Action of Trichoderma reesei and Aspergillus oryzae esterases in the deacetylation of hemicelluloses

Maija Tenkanen

Research output: Contribution to journalArticleScientificpeer-review

38 Citations (Scopus)

Abstract

Xylans and mannans contain different esterified substituents such as acetyl, feruloyl and p‐coumaroyl side groups.
The functions of hemicellulose‐deacetylating esterases of Trichoderma reesei and Aspergillus oryzae are discussed in this paper. Both fungi produce multiple esterases and two different esterases were isolated from both T. reesei and A. oryzae.
The enzymes differed significantly in their substrate specificities. Acetyl xylan esterase of T. reesei was highly active on polymeric xylan but was unable to remove acetyl substituents from glucomannan or phenolic substituents from wheat straw arabinoxylan.
Another esterase, acetyl esterase from T. reesei, had activity only towards short oligomeric and monomeric acetates derived both from xylan and glucomannan.
The acetyl glucomannan esterase of A. oryzae was most active towards polymeric glucomannan, but was also able to remove acetyl groups from xylan. The only esterase studied which was active against phenolic substituents in arabinoxylans was the feruloyl esterase from A. oryzae.
Feruloyl esterase had the widest substrate specificity of the esterases studied. It was also able to act on acetyl groups both in xylan and in glucomannan. The simultaneous enzymic liberation of acetyl groups from xylan and glucomannan clearly enhanced the action of xylan‐ and mannan‐degrading enzymes, thus increasing the hydrolysis yield significantly.
However, none of the esterases was able to remove all acetyl substituents when acting alone and simultaneous action of two esterases was needed for complete deacetylation.
Original languageEnglish
Pages (from-to)19-24
JournalBiotechnology and Applied Biochemistry
Volume27
Issue number1
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

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Aspergillus oryzae
Trichoderma
Aspergillus
Esterases
Xylans
acetylxylan esterase
Substrate Specificity
hemicellulose
Mannans
Enzymes
Straw
Substrates
Fungi
Triticum
(1-6)-alpha-glucomannan
Hydrolysis
Acetates

Cite this

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title = "Action of Trichoderma reesei and Aspergillus oryzae esterases in the deacetylation of hemicelluloses",
abstract = "Xylans and mannans contain different esterified substituents such as acetyl, feruloyl and p‐coumaroyl side groups. The functions of hemicellulose‐deacetylating esterases of Trichoderma reesei and Aspergillus oryzae are discussed in this paper. Both fungi produce multiple esterases and two different esterases were isolated from both T. reesei and A. oryzae. The enzymes differed significantly in their substrate specificities. Acetyl xylan esterase of T. reesei was highly active on polymeric xylan but was unable to remove acetyl substituents from glucomannan or phenolic substituents from wheat straw arabinoxylan. Another esterase, acetyl esterase from T. reesei, had activity only towards short oligomeric and monomeric acetates derived both from xylan and glucomannan. The acetyl glucomannan esterase of A. oryzae was most active towards polymeric glucomannan, but was also able to remove acetyl groups from xylan. The only esterase studied which was active against phenolic substituents in arabinoxylans was the feruloyl esterase from A. oryzae. Feruloyl esterase had the widest substrate specificity of the esterases studied. It was also able to act on acetyl groups both in xylan and in glucomannan. The simultaneous enzymic liberation of acetyl groups from xylan and glucomannan clearly enhanced the action of xylan‐ and mannan‐degrading enzymes, thus increasing the hydrolysis yield significantly. However, none of the esterases was able to remove all acetyl substituents when acting alone and simultaneous action of two esterases was needed for complete deacetylation.",
author = "Maija Tenkanen",
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Action of Trichoderma reesei and Aspergillus oryzae esterases in the deacetylation of hemicelluloses. / Tenkanen, Maija.

In: Biotechnology and Applied Biochemistry, Vol. 27, No. 1, 1998, p. 19-24.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Action of Trichoderma reesei and Aspergillus oryzae esterases in the deacetylation of hemicelluloses

AU - Tenkanen, Maija

PY - 1998

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N2 - Xylans and mannans contain different esterified substituents such as acetyl, feruloyl and p‐coumaroyl side groups. The functions of hemicellulose‐deacetylating esterases of Trichoderma reesei and Aspergillus oryzae are discussed in this paper. Both fungi produce multiple esterases and two different esterases were isolated from both T. reesei and A. oryzae. The enzymes differed significantly in their substrate specificities. Acetyl xylan esterase of T. reesei was highly active on polymeric xylan but was unable to remove acetyl substituents from glucomannan or phenolic substituents from wheat straw arabinoxylan. Another esterase, acetyl esterase from T. reesei, had activity only towards short oligomeric and monomeric acetates derived both from xylan and glucomannan. The acetyl glucomannan esterase of A. oryzae was most active towards polymeric glucomannan, but was also able to remove acetyl groups from xylan. The only esterase studied which was active against phenolic substituents in arabinoxylans was the feruloyl esterase from A. oryzae. Feruloyl esterase had the widest substrate specificity of the esterases studied. It was also able to act on acetyl groups both in xylan and in glucomannan. The simultaneous enzymic liberation of acetyl groups from xylan and glucomannan clearly enhanced the action of xylan‐ and mannan‐degrading enzymes, thus increasing the hydrolysis yield significantly. However, none of the esterases was able to remove all acetyl substituents when acting alone and simultaneous action of two esterases was needed for complete deacetylation.

AB - Xylans and mannans contain different esterified substituents such as acetyl, feruloyl and p‐coumaroyl side groups. The functions of hemicellulose‐deacetylating esterases of Trichoderma reesei and Aspergillus oryzae are discussed in this paper. Both fungi produce multiple esterases and two different esterases were isolated from both T. reesei and A. oryzae. The enzymes differed significantly in their substrate specificities. Acetyl xylan esterase of T. reesei was highly active on polymeric xylan but was unable to remove acetyl substituents from glucomannan or phenolic substituents from wheat straw arabinoxylan. Another esterase, acetyl esterase from T. reesei, had activity only towards short oligomeric and monomeric acetates derived both from xylan and glucomannan. The acetyl glucomannan esterase of A. oryzae was most active towards polymeric glucomannan, but was also able to remove acetyl groups from xylan. The only esterase studied which was active against phenolic substituents in arabinoxylans was the feruloyl esterase from A. oryzae. Feruloyl esterase had the widest substrate specificity of the esterases studied. It was also able to act on acetyl groups both in xylan and in glucomannan. The simultaneous enzymic liberation of acetyl groups from xylan and glucomannan clearly enhanced the action of xylan‐ and mannan‐degrading enzymes, thus increasing the hydrolysis yield significantly. However, none of the esterases was able to remove all acetyl substituents when acting alone and simultaneous action of two esterases was needed for complete deacetylation.

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JO - Biotechnology and Applied Biochemistry

JF - Biotechnology and Applied Biochemistry

SN - 0885-4513

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ER -