Fructosyltransferase production by Aspergillus oryzae BM-DIA using solid-state fermentation and the properties of its
Mariela R Michel1, Adriana C Flores- Gallegos1, Sandra L Villarreal-Morales1
1Department of Food Research, School of Chemistry, Autonomous University of Coahuila, Blvd. V. Carranza e Ing, José Cárdenas S/N. República Oriente, 25280, Saltillo, Coahuila, Mexico.
Abstract:
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.
