Immobilization of glyceraldehyde-3-phosphate dehydrogenase on Fe3O4 magnetic nanoparticles and its application in histamine removal.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactobacillus plantarum is a novel biocatalyst in the degradation of histamine, but its properties need enhancement before practical application. Herein, we used Fe3O4 magnetic nanoparticles (MNPs) as the carrier core to prepare immobilized GAPDH. GAPDH was cloned, expressed in E. coli and purified, followed by immobilization on Fe3O4 MNPs and characterization by TEM and FT-IR. Then, characteristic comparisons between immobilized enzyme and its free form showed that the optimal pH and temperature of the former shifted to 7.5 and 40 °C, respectively, and pH tolerance and thermostability were separately broadened to 4.5-8.5 and 50-60 °C. In a wine-making experiment, including grape and black raspberry wines, using the immobilized enzyme, the results showed that over 81 %, 75 % and 59 % of histamine was removed after each treatment. These findings demonstrate that immobilizing GAPDH onto Fe3O4 MNPs is facile and efficient for histamine removal in fermented beverages.