Rhodococcus sp. may convert ethylene to acetaldehyde to slow ripening in climacteric fruit.
- Published
- Accepted
- Subject Areas
- Agricultural Science, Biochemistry, Biotechnology, Food Science and Technology, Microbiology
- Keywords
- Fruit Storage, Fruit Ripening, Ethylene, agriculture, Rhodococcus, Bacillus, Storage, Ethanol, Biofuel, guenevere
- Copyright
- © 2019 Perry
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
- Cite this article
- 2019. Rhodococcus sp. may convert ethylene to acetaldehyde to slow ripening in climacteric fruit. PeerJ Preprints 7:e3398v2 https://doi.org/10.7287/peerj.preprints.3398v2
Abstract
Pre-Print Update. Previous studies suggested Rhodococcus rhodochrous and Bacillus licheniformis cells converted ethylene to a nitrile compound to delay the effects of ripening, (Perry, G. Nov. 9, 2017). However, there may be an alternative compound that plays a more significant role in induced Rhodococcus and Bacillus ability to delay ripening. It has been known for years that Rhodococcus can convert the alkyne compound acetylene to acetaldehyde and potentially ethanol as a secondary product (DeBont, 1980).
This pre-print revisit re-examines the prior data to determine if the tri-phasic system previously discussed in 2017, induced bacteria to convert ethylene and/or propylene into acetaldehyde (a primary product), ethanol (a secondary product), and acetonitrile (a product of ethanol and a subsequent ammoxidation reaction). The acetaldehyde may delay the effects of ripening and inhibit fungal growth, while the nitrile by products enhance early plant development including germination and root elongation. Experimental results suggest an inducible monooxygenase or dioxygenase like enzyme is required to facilitate this process.
Author Comment
This pre-print re-visits my prior submission published Nov. 19, 2018. There is little additional data, the proposed pathway has been modified.