Exo-inulinase of Aspergillus niger N402: A hydrolytic enzyme with significant transfructosylating activity

The purified exo-inulinase enzyme of Aspergillus niger N402 (AngInuE; heterologously expressed in Escherichia coli) displayed a sucrose:inulin (S/I) hydrolysis ratio of 2.3, characteristic for a typical exo-inulinase. The enzyme also had significant transfructosylating activity with increasing sucro...

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Bibliographic Details
Published inBiocatalysis and biotransformation Vol. 26; no. 1-2; pp. 49 - 58
Main Authors Goosen, C., Van Der Maarel, M. J. E. C., Dijkhuizen, L.
Format Journal Article Conference Proceeding
LanguageEnglish
Published Abingdon Informa UK Ltd 2008
Taylor & Francis
Taylor and Francis
Subjects
Aspergillus niger
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
exo-inulinase
Fundamental and applied biological sciences. Psychology
glycoside hydrolase
hydrolysis
Methods. Procedures. Technologies
SVEVF motif
transfructosylation
Enzyme
transfructosylation
SVEVF motif
Fungi
Glycosylases
Hydrolysis
glycoside hydrolase
Aspergillus niger
Glycosidases
Inulinase
Hydrolases
Glycoside
exo-inulinase
Fungi Imperfecti
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Summary:The purified exo-inulinase enzyme of Aspergillus niger N402 (AngInuE; heterologously expressed in Escherichia coli) displayed a sucrose:inulin (S/I) hydrolysis ratio of 2.3, characteristic for a typical exo-inulinase. The enzyme also had significant transfructosylating activity with increasing sucrose concentrations, producing various oligosaccharides. The AngInuE protein molecular mass was 57 kDa, close to the calculated value for the mature protein. AngInuE thus was active as a monomeric, non-glycosylated protein. Contradictory data on hydrolysis/transfructosylation activity ratios have been published for the (almost) identical (but monomeric or dimeric and glycosylated) exo-inulinases of other aspergilli. Our data clearly show that the AngInuE enzyme, produced in and purified from E. coli, is a broad specificity exo-inulinase that also has significant transfructosylating activity with sucrose. Analysis of site-directed mutants of AngInuE showed that the glycoside hydrolase family 32 conserved domain G is important for catalytic efficiency, with a clear role in hydrolysis of both sucrose and fructans.
ISSN:1024-2422
1029-2446
DOI:10.1080/10242420701806686