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Fructosyltransferase production by Aspergillus oryzae BM-DIA using solid-state fermentation and the properties of its nucleotide and protein sequences
MR. Michel, ACF. Gallegos, SL. Villarreal-Morales, P. Aguilar-Zárate, CN. Aguilar, M. Riutort, R. Rodríguez-Herrera
Language English Country United States
Document type Journal Article
- MeSH
- Aspergillus oryzae * enzymology genetics MeSH
- Fermentation * MeSH
- Hexosyltransferases * biosynthesis chemistry MeSH
- Nucleotides chemistry MeSH
- Proteins chemistry MeSH
- Industrial Microbiology * methods MeSH
- Publication type
- Journal Article MeSH
Fructosyltransferase (FTase) catalyzes the transfer of a fructosyl group to a sucrose molecule or a fructooligosaccharide (FOS) when a FOS with a longer chain is formed. Production of FTase by two Aspergillus species and its mixture was exploited using solid-state fermentation (SSF) and employing agave sap as substrate. The maximum FTase activity (1.59 U/mL) by Aspergillus oryzae was obtained after 24 h, using a temperature of 30 °C, with an inoculum of 2 × 107 spores/mL. The nucleotide sequence coding for the fructosyltransferase showed 1494 bp and encodes for a protein of 498 amino acids. The hypothetical molecular tertiary structure of Aspergillus oryzae BM-DIA FTase showed the presence of structural domains, such as a five-bladed beta-propeller domain characteristic of GH (glycoside hydrolase) and C terminal, which forms a beta-sandwich module. This study contributes to the knowledge of stability, compatibility, and genetic expression of Aspergillus oryzae BM-DIA under SSF bioprocess conditions for industrial production of fructosyltransferase.
References provided by Crossref.org
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