An acetylglucomannan esterase of Aspergillus oryzae

Purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan

Maija Tenkanen (Corresponding Author), Jeff Thornton, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

32 Citations (Scopus)

Abstract

An acetyl glucomannan esterase (AGME) was purified to eiectrophoretic homogeneity from the culture supernatant of Aspergillus oryzae. This new enzyme had a molecular mass of 36 kDa and an isoelectric point of 4.6. It was most active in the pH range 5.0–5.5 and was stable for 24 h at 40 °C at pH 5.0–6.0. The purified esterase liberated acetic acid from O-acetyl-galactoglucomannan, O-acetyl-4-O-methylglucuronoxylan and α-naphtyl acetate. The specific activity was 10-times higher for acetylated mannan than for acetylated xylan. The enzyme was able to act on polymeric substrate but activity was clearly enhanced by addition of mannanase from Trichoderma reesei and α-galactosidase from guar seeds. Presence of mannanase also increased the liberation of acetic acid in long-term hydrolysis (24 h), while the addition of α-galactosidase had no effect. No significant synergism between these two glycanases and the previously characterized esterase of A. oryzae (FE), which is also able to deacetylate galactoglucomannan, was observed. Even though the AGME had 8-times higher specific galactomannan deacetylating activity than the FE, the maximum amount of acetic acid liberated from the polymeric galactoglucomannan by AGME was only 80% of that of FE. Both esterases clearly enhanced the action of mannanase and α-galactosidase in the degradation of O-acetyl-galactoglucomannan isolated from Norway spruce.
Original languageEnglish
Pages (from-to)197-206
JournalJournal of Biotechnology
Volume42
Issue number3
DOIs
Publication statusPublished - 1995
MoE publication typeA1 Journal article-refereed

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Aspergillus oryzae
Aspergillus
Esterases
Purification
Galactosidases
Hydrolysis
Acetic Acid
Acetic acid
Cyamopsis
Mannans
Enzymes
Xylans
Carboxylesterase
Trichoderma
Isoelectric Point
Norway
Molecular mass
Seeds
Acetates
Seed

Cite this

@article{a3e2295fc1484e07b8dbf0e1b03bec5d,
title = "An acetylglucomannan esterase of Aspergillus oryzae: Purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan",
abstract = "An acetyl glucomannan esterase (AGME) was purified to eiectrophoretic homogeneity from the culture supernatant of Aspergillus oryzae. This new enzyme had a molecular mass of 36 kDa and an isoelectric point of 4.6. It was most active in the pH range 5.0–5.5 and was stable for 24 h at 40 °C at pH 5.0–6.0. The purified esterase liberated acetic acid from O-acetyl-galactoglucomannan, O-acetyl-4-O-methylglucuronoxylan and α-naphtyl acetate. The specific activity was 10-times higher for acetylated mannan than for acetylated xylan. The enzyme was able to act on polymeric substrate but activity was clearly enhanced by addition of mannanase from Trichoderma reesei and α-galactosidase from guar seeds. Presence of mannanase also increased the liberation of acetic acid in long-term hydrolysis (24 h), while the addition of α-galactosidase had no effect. No significant synergism between these two glycanases and the previously characterized esterase of A. oryzae (FE), which is also able to deacetylate galactoglucomannan, was observed. Even though the AGME had 8-times higher specific galactomannan deacetylating activity than the FE, the maximum amount of acetic acid liberated from the polymeric galactoglucomannan by AGME was only 80{\%} of that of FE. Both esterases clearly enhanced the action of mannanase and α-galactosidase in the degradation of O-acetyl-galactoglucomannan isolated from Norway spruce.",
author = "Maija Tenkanen and Jeff Thornton and Liisa Viikari",
note = "Project code: BEL4103",
year = "1995",
doi = "10.1016/0168-1656(95)00080-A",
language = "English",
volume = "42",
pages = "197--206",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "3",

}

An acetylglucomannan esterase of Aspergillus oryzae : Purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan. / Tenkanen, Maija (Corresponding Author); Thornton, Jeff; Viikari, Liisa.

In: Journal of Biotechnology, Vol. 42, No. 3, 1995, p. 197-206.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - An acetylglucomannan esterase of Aspergillus oryzae

T2 - Purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan

AU - Tenkanen, Maija

AU - Thornton, Jeff

AU - Viikari, Liisa

N1 - Project code: BEL4103

PY - 1995

Y1 - 1995

N2 - An acetyl glucomannan esterase (AGME) was purified to eiectrophoretic homogeneity from the culture supernatant of Aspergillus oryzae. This new enzyme had a molecular mass of 36 kDa and an isoelectric point of 4.6. It was most active in the pH range 5.0–5.5 and was stable for 24 h at 40 °C at pH 5.0–6.0. The purified esterase liberated acetic acid from O-acetyl-galactoglucomannan, O-acetyl-4-O-methylglucuronoxylan and α-naphtyl acetate. The specific activity was 10-times higher for acetylated mannan than for acetylated xylan. The enzyme was able to act on polymeric substrate but activity was clearly enhanced by addition of mannanase from Trichoderma reesei and α-galactosidase from guar seeds. Presence of mannanase also increased the liberation of acetic acid in long-term hydrolysis (24 h), while the addition of α-galactosidase had no effect. No significant synergism between these two glycanases and the previously characterized esterase of A. oryzae (FE), which is also able to deacetylate galactoglucomannan, was observed. Even though the AGME had 8-times higher specific galactomannan deacetylating activity than the FE, the maximum amount of acetic acid liberated from the polymeric galactoglucomannan by AGME was only 80% of that of FE. Both esterases clearly enhanced the action of mannanase and α-galactosidase in the degradation of O-acetyl-galactoglucomannan isolated from Norway spruce.

AB - An acetyl glucomannan esterase (AGME) was purified to eiectrophoretic homogeneity from the culture supernatant of Aspergillus oryzae. This new enzyme had a molecular mass of 36 kDa and an isoelectric point of 4.6. It was most active in the pH range 5.0–5.5 and was stable for 24 h at 40 °C at pH 5.0–6.0. The purified esterase liberated acetic acid from O-acetyl-galactoglucomannan, O-acetyl-4-O-methylglucuronoxylan and α-naphtyl acetate. The specific activity was 10-times higher for acetylated mannan than for acetylated xylan. The enzyme was able to act on polymeric substrate but activity was clearly enhanced by addition of mannanase from Trichoderma reesei and α-galactosidase from guar seeds. Presence of mannanase also increased the liberation of acetic acid in long-term hydrolysis (24 h), while the addition of α-galactosidase had no effect. No significant synergism between these two glycanases and the previously characterized esterase of A. oryzae (FE), which is also able to deacetylate galactoglucomannan, was observed. Even though the AGME had 8-times higher specific galactomannan deacetylating activity than the FE, the maximum amount of acetic acid liberated from the polymeric galactoglucomannan by AGME was only 80% of that of FE. Both esterases clearly enhanced the action of mannanase and α-galactosidase in the degradation of O-acetyl-galactoglucomannan isolated from Norway spruce.

U2 - 10.1016/0168-1656(95)00080-A

DO - 10.1016/0168-1656(95)00080-A

M3 - Article

VL - 42

SP - 197

EP - 206

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 3

ER -