Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation

Sanna Koutaniemi, Martine P van Gool, Minna Juvonen, Jouni Jokela, Sandra W Hinz, Henk A Schols, Maija Tenkanen

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Mass spectrometric analysis was used to compare the roles of two acetyl esterases (AE, carbohydrate esterase family CE16) and three acetyl xylan esterases (AXE, families CE1 and CE5) in deacetylation of natural substrates, neutral (linear) and 4-O-methyl glucuronic acid (MeGlcA) substituted xylooligosaccharides (XOS). AEs were similarly restricted in their action and apparently removed in most cases only one acetyl group from the non-reducing end of XOS, acting as exo-deacetylases. In contrast, AXEs completely deacetylated longer neutral XOS but had difficulties with the shorter ones. Complete deacetylation of neutral XOS was obtained after the combined action of AEs and AXEs. MeGlcA substituents partially restricted the action of both types of esterases and the remaining acidic XOS were mainly substituted with one MeGlcA and one acetyl group, supposedly on the same xylopyranosyl residue. These resisting structures were degraded to great extent only after inclusion of α-glucuronidase, which acted with the esterases in a synergistic manner. When used together with xylan backbone degrading endoxylanase and β-xylosidase, both AE and AXE enhanced the hydrolysis of complex XOS equally.
Original languageEnglish
JournalJournal of Biotechnology
Volume168
Issue number4
Pages (from-to)684– 692
Number of pages9
ISSN0168-1656
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 414 Agricultural biotechnology
  • 1182 Biochemistry, cell and molecular biology

Cite this

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title = "Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation",
abstract = "Mass spectrometric analysis was used to compare the roles of two acetyl esterases (AE, carbohydrate esterase family CE16) and three acetyl xylan esterases (AXE, families CE1 and CE5) in deacetylation of natural substrates, neutral (linear) and 4-O-methyl glucuronic acid (MeGlcA) substituted xylooligosaccharides (XOS). AEs were similarly restricted in their action and apparently removed in most cases only one acetyl group from the non-reducing end of XOS, acting as exo-deacetylases. In contrast, AXEs completely deacetylated longer neutral XOS but had difficulties with the shorter ones. Complete deacetylation of neutral XOS was obtained after the combined action of AEs and AXEs. MeGlcA substituents partially restricted the action of both types of esterases and the remaining acidic XOS were mainly substituted with one MeGlcA and one acetyl group, supposedly on the same xylopyranosyl residue. These resisting structures were degraded to great extent only after inclusion of α-glucuronidase, which acted with the esterases in a synergistic manner. When used together with xylan backbone degrading endoxylanase and β-xylosidase, both AE and AXE enhanced the hydrolysis of complex XOS equally.",
keywords = "414 Agricultural biotechnology, 1182 Biochemistry, cell and molecular biology",
author = "Sanna Koutaniemi and {van Gool}, {Martine P} and Minna Juvonen and Jouni Jokela and Hinz, {Sandra W} and Schols, {Henk A} and Maija Tenkanen",
year = "2013",
doi = "10.1016/j.jbiotec.2013.10.009",
language = "English",
volume = "168",
pages = "684– 692",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier Scientific Publ. Co",
number = "4",

}

Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation. / Koutaniemi, Sanna; van Gool, Martine P; Juvonen, Minna; Jokela, Jouni; Hinz, Sandra W; Schols, Henk A; Tenkanen, Maija.

In: Journal of Biotechnology, Vol. 168, No. 4, 2013, p. 684– 692.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation

AU - Koutaniemi, Sanna

AU - van Gool, Martine P

AU - Juvonen, Minna

AU - Jokela, Jouni

AU - Hinz, Sandra W

AU - Schols, Henk A

AU - Tenkanen, Maija

PY - 2013

Y1 - 2013

N2 - Mass spectrometric analysis was used to compare the roles of two acetyl esterases (AE, carbohydrate esterase family CE16) and three acetyl xylan esterases (AXE, families CE1 and CE5) in deacetylation of natural substrates, neutral (linear) and 4-O-methyl glucuronic acid (MeGlcA) substituted xylooligosaccharides (XOS). AEs were similarly restricted in their action and apparently removed in most cases only one acetyl group from the non-reducing end of XOS, acting as exo-deacetylases. In contrast, AXEs completely deacetylated longer neutral XOS but had difficulties with the shorter ones. Complete deacetylation of neutral XOS was obtained after the combined action of AEs and AXEs. MeGlcA substituents partially restricted the action of both types of esterases and the remaining acidic XOS were mainly substituted with one MeGlcA and one acetyl group, supposedly on the same xylopyranosyl residue. These resisting structures were degraded to great extent only after inclusion of α-glucuronidase, which acted with the esterases in a synergistic manner. When used together with xylan backbone degrading endoxylanase and β-xylosidase, both AE and AXE enhanced the hydrolysis of complex XOS equally.

AB - Mass spectrometric analysis was used to compare the roles of two acetyl esterases (AE, carbohydrate esterase family CE16) and three acetyl xylan esterases (AXE, families CE1 and CE5) in deacetylation of natural substrates, neutral (linear) and 4-O-methyl glucuronic acid (MeGlcA) substituted xylooligosaccharides (XOS). AEs were similarly restricted in their action and apparently removed in most cases only one acetyl group from the non-reducing end of XOS, acting as exo-deacetylases. In contrast, AXEs completely deacetylated longer neutral XOS but had difficulties with the shorter ones. Complete deacetylation of neutral XOS was obtained after the combined action of AEs and AXEs. MeGlcA substituents partially restricted the action of both types of esterases and the remaining acidic XOS were mainly substituted with one MeGlcA and one acetyl group, supposedly on the same xylopyranosyl residue. These resisting structures were degraded to great extent only after inclusion of α-glucuronidase, which acted with the esterases in a synergistic manner. When used together with xylan backbone degrading endoxylanase and β-xylosidase, both AE and AXE enhanced the hydrolysis of complex XOS equally.

KW - 414 Agricultural biotechnology

KW - 1182 Biochemistry, cell and molecular biology

U2 - 10.1016/j.jbiotec.2013.10.009

DO - 10.1016/j.jbiotec.2013.10.009

M3 - Article

VL - 168

SP - 684

EP - 692

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 4

ER -