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A Purified α-galactosidase from aspergillus niger with enhanced kinetic characteristics
National Technical University of Athens.
National Technical University of Athens.
National Technical University of Athens.
1991 (English)In: Acta Biotechnologica, ISSN 0138-4988, E-ISSN 1521-3846, Vol. 11, no 5, p. 479-484Article in journal (Refereed) Published
Abstract [en]

Extracellular α-galactosidase from Aspergillus niger was purified 128-fold over the crude extract by gel filtration, ion exchange chromatography and chromatofocusing. Certain substrates and end products affected enzyme activity. Among the former p-nitrophenyl-α-galactopyranoside (PNPG) inhibited the enzyme at 1.4 mM while melibiose did not inhibit α-galactosidase at concentrations up to 50 mM. Enzymic end products such as glucose did not inhibit the enzyme at concentrations up to 100 mM while galactose exhibited a competitive inhibition with a Ki = 1.29 mM. The kinetic characteristics of the enzyme compared favourably to other microbial α-galactosidases and make it suitable for food process applications.

Place, publisher, year, edition, pages
1991. Vol. 11, no 5, p. 479-484
Identifiers
URN: urn:nbn:se:ltu:diva-9751DOI: 10.1002/abio.370110513Local ID: 86ba2f20-25b5-4fb3-81c3-1fba0d8ef2cdOAI: oai:DiVA.org:ltu-9751DiVA, id: diva2:982689
Note
Upprättat; 1991; 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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