Valorization of Soy Lecithin by Enzyme Cascade Reactions Including a Phospholipase A2, a Fatty Acid Double-Bond Hydratase, and/or a Photoactivated Decarboxylase

Hyo Ran Lee, Seung Yeon Kwon, Su Ah Choi, Jeong Hoo Lee, Hye Seong Lee, Jin Byung Park

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

A huge amount of phospholipids or lecithin is produced as a byproduct in the vegetable oil industry. However, most are just used as a feed additive. This study has focused on enzymatic valorization of lecithin. This was exploited by enzymatic transformation of soy lecithin into lysolecithin liposomes, including functional free fatty acids, hydroxy fatty acids, hydrocarbons, or secondary fatty alcohols. One of the representative examples was the preparation of lysolecithin liposomes containing secondary fatty alcohols [e.g., 9-Hydroxyheptadec-11-ene (9) and 9-heptadecanol (10)] by using a phospholipase A2 from Streptomyces violaceoruber, a fatty acid double-bond hydratase from Stenotrophomonas maltophilia, and a photoactivated decarboxylase from Chlorella variabilis NC64A. The engineered liposomes turned out to range ca. 144 nm in diameter by dynamic light scattering analysis. Thereby, this study will contribute to application of functional fatty acids and their derivatives as well as valorization of lecithin for the food and cosmetic industries.

Original languageEnglish
JournalJournal of Agricultural and Food Chemistry
DOIs
StatePublished - 7 Sep 2022

Bibliographical note

Funding Information:
This work was supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MEST) [grant number 2020R1A2B5B03002376]. This research was supported by the Korea Institute of Marine Science & Technology Promotion (KIMST) funded by the Ministry of Oceans and Fisheries (no. D11013214H480000100).

Publisher Copyright:
© 2022 American Chemical Society.

Keywords

  • fatty acid double-bond hydratase
  • lecithin
  • liposome
  • lysolecithin
  • phospholipase A2
  • photoactivated decarboxylase

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