Journal
FRONTIERS IN CHEMISTRY
Volume 6, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fchem.2018.00354
Keywords
browning-related protein (BRP); polyphenol oxidase (PPO); purification; melon; structural characterization
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Funding
- Hubei Province Technical Innovation Special Major Project [CXZD2017000255]
- Fundamental Research Funds for the Central Universities [2662018JC018]
- National Natural Science Foundation of China [31401507]
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Polyphenol oxidase (PPO) in plants plays an important role in browning reactions andmay affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (K-m = 0.04278M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the alpha-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system.
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