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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 DH5α, 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 SO2 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.

SUBMITTER: Jiang D 

PROVIDER: S-EPMC7708551 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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

Jiang Dongqi D   Li Huamin H   Sun Shuyang S  

Food science and biotechnology 20201031 12


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 <i>Lactobacillus plantarum</i> was cloned and successfully expressed in <i>Escherichia coli</i> DH5α, with the recombinant host determined as histamine-degrading active. The recombinant GAPDH was then  ...[more]

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