Abstract
A β-amylase extracted from Ecballium elaterium was purified on Q-Sepharose anion exchange chromatography and identified with molecular mass. A successful immobilization by adsorption onto a matrix of titanium dioxide-cellulose acetate butyrate and copolymer of acrylonitrile-acrylamide yielded 32.17%. Thermal stability approved that Ecballium β-amylase retained 89.21% of its initial activity (IA) after 180 min at 70 °C. A promoted catalytic activity was revealed at 70 °C and pH 7.5 with the immobilization procedure. The heterogeneous system based on the process of the substrate conversion degree (α) was studied kinetically via the modified Prout–Tompkins topochemical equation. α increased in accordance with the temperature increase up to 100 min of the reaction time. At 30 °C only 7.6% of optimum conversion degree was lost after 3 h. Power factor (χ) was equal to 1.16. An accomplished application of Ecballium β-amylase proved that it could be a good candidate to produce maltose syrup due to the highest maltose content of 52.9% after 8 h hydrolysis. It will be also very useful during manufacturing processes to minimize starch saccharification time even enzymatic liquefaction costs.
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Lahmar, I., Velitchkova, M., Radeva, G. et al. β-Amylase Squirting Cucumber Between Immobilization, Kinetic Modeling and Application for Maltose Syrup Production. Chemistry Africa 7, 1293–1301 (2024). https://doi.org/10.1007/s42250-023-00833-x
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DOI: https://doi.org/10.1007/s42250-023-00833-x