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- Title
Identification and Functional Characterization of a Fructooligosaccharides-Forming Enzyme from Aspergillus aculeatus.
- Authors
Virgen-Ortíz, José; Ibarra-Junquera, Vrani; Escalante-Minakata, Pilar; Centeno-Leija, Sara; Serrano-Posada, Hugo; Jesús Ornelas-Paz, José; Pérez-Martínez, Jaime; Osuna-Castro, Juan
- Abstract
Although fructosyltransferases from Aspergillus aculeatus have received a considerable interest for the prebiotics industry, their amino acid sequences and structural features remain unknown. This study sequenced and characterized a fructosyltransferase from A. aculeatus ( AcFT) isolated by heat treatment of Pectinex Ultra SP-L. The AcFT enzyme showed two isoforms, low-glycosylated AcFT1 and high-glycosylated AcFT2 forms, with similar optimum activity at 60 °C. The purified heat-resistant AcFT1 and AcFT2 isoforms produced identical patterns of fructooligosaccharides (FOS; kestose, nystose and fructosylnystose) with a notable transfructosylation capability (~90 % transferase/hydrolase ratio). In contrast, the pI and optimum pH values exhibited discrete differences, attributable to their glycosylation pattern. Partial protein sequencing showed that AcFT enzyme corresponds to Aspac1_37092, a putative 654-residue fructosyltransferase encoded in the genome of A. aculeatus ATCC16872. A homology model of AcFT also revealed the typical fold common to members of the glycoside hydrolase family 32 (GH32), with an N-terminal five-blade β-propeller domain enclosing catalytic residues D60, D191, and E292, linked to a C-terminal β-sandwich domain. To our knowledge, this is the first report describing the amino acid sequence and structural features of a heat-resistant FOS-forming enzyme from A. aculeatus, providing insights into its potential applications in the prebiotics industry.
- Subjects
AMINO acid sequence; FRUCTOSYLTRANSFERASES; HEAT treatment; FRUCTOOLIGOSACCHARIDES; ASPERGILLUS
- Publication
Applied Biochemistry & Biotechnology, 2016, Vol 179, Issue 3, p497
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-016-2009-8