Enzymatic deacetylation of galactoglucomannans

Maija Tenkanen, Jurgen Puls, Marjaana Rättö, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

37 Citations (Scopus)

Abstract

Several hemicellulolytic microorganisms were screened for their capability of liberating acetyl side groups from native softwood galactoglucomannan. All the microorganisms tested were found to produce an extracellular acetyl glucomannan esterase(s). The highest activity was detected in Schizophyllum commune culture filtrate. However, the enzyme produced by Aspergillus oryzae was most efficient in long-term hydrolysis. Acting alone, the purified esterase of A. oryzae was able to liberate most of the acetic acid from galactoglucomannan. The addition of other galactoglucomannan-degrading enzymes did not affect the action of esterase. On the other hand, the addition of esterase clearly enhanced the action of mannanase and α-galactosidase. The purified acetyl esterase of Trichoderma reesei was able to liberate acetic acid from short oligomers of glucomannan, whereas the acetyl xylan esterase of T. reesei was unable to act on glucomannan oligomers of any size.

Original languageEnglish
Pages (from-to)159 - 165
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume39
Issue number2
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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Esterases
Aspergillus oryzae
acetylxylan esterase
Acetic Acid
Schizophyllum
Galactosidases
Trichoderma
Enzymes
Hydrolysis
(1-6)-alpha-glucomannan
galactoglucomannan

Cite this

Tenkanen, M., Puls, J., Rättö, M., & Viikari, L. (1993). Enzymatic deacetylation of galactoglucomannans. Applied Microbiology and Biotechnology, 39(2), 159 - 165. https://doi.org/10.1007/BF00228600
Tenkanen, Maija ; Puls, Jurgen ; Rättö, Marjaana ; Viikari, Liisa. / Enzymatic deacetylation of galactoglucomannans. In: Applied Microbiology and Biotechnology. 1993 ; Vol. 39, No. 2. pp. 159 - 165.
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abstract = "Several hemicellulolytic microorganisms were screened for their capability of liberating acetyl side groups from native softwood galactoglucomannan. All the microorganisms tested were found to produce an extracellular acetyl glucomannan esterase(s). The highest activity was detected in Schizophyllum commune culture filtrate. However, the enzyme produced by Aspergillus oryzae was most efficient in long-term hydrolysis. Acting alone, the purified esterase of A. oryzae was able to liberate most of the acetic acid from galactoglucomannan. The addition of other galactoglucomannan-degrading enzymes did not affect the action of esterase. On the other hand, the addition of esterase clearly enhanced the action of mannanase and α-galactosidase. The purified acetyl esterase of Trichoderma reesei was able to liberate acetic acid from short oligomers of glucomannan, whereas the acetyl xylan esterase of T. reesei was unable to act on glucomannan oligomers of any size.",
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Tenkanen, M, Puls, J, Rättö, M & Viikari, L 1993, 'Enzymatic deacetylation of galactoglucomannans', Applied Microbiology and Biotechnology, vol. 39, no. 2, pp. 159 - 165. https://doi.org/10.1007/BF00228600

Enzymatic deacetylation of galactoglucomannans. / Tenkanen, Maija; Puls, Jurgen; Rättö, Marjaana; Viikari, Liisa.

In: Applied Microbiology and Biotechnology, Vol. 39, No. 2, 1993, p. 159 - 165.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Tenkanen, Maija

AU - Puls, Jurgen

AU - Rättö, Marjaana

AU - Viikari, Liisa

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AB - Several hemicellulolytic microorganisms were screened for their capability of liberating acetyl side groups from native softwood galactoglucomannan. All the microorganisms tested were found to produce an extracellular acetyl glucomannan esterase(s). The highest activity was detected in Schizophyllum commune culture filtrate. However, the enzyme produced by Aspergillus oryzae was most efficient in long-term hydrolysis. Acting alone, the purified esterase of A. oryzae was able to liberate most of the acetic acid from galactoglucomannan. The addition of other galactoglucomannan-degrading enzymes did not affect the action of esterase. On the other hand, the addition of esterase clearly enhanced the action of mannanase and α-galactosidase. The purified acetyl esterase of Trichoderma reesei was able to liberate acetic acid from short oligomers of glucomannan, whereas the acetyl xylan esterase of T. reesei was unable to act on glucomannan oligomers of any size.

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