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Exceptionally thermostable α- and β-galactosidase from Aspergillus niger separated in one step
National Technical University of Athens.
1990 (English)In: Process Biochemistry, ISSN 1359-5113, E-ISSN 1873-3298, Vol. 25, no 6, p. 210-212Article in journal (Refereed) Published
Abstract [en]

Extracellular alpha- and-beta-galactosidases from a strain of Aspergillus niger were separated and purified in one step by cation exchange chromatography. Both enzymes had acidic pH (3.5-4.0) and high temperature (65-degrees-C) optima and an exceptionally high thermostability. Thus, -alpha-galactosidase had an activity half-time of 104 min at 60-degrees-C whereas at the same temperature the respective value for-beta-galactosidase was 835 min. At optimum conditions of activity the apparent K(m) values of alpha- and beta-galactosidase were 0.44mM and 1.1mM respectively. Both the high temperature optima and thermostability properties of the enzymes make them particularly suitable for high temperature processes.

Place, publisher, year, edition, pages
1990. Vol. 25, no 6, p. 210-212
Identifiers
URN: urn:nbn:se:ltu:diva-3943Local ID: 1c9fd78e-efda-4297-82c4-3bd547e32431OAI: oai:DiVA.org:ltu-3943DiVA, id: diva2:976805
Note
Upprättat; 1990; 20130215 (ysko)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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Christakopoulos, Paul

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