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.
- Klíčová slova
- Agave sap, Amino acids, Fructooligosaccharides, Nucleotide sequencing,
- MeSH
- Aspergillus oryzae * enzymologie genetika MeSH
- fermentace * MeSH
- hexosyltransferasy * biosyntéza chemie MeSH
- nukleotidy chemie MeSH
- proteiny chemie MeSH
- průmyslová mikrobiologie * metody MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- hexosyltransferasy * MeSH
- inulosucrase MeSH Prohlížeč
- nukleotidy MeSH
- proteiny MeSH
