Synergy between xylanases from glycoside hydrolase family 10 and family 11 and a feruloyl esterase in the release of phenolic acids from cereal arabinoxylan
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The bioconversion of waste residues (by-products) from cereal processing industries requires the cooperation of enzymes able to degrade xylanolytic and cellulosic material. The type A feruloyl esterase from Aspergillus niger, AnFaeA, works synergistically with (1→4)-β-d-xylopyranosidases (xylanases) to release monomeric and dimeric ferulic acid (FA) from cereal cell wall-derived material. The esterase was more effective with a family 11 xylanase from Trichoderma viride in releasing FA and with a family 10 xylanase from Thermoascus aurantiacus in releasing the 5,5′ form of diferulic acid from arabinoxylan (AX) derived from brewers’ spent grain. The converse was found for the release of the phenolic acids from wheat bran-derived AXs. This may be indicative of compositional differences in AXs in cereals.
KeywordsFerulic Acid Wheat Bran Aleurone Layer Trichoderma Viride Feruloyl Esterase
Brewers’ spent grain
Family 10 xylanase
Family 11 xylanase
This work was supported by the Biotechnology and Biological Sciences Research Council (BBSRC), UK; the General Secretariat for Research and Technology (GSRT), Greece; the British Council (Athens); the European Social Fund; and the Department of the Environment, Food and Rural Affairs (DEFRA), UK. We would like to express our gratitude to Scottish Courage Ltd for supplying BSG and to ARD for the WB sample.
- Bartolomé B, Faulds CB, Tuohy M, Hazlewood GP, Gilbert HJ, Williamson G (1995) Influence of different xylanases on the activity of ferulic acid esterase on wheat bran. Biotechnol Appl Biochem 22:65–73Google Scholar
- Bartolomé B, Faulds CB, Kroon PA, Waldron K, Gilbert HJ, Hazlewood GP, 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 63:208–212PubMedGoogle Scholar
- Coutinho PM, Henrissat B (1999) Carbohydrate-active enzymes: an integrated database approach. In: Gilbert HJ, Davies GJ, Henrissat B, Svensson B (eds) Recent advances in carbohydrate bioengineering. Royal Society of Chemistry, Cambridge pp 3–12Google Scholar
- Debeire P, Priem B, Strecker G, Vignon M (1990) Purification and properties of an endo-1,4-xylanase excreted by a hydrolytic thermophilic anaerobe, Clostridium thermolacticum—a proposal for its action mechanism on larchwood 4-O-methylglucuronoxylan. Eur J Biochem 187:573–580CrossRefPubMedGoogle Scholar
- Faulds CB (2003) Feruloyl esterases: molecular tools to unravel cell structure. Recent Res Dev Appl Microbiol Biotechnol 1:245–275Google Scholar
- Kormelink FJM, Searle-van Leeuwen MJF, Wood TM, Voragen AGJ (1993) Purification and characterization of a (1,4)-β-D-arabinoxylan arabinofuranohydrolase from Aspergillus awamori. Appl Microbiol Biotechnol 35:753–758Google Scholar
- Parker ML, Ng A, Waldron KW (2005) The phenolic acid and polysaccharide composition of cell walls of bran layers of mature wheat (Triticum aestivum L. cv Avalon) grains. J Sci Food Agric (in press)Google Scholar
- Valverde P (1994) Barley spent grain and its future. Cerveza y Malta 122:7–26Google Scholar