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.

当形成具有较长链的 FOS 时，果糖基转移酶 (FTase) 催化果糖基团转移到蔗糖分子或低聚果糖 (FOS)。使用固态发酵 (SSF) 并使用龙舌兰汁液作为底物，利用两种曲霉属及其混合物生产 FTase 。米曲霉的最大 FTase 活性 (1.59 U/mL)在 24 小时后获得，温度为 30 °C，接种量为 2 × 10 ⁷孢子/mL。编码果糖基转移酶的核苷酸序列显示为 1494 bp，编码 498 个氨基酸的蛋白质。米曲霉的假设分子三级结构BM-DIA FTase 显示结构域的存在，例如 GH（糖苷水解酶）和 C 末端特征的五叶 β 螺旋桨域，其形成了一个 β 夹心模块。本研究有助于了解米曲霉BM-DIA 在 SSF 生物工艺条件下用于果糖基转移酶的工业生产的稳定性、相容性和遗传表达。