Post-graduation Program in Food Science and Technology, University of Passo Fundo (UPF), Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, Rio Grande do Sul, Brazil.
Food Engineering Course, University of Passo Fundo (UPF), Passo Fundo, RS 99052-900, Brazil.
Int J Biol Macromol. 2020 Dec 15;165(Pt A):1002-1009. doi: 10.1016/j.ijbiomac.2020.09.220. Epub 2020 Oct 1.
The aim of this study was to carry out the co-immobilization of α-amylase and glucoamylase in crosslinked gelatin porous supports. For this, two methods of co-immobilization were proposed based on the crosslinking with glutaraldehyde (Ggta) or CaCl in presence of alginate (Gcal). The supports characterization revealed a porous microstructure with good interaction between its components according to the FTIR analysis and thermal properties. Optimal pH and temperature of the Gcal co-immobilized enzymes were determined at 60 °C and pH 6.0, present an enzymatic activity of 120 μmol·mL·min. Moreover, both supports were reused for up to 8 hydrolysis cycles. In addition, co-immobilized enzymes were more efficient than free enzymes in starch saccharification of starch in the long term. These results reveal that the co-immobilization of amylases in gelatinous supports is a promising approach in enzymatic chain reactions.
本研究旨在将α-淀粉酶和糖化酶共同固定在交联明胶多孔载体中。为此，提出了两种共固定化方法，分别基于戊二醛（Ggta）或海藻酸钠（Gcal）存在下的交联。根据 FTIR 分析和热性能，载体的特性表明其具有多孔微结构和良好的组分相互作用。确定了 Gcal 共固定化酶的最佳 pH 值和温度为 60°C 和 pH 6.0，酶活性为 120μmol·mL·min。此外，两种载体在多达 8 次水解循环中都可以重复使用。此外，共固定化酶在淀粉的长期糖化中比游离酶更有效。这些结果表明，在明胶载体中固定化淀粉酶是酶级联反应中很有前途的方法。
