Investigation of commercial enzyme preparations for selective release of arabinose from corn fibre

Csaba Fehér, Boglárka Gál, Anikó Fehér, Zsolt Barta, K. Réczey

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

BACKGROUND: Lignocellulosic materials have great potential in the production of L-arabinose in a new cost-effective way. Selective enzymatic liberation of L-arabinose from agricultural residues could be a promising method if purification of specific enzymes and extraction of pure polysaccharides could be omitted from the process. To achieve this goal, investigation of commercial multi-component enzyme preparations for selective release of L-arabinose from destarched corn fibre and soaking in aqueous ammonia (SAA) pretreated destarched corn fibres were performed. RESULTS: Hemicellulase NS22002 (Novozymes) has a relative xylanase activity of 1% (of measured highest) and 9%, and a relative arabinoxylan-arabinofuranohydrolase (AX-AFH) activity of 71% and 100% at pH 3 and 4, respectively. At pH 6 its relative xylanase and AX-AFH activities are 93% and 52%, respectively. Hydrolyses of SAA pretreated destarched corn fibre with Hemicellulase NS22002 at pH 4 and 6 resulted in a large amount of hemicellulosic oligomers, considerable amount of monomer arabinose and negligible amount of monomer xylose and galactose in the supernatants. During the hydrolysis at pH 3 monomer sugars were not released and low amounts of hemicellulosic oligomers were solubilised. CONCLUSION: SAA pretreatment has been found to be an appropriate method to make the structure of destarched corn fibre accessible for hemicellulose-degrading enzymes. Hemicellulase NS22002 has high endo-xylanase activity over a broad pH range, and its α-L-arabinofuranosidase can release arabinose from solubilised hemicellulosic oligomers derived from corn fibre. Enzymatic hydrolysis of SAA pretreated destarched corn fibre using Hemicellulase NS22002 is suitable to solubilise the hemicellulose fraction, however it cannot selectively release arabinose monomers.

Original languageEnglish
Pages (from-to)1329-1337
Number of pages9
JournalJournal of Chemical Technology and Biotechnology
Volume90
Issue number7
DOIs
Publication statusPublished - Jul 1 2015

Fingerprint

Arabinose
Zea mays
Enzymes
maize
enzyme
Ammonia
Fibers
ammonia
Monomers
Oligomers
hydrolysis
Hydrolysis
Agricultural wastes
Xylose
Enzymatic hydrolysis
Polysaccharides
Galactose
polysaccharide
Sugars
Purification

Keywords

  • Arabinofuranosidase
  • Corn fibre arabinoxylan
  • Enzymatic hydrolysis
  • Enzyme activity
  • Hemicellulases
  • Xylanase

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Biotechnology
  • Fuel Technology
  • Renewable Energy, Sustainability and the Environment
  • Pollution
  • Waste Management and Disposal
  • Inorganic Chemistry
  • Organic Chemistry

Cite this

Investigation of commercial enzyme preparations for selective release of arabinose from corn fibre. / Fehér, Csaba; Gál, Boglárka; Fehér, Anikó; Barta, Zsolt; Réczey, K.

In: Journal of Chemical Technology and Biotechnology, Vol. 90, No. 7, 01.07.2015, p. 1329-1337.

Research output: Contribution to journalArticle

Fehér, Csaba ; Gál, Boglárka ; Fehér, Anikó ; Barta, Zsolt ; Réczey, K. / Investigation of commercial enzyme preparations for selective release of arabinose from corn fibre. In: Journal of Chemical Technology and Biotechnology. 2015 ; Vol. 90, No. 7. pp. 1329-1337.
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AU - Barta, Zsolt

AU - Réczey, K.

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N2 - BACKGROUND: Lignocellulosic materials have great potential in the production of L-arabinose in a new cost-effective way. Selective enzymatic liberation of L-arabinose from agricultural residues could be a promising method if purification of specific enzymes and extraction of pure polysaccharides could be omitted from the process. To achieve this goal, investigation of commercial multi-component enzyme preparations for selective release of L-arabinose from destarched corn fibre and soaking in aqueous ammonia (SAA) pretreated destarched corn fibres were performed. RESULTS: Hemicellulase NS22002 (Novozymes) has a relative xylanase activity of 1% (of measured highest) and 9%, and a relative arabinoxylan-arabinofuranohydrolase (AX-AFH) activity of 71% and 100% at pH 3 and 4, respectively. At pH 6 its relative xylanase and AX-AFH activities are 93% and 52%, respectively. Hydrolyses of SAA pretreated destarched corn fibre with Hemicellulase NS22002 at pH 4 and 6 resulted in a large amount of hemicellulosic oligomers, considerable amount of monomer arabinose and negligible amount of monomer xylose and galactose in the supernatants. During the hydrolysis at pH 3 monomer sugars were not released and low amounts of hemicellulosic oligomers were solubilised. CONCLUSION: SAA pretreatment has been found to be an appropriate method to make the structure of destarched corn fibre accessible for hemicellulose-degrading enzymes. Hemicellulase NS22002 has high endo-xylanase activity over a broad pH range, and its α-L-arabinofuranosidase can release arabinose from solubilised hemicellulosic oligomers derived from corn fibre. Enzymatic hydrolysis of SAA pretreated destarched corn fibre using Hemicellulase NS22002 is suitable to solubilise the hemicellulose fraction, however it cannot selectively release arabinose monomers.

AB - BACKGROUND: Lignocellulosic materials have great potential in the production of L-arabinose in a new cost-effective way. Selective enzymatic liberation of L-arabinose from agricultural residues could be a promising method if purification of specific enzymes and extraction of pure polysaccharides could be omitted from the process. To achieve this goal, investigation of commercial multi-component enzyme preparations for selective release of L-arabinose from destarched corn fibre and soaking in aqueous ammonia (SAA) pretreated destarched corn fibres were performed. RESULTS: Hemicellulase NS22002 (Novozymes) has a relative xylanase activity of 1% (of measured highest) and 9%, and a relative arabinoxylan-arabinofuranohydrolase (AX-AFH) activity of 71% and 100% at pH 3 and 4, respectively. At pH 6 its relative xylanase and AX-AFH activities are 93% and 52%, respectively. Hydrolyses of SAA pretreated destarched corn fibre with Hemicellulase NS22002 at pH 4 and 6 resulted in a large amount of hemicellulosic oligomers, considerable amount of monomer arabinose and negligible amount of monomer xylose and galactose in the supernatants. During the hydrolysis at pH 3 monomer sugars were not released and low amounts of hemicellulosic oligomers were solubilised. CONCLUSION: SAA pretreatment has been found to be an appropriate method to make the structure of destarched corn fibre accessible for hemicellulose-degrading enzymes. Hemicellulase NS22002 has high endo-xylanase activity over a broad pH range, and its α-L-arabinofuranosidase can release arabinose from solubilised hemicellulosic oligomers derived from corn fibre. Enzymatic hydrolysis of SAA pretreated destarched corn fibre using Hemicellulase NS22002 is suitable to solubilise the hemicellulose fraction, however it cannot selectively release arabinose monomers.

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KW - Corn fibre arabinoxylan

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KW - Enzyme activity

KW - Hemicellulases

KW - Xylanase

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