Deacetylation of xylans by acetyl esterases of Trichoderma reesei

Kaisa Poutanen, Maija Sundberg, Hans Korte, Jurgen Puls

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Two previously purified esterases of Trichoderma reesei were used to study the deacetylation of polymeric, oligomeric and dimeric acetylated xylan fragments. For the first time nearly complete enzymatic deacetylation of polymeric xylan with purified acetyl xylan esterase was demonstrated, resulting in precipitation of the remaining polymer structure. The esterases had very different substrate specifities, one having a preference for high molecular weight substrates and the other showing high activity only towards acetyl xylobiose. The latter enzyme was also regioselective, cleaving off the acetyl substituent only from the C-3 position of the xylopyranose ring. The highest xylose yield from acetylated xylan was obtained by the synergistic action of xylanase, \-xylosidase and acetyl xylan esterase.
Original languageEnglish
Pages (from-to)506-510
JournalApplied Microbiology and Biotechnology
Volume33
Issue number5
DOIs
Publication statusPublished - 1990
MoE publication typeA1 Journal article-refereed

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acetylxylan esterase
Xylans
Trichoderma
Esterases
Xylosidases
Xylose
Polymers
Molecular Weight
Enzymes

Cite this

Poutanen, Kaisa ; Sundberg, Maija ; Korte, Hans ; Puls, Jurgen. / Deacetylation of xylans by acetyl esterases of Trichoderma reesei. In: Applied Microbiology and Biotechnology. 1990 ; Vol. 33, No. 5. pp. 506-510.
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abstract = "Two previously purified esterases of Trichoderma reesei were used to study the deacetylation of polymeric, oligomeric and dimeric acetylated xylan fragments. For the first time nearly complete enzymatic deacetylation of polymeric xylan with purified acetyl xylan esterase was demonstrated, resulting in precipitation of the remaining polymer structure. The esterases had very different substrate specifities, one having a preference for high molecular weight substrates and the other showing high activity only towards acetyl xylobiose. The latter enzyme was also regioselective, cleaving off the acetyl substituent only from the C-3 position of the xylopyranose ring. The highest xylose yield from acetylated xylan was obtained by the synergistic action of xylanase, \-xylosidase and acetyl xylan esterase.",
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Deacetylation of xylans by acetyl esterases of Trichoderma reesei. / Poutanen, Kaisa; Sundberg, Maija; Korte, Hans; Puls, Jurgen.

In: Applied Microbiology and Biotechnology, Vol. 33, No. 5, 1990, p. 506-510.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Deacetylation of xylans by acetyl esterases of Trichoderma reesei

AU - Poutanen, Kaisa

AU - Sundberg, Maija

AU - Korte, Hans

AU - Puls, Jurgen

PY - 1990

Y1 - 1990

N2 - Two previously purified esterases of Trichoderma reesei were used to study the deacetylation of polymeric, oligomeric and dimeric acetylated xylan fragments. For the first time nearly complete enzymatic deacetylation of polymeric xylan with purified acetyl xylan esterase was demonstrated, resulting in precipitation of the remaining polymer structure. The esterases had very different substrate specifities, one having a preference for high molecular weight substrates and the other showing high activity only towards acetyl xylobiose. The latter enzyme was also regioselective, cleaving off the acetyl substituent only from the C-3 position of the xylopyranose ring. The highest xylose yield from acetylated xylan was obtained by the synergistic action of xylanase, \-xylosidase and acetyl xylan esterase.

AB - Two previously purified esterases of Trichoderma reesei were used to study the deacetylation of polymeric, oligomeric and dimeric acetylated xylan fragments. For the first time nearly complete enzymatic deacetylation of polymeric xylan with purified acetyl xylan esterase was demonstrated, resulting in precipitation of the remaining polymer structure. The esterases had very different substrate specifities, one having a preference for high molecular weight substrates and the other showing high activity only towards acetyl xylobiose. The latter enzyme was also regioselective, cleaving off the acetyl substituent only from the C-3 position of the xylopyranose ring. The highest xylose yield from acetylated xylan was obtained by the synergistic action of xylanase, \-xylosidase and acetyl xylan esterase.

U2 - 10.1007/BF00172542

DO - 10.1007/BF00172542

M3 - Article

VL - 33

SP - 506

EP - 510

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 5

ER -