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00253-003-1476-3

Keywords

Search

Navigation