Induction and characterization of an unusual α-d-galactosidase from Talaromyces flavus

Simerska, Pavla, Monti, Daniela, Cechova, Ivana, Pelantova, Helena, Mackova, Martina, Bezouska, Karel, Riva, Sergio and Kren, Vladimir (2007) Induction and characterization of an unusual α-d-galactosidase from Talaromyces flavus. Journal of Biotechnology, 128 1: 61-71. doi:10.1016/j.jbiotec.2006.09.006


Author Simerska, Pavla
Monti, Daniela
Cechova, Ivana
Pelantova, Helena
Mackova, Martina
Bezouska, Karel
Riva, Sergio
Kren, Vladimir
Title Induction and characterization of an unusual α-d-galactosidase from Talaromyces flavus
Formatted title
Induction and characterization of an unusual α-d-galactosidase from Talaromyces flavus
Journal name Journal of Biotechnology   Check publisher's open access policy
ISSN 0168-1656
1873-4863
Publication date 2007-01-30
Year available 2006
Sub-type Article (original research)
DOI 10.1016/j.jbiotec.2006.09.006
Volume 128
Issue 1
Start page 61
End page 71
Total pages 11
Place of publication Amsterdam, Netherlands
Publisher Elsevier BV
Language eng
Formatted abstract
An extracellular α-d-galactosidase from Talaromyces flavus CCF 2686 with extremely broad and unusual acceptor specificity is produced exclusively in the presence of the specific inducer—6-deoxy-d-glucose (quinovose). The procedure for the preparation of this very expensive substance has been modified and optimized. Surprisingly, any of other common α-d-galactosidase inducers or substrates, e.g., d-galactose, melibiose and raffinose, did not stimulate its production. The crude α-d-galactosidase preparation was purified by anion-exchange chromatography and three isoenzymes with different substrate specificities were identified. The main isoenzyme (αGal1) was further purified by cation-exchange chromatography and fully characterized. When compared with other α-galactosidases and also with other isoenzymes produced by T. flavus, it showed a markedly different regioselectivity and also negligible hydrolytic activity towards melibiose. Moreover, it was active on polymeric substrates (locust bean gum, guar gum) and significantly inhibited by α-d-galactopyranosyl azide, d-galactose, d-xylose, melibiose, methyl α- and β-d-galactopyranoside and lactose.
Keyword α-d-Galactosidase
Talaromyces flavus
6-Deoxy-d-glucose (quinovose)
Enzyme purification
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes Available online 22 September 2006

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Wed, 28 Sep 2011, 02:41:25 EST by Dr Pavla Simerska on behalf of School of Chemistry & Molecular Biosciences