Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase
(1998) In Journal of Biotechnology 63(3). p.199-210- Abstract
- The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with... (More)
- The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with Aspergillus aculeatus β-mannanase indicated high identity. The enzyme most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/125459
- author
- Ademark, Pia ; Varga, Arthur LU ; Medve, József ; Harjunpää, Vesa ; Drakenberg, Torbjörn LU ; Tjerneld, Folke LU and Stålbrand, Henrik LU
- organization
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Hemicellulase, α-Galactosidase, Aspergillus niger, β-Mannanase
- in
- Journal of Biotechnology
- volume
- 63
- issue
- 3
- pages
- 199 - 210
- publisher
- Elsevier
- external identifiers
-
- scopus:0345389971
- ISSN
- 1873-4863
- DOI
- 10.1016/S0168-1656(98)00086-8
- language
- English
- LU publication?
- yes
- id
- 2fcd7179-8bb2-4398-bc3a-15533111a0c6 (old id 125459)
- date added to LUP
- 2016-04-01 11:59:10
- date last changed
- 2022-01-26 21:11:40
@article{2fcd7179-8bb2-4398-bc3a-15533111a0c6, abstract = {{The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with Aspergillus aculeatus β-mannanase indicated high identity. The enzyme most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose.}}, author = {{Ademark, Pia and Varga, Arthur and Medve, József and Harjunpää, Vesa and Drakenberg, Torbjörn and Tjerneld, Folke and Stålbrand, Henrik}}, issn = {{1873-4863}}, keywords = {{Hemicellulase; α-Galactosidase; Aspergillus niger; β-Mannanase}}, language = {{eng}}, number = {{3}}, pages = {{199--210}}, publisher = {{Elsevier}}, series = {{Journal of Biotechnology}}, title = {{Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase}}, url = {{http://dx.doi.org/10.1016/S0168-1656(98)00086-8}}, doi = {{10.1016/S0168-1656(98)00086-8}}, volume = {{63}}, year = {{1998}}, }