Verification of a novel glyceraldehyde-3-phosphate dehydrogenase capable of histamine degradation and its preliminary application in wine production

Abstract

The search for enzymes with histamine-degrading activity is of great interest, since it has great potential in the way of solving the problem of high histamine levels in food. In this study, the gene of a novel histamine-degrading enzyme, i.e., glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactobacillus plantarum was cloned and successfully expressed in Escherichia coli DH5a, with the recombinant host determined as histamine-degrading active. The recombinant GAPDH was then purified to homogeneity by ammonium sulfate fraction and gel filtration. The optimum pH and temperature were 5.5 and 40 °C and it was strongly resistant to SO 2 and ethanol. Afterwards, the histamine degradative activity of partially purified GAPDH in actual wine environments (grape and cherry wines) was examined by incubating the enzymes in the middle, near the end and completion of malolactic fermentation, and histamine in the corresponding contaminated wines was decreased by 36.8-52. 4%, 59.6-66.9% and 83.1-85.5%, respectively.

Malolactic Fermentation: New Approaches to Old Problems

“…Moreover, Jiang et al successfully expressed GAPDH in Escherichia coli for the first time and purified it. It was also found that recombinant GAPDH was highly resistant under both sulphate and ethanol stress, and the histamine in wine was broken down by 83.1-85.5% [67].…”