Purification and characterization of three alfa-arabinosidases from Aspergillus terreus

Elina Luonteri (Corresponding Author), Matti Siika-aho, Maija Tenkanen, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

31 Citations (Scopus)

Abstract

Three α-arabinosidases were purified from a culture filtrate of Aspergillus terreus VTT-D-82209 grown on sugar beet extraction waste as carbon source. The isoelectric points were 7.5, 8.3 and 8.5, and the molecular masses as determined by SDS-PAGE were 39, 59 and 59 kDa, respectively. The optimum pH was 3.5–4.5 for all three α-arabinosidases. The pI 8.5 enzyme was more stable at higher pH and temperature than the other two. All three α-arabinosidases were able to hydrolyze p-nitrophenyl-a-L-arabinofuranoside, oat spelt arabinoglucuronoxylan, rye flour arabinoxylan and rye flour.
About 80% of the total arabinose of arabinoglucuronoxylan isolated from softwood kraft pulp was hydrolyzed with all three enzymes, but the hydrolysis yield of arabinose from arabinoglucuronoxylan isolated from bleached pulp was low.
The amount of arabinose released did not significantly increase in simultaneous hydrolysis with xylanase.
Original languageEnglish
Pages (from-to)279-291
JournalJournal of Biotechnology
Volume38
Issue number3
DOIs
Publication statusPublished - 1995
MoE publication typeA1 Journal article-refereed

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Arabinose
Aspergillus
Purification
Hydrolysis
Enzymes
Flour
Sugar beets
Bleached pulp
Kraft pulp
Softwoods
Molecular mass
Beta vulgaris
Isoelectric Point
Carbon
Polyacrylamide Gel Electrophoresis
Temperature
alpha-N-arabinofuranosidase
Secale

Cite this

Luonteri, Elina ; Siika-aho, Matti ; Tenkanen, Maija ; Viikari, Liisa. / Purification and characterization of three alfa-arabinosidases from Aspergillus terreus. In: Journal of Biotechnology. 1995 ; Vol. 38, No. 3. pp. 279-291.
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abstract = "Three α-arabinosidases were purified from a culture filtrate of Aspergillus terreus VTT-D-82209 grown on sugar beet extraction waste as carbon source. The isoelectric points were 7.5, 8.3 and 8.5, and the molecular masses as determined by SDS-PAGE were 39, 59 and 59 kDa, respectively. The optimum pH was 3.5–4.5 for all three α-arabinosidases. The pI 8.5 enzyme was more stable at higher pH and temperature than the other two. All three α-arabinosidases were able to hydrolyze p-nitrophenyl-a-L-arabinofuranoside, oat spelt arabinoglucuronoxylan, rye flour arabinoxylan and rye flour. About 80{\%} of the total arabinose of arabinoglucuronoxylan isolated from softwood kraft pulp was hydrolyzed with all three enzymes, but the hydrolysis yield of arabinose from arabinoglucuronoxylan isolated from bleached pulp was low. The amount of arabinose released did not significantly increase in simultaneous hydrolysis with xylanase.",
author = "Elina Luonteri and Matti Siika-aho and Maija Tenkanen and Liisa Viikari",
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Purification and characterization of three alfa-arabinosidases from Aspergillus terreus. / Luonteri, Elina (Corresponding Author); Siika-aho, Matti; Tenkanen, Maija; Viikari, Liisa.

In: Journal of Biotechnology, Vol. 38, No. 3, 1995, p. 279-291.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Purification and characterization of three alfa-arabinosidases from Aspergillus terreus

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AU - Siika-aho, Matti

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AU - Viikari, Liisa

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AB - Three α-arabinosidases were purified from a culture filtrate of Aspergillus terreus VTT-D-82209 grown on sugar beet extraction waste as carbon source. The isoelectric points were 7.5, 8.3 and 8.5, and the molecular masses as determined by SDS-PAGE were 39, 59 and 59 kDa, respectively. The optimum pH was 3.5–4.5 for all three α-arabinosidases. The pI 8.5 enzyme was more stable at higher pH and temperature than the other two. All three α-arabinosidases were able to hydrolyze p-nitrophenyl-a-L-arabinofuranoside, oat spelt arabinoglucuronoxylan, rye flour arabinoxylan and rye flour. About 80% of the total arabinose of arabinoglucuronoxylan isolated from softwood kraft pulp was hydrolyzed with all three enzymes, but the hydrolysis yield of arabinose from arabinoglucuronoxylan isolated from bleached pulp was low. The amount of arabinose released did not significantly increase in simultaneous hydrolysis with xylanase.

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