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Dongqi Jiang,Huamin Li,Shuyang Sun 한국식품과학회 2020 Food Science and Biotechnology Vol.29 No.12
The search for enzymes with histamine-degradingactivity is of great interest, since it has great potential inthe way of solving the problem of high histamine levels infood. In this study, the gene of a novel histamine-degradingenzyme, i.e., glyceraldehyde-3-phosphate dehydrogenase(GAPDH) from Lactobacillus plantarum was cloned andsuccessfully expressed in Escherichia coli DH5a, with therecombinant host determined as histamine-degradingactive. The recombinant GAPDH was then purified tohomogeneity by ammonium sulfate fraction and gel filtration. The optimum pH and temperature were 5.5 and 40 Cand it was strongly resistant to SO2 and ethanol. Afterwards,the histamine degradative activity of partiallypurified GAPDH in actual wine environments (grape andcherry wines) was examined by incubating the enzymes inthe middle, near the end and completion of malolacticfermentation, and histamine in the correspondingcontaminated wines was decreased by 36.8–52.4%,59.6–66.9% and 83.1–85.5%, respectively.