Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics

Maija Tenkanen (Corresponding Author), Johannes Schuseil, Jurgen Puls, Kaisa Poutanen

Research output: Contribution to journalArticleScientificpeer-review

113 Citations (Scopus)

Abstract

Production of extracellular esterase cleaving phenolic sidegroups from xylan was investigated using strains of Aspergillus. The activity levels produced were unrelated to the ferulic acid content of the lignocellulosic raw material in the cultivation medium. No correlation between the production of feruloyl esterase, acetyl xylan esterase and acetyl esterase activities was observed either. An esterase produced by Aspergillus oryzae was purified to electrophoretic homogeneity. The enzyme was an acidic monomeric protein having an isoelectric point of 3.6 and a molecular mass of 30 kDa. It was most active in the pH-range from 4.5 to 6.0 and was stable at temperatures up to 45°C. The esterase had a wide substrate specificity, liberating ferulic, p-coumaric and acetic acids from steam-extracted wheat straw fragments and acetic acid from acetylated xylo-oligomers and α-naphthyl acetate. The enzyme acted in synergism with other xylanolytic enzymes, which was reflected in increased production of phenolic acids from wheat straw xylo-oligosaccharides in the presence of xylanases of Trichoderma reesei.

Original languageEnglish
Pages (from-to)69 - 84
Number of pages16
JournalJournal of Biotechnology
Volume18
Issue number1
DOIs
Publication statusPublished - 1991
MoE publication typeA1 Journal article-refereed

Fingerprint

Esterases
Purification
ferulic acid
Acids
Aspergillus
acetylxylan esterase
Straw
Triticum
Enzymes
Aspergillus oryzae
Acetic acid
Xylans
Trichoderma
Steam
Isoelectric Point
Molecular mass
Substrate Specificity
Oligosaccharides
Oligomers
Acetic Acid

Cite this

@article{7b27bd1ad61a46e69e1320841d80d4f1,
title = "Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics",
abstract = "Production of extracellular esterase cleaving phenolic sidegroups from xylan was investigated using strains of Aspergillus. The activity levels produced were unrelated to the ferulic acid content of the lignocellulosic raw material in the cultivation medium. No correlation between the production of feruloyl esterase, acetyl xylan esterase and acetyl esterase activities was observed either. An esterase produced by Aspergillus oryzae was purified to electrophoretic homogeneity. The enzyme was an acidic monomeric protein having an isoelectric point of 3.6 and a molecular mass of 30 kDa. It was most active in the pH-range from 4.5 to 6.0 and was stable at temperatures up to 45°C. The esterase had a wide substrate specificity, liberating ferulic, p-coumaric and acetic acids from steam-extracted wheat straw fragments and acetic acid from acetylated xylo-oligomers and α-naphthyl acetate. The enzyme acted in synergism with other xylanolytic enzymes, which was reflected in increased production of phenolic acids from wheat straw xylo-oligosaccharides in the presence of xylanases of Trichoderma reesei.",
author = "Maija Tenkanen and Johannes Schuseil and Jurgen Puls and Kaisa Poutanen",
note = "Project code: BIO1023",
year = "1991",
doi = "10.1016/0168-1656(91)90236-O",
language = "English",
volume = "18",
pages = "69 -- 84",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "1",

}

Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics. / Tenkanen, Maija (Corresponding Author); Schuseil, Johannes; Puls, Jurgen; Poutanen, Kaisa.

In: Journal of Biotechnology, Vol. 18, No. 1, 1991, p. 69 - 84.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics

AU - Tenkanen, Maija

AU - Schuseil, Johannes

AU - Puls, Jurgen

AU - Poutanen, Kaisa

N1 - Project code: BIO1023

PY - 1991

Y1 - 1991

N2 - Production of extracellular esterase cleaving phenolic sidegroups from xylan was investigated using strains of Aspergillus. The activity levels produced were unrelated to the ferulic acid content of the lignocellulosic raw material in the cultivation medium. No correlation between the production of feruloyl esterase, acetyl xylan esterase and acetyl esterase activities was observed either. An esterase produced by Aspergillus oryzae was purified to electrophoretic homogeneity. The enzyme was an acidic monomeric protein having an isoelectric point of 3.6 and a molecular mass of 30 kDa. It was most active in the pH-range from 4.5 to 6.0 and was stable at temperatures up to 45°C. The esterase had a wide substrate specificity, liberating ferulic, p-coumaric and acetic acids from steam-extracted wheat straw fragments and acetic acid from acetylated xylo-oligomers and α-naphthyl acetate. The enzyme acted in synergism with other xylanolytic enzymes, which was reflected in increased production of phenolic acids from wheat straw xylo-oligosaccharides in the presence of xylanases of Trichoderma reesei.

AB - Production of extracellular esterase cleaving phenolic sidegroups from xylan was investigated using strains of Aspergillus. The activity levels produced were unrelated to the ferulic acid content of the lignocellulosic raw material in the cultivation medium. No correlation between the production of feruloyl esterase, acetyl xylan esterase and acetyl esterase activities was observed either. An esterase produced by Aspergillus oryzae was purified to electrophoretic homogeneity. The enzyme was an acidic monomeric protein having an isoelectric point of 3.6 and a molecular mass of 30 kDa. It was most active in the pH-range from 4.5 to 6.0 and was stable at temperatures up to 45°C. The esterase had a wide substrate specificity, liberating ferulic, p-coumaric and acetic acids from steam-extracted wheat straw fragments and acetic acid from acetylated xylo-oligomers and α-naphthyl acetate. The enzyme acted in synergism with other xylanolytic enzymes, which was reflected in increased production of phenolic acids from wheat straw xylo-oligosaccharides in the presence of xylanases of Trichoderma reesei.

U2 - 10.1016/0168-1656(91)90236-O

DO - 10.1016/0168-1656(91)90236-O

M3 - Article

VL - 18

SP - 69

EP - 84

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 1

ER -