期刊
FOOD CHEMISTRY
卷 365, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.130454
关键词
Polyphenol oxidase; Purification; Characterization; Mass spectrometry; Potato (Solanum tuberosum)
资金
- Danish Innovation Foundation
- Danish Council for Independent Research
- Novo Nordic Foundation
This study identified multiple PPOs in potatoes, with two major ones showing stability at pH 5 and different optimal temperatures. It was found that reducing agents effectively inhibited oxidase activity, while chelators did not have the same effect.
Potato is widely consumed across the globe. Understanding and inhibiting the oxidation caused by polyphenol oxidase (PPO) could improve shelf life and increase the nutritional and economic value of potato proteins. This study aimed to identify and quantify all expressed PPOs in potato tuber (Solanum tuberosum) and to purify and characterize the major PPOs responsible for oxidase activity. Four different PPOs were expressed in potato tuber, with 2 PPOs constituting the majority. These 2 PPOs were copurified and characterized. Both potato juice and the purified PPOs had an optimum pH of 5 and were stable over a broad pH range (6-11). The optimum temperature and stability varied, with potato juice having an optimum at 30 degrees C and showing a gradual decline in oxidase activity with increasing incubation temperature, while the purified PPOs had an optimum temperature and were stable up to 40 degrees C. Reducing agents effectively inhibited oxidase activity, while chelators did not.
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