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http://dx.doi.org/10.1038/bjc.1965.31DOI Listing

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February 2020

Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China. Electronic address:

Compared to the control longans, hydrogen peroxide (HO)-treated longans exhibited higher index of pulp breakdown, higher fruit respiration rate, higher activities of pulp phosphohexose isomerase (PGI), succinate dehydrogenase (SDH), cytochrome C oxidase (CCO), ascorbic acid oxidase (AAO) and polyphenol oxidase (PPO), but lower activity of pulp nicotinamide adenine dinucleotide kinase (NADK). HO-treated longans also exhibited lower total activities of pulp glucose-6-phosphate dehydrogenase (G-6-PDH) and 6-phosphogluconate dehydrogenase (6-PGDH), lower levels of pulp NADP(H), but higher levels of pulp NAD(H). These data indicated that HO-stimulated longan pulp breakdown was owing to a decreased proportion of pentose phosphate pathway (PPP), the increased proportions of Embden-Meyerhof-Parnas pathway (EMP), tricarboxylic acid (TCA) cycle and cytochrome pathway (CCP) in total respiratory pathways.

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Article Synopsis
  • The study examined the relationship between root respiration and the levels of biomass and glycyrrhizic acid in a specific plant, using various biochemical analyses.
  • Different respiration-related enzymes and pathways, such as glycolysis (EMP), TCA cycle, and pentose phosphate pathway, were evaluated for their roles in root respiration.
  • Results showed a strong correlation between TCA pathway and biomass, as well as insights into how metabolites like pyruvic acid and acetyl coenzyme A relate to glycyrrhizic acid production, suggesting future cultivation improvements.
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Enzymes sample multiple conformations during their catalytic cycles. Chemical shifts from Nuclear Magnetic Resonance (NMR) are hypersensitive to conformational changes and ensembles in solution. Phosphomannomutase/phosphoglucomutase (PMM/PGM) is a ubiquitous four-domain enzyme that catalyzes phosphoryl transfer across phosphohexose substrates.

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