1. Enzymatic synthesis and characterization of novel lipophilic inotodiol–oleic acid conjugates.
- Author
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Nguyen, Phu Cuong, Nguyen, My Tuyen Thi, Ban, So-Young, Choi, Kyeong-Ok, Park, Ji-Hyun, Tran, Phuong Lan, Pyo, Jang-Won, Kim, Jaehan, and Park, Jong-Tae
- Subjects
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OLEIC acid , *MELTING points , *INTESTINAL diseases , *SMALL intestine , *LARGE intestine , *ESTERS - Abstract
[Display omitted] • This is the first report of successful enzymatic synthesis of inotodiol-based esters. • CALA enzyme efficiently catalyzed the esterification of inotodiol and oleic acid. • Ester bond was selectively introduced at the C3 or the C22 positions of inotodiol. • Inotodiyl-oleate (IO) monoesters had a greatly lowered melting temperature. • IOs were more stable during small intestine digestion than cholesteryl ester. In this study, we establish an efficient enzymatic approach for producing novel inotodiyl-oleates (IOs) from pure inotodiol and oleic acid to improve the properties of inotodiol. For the esterification between inotodiol and oleic acid, CALA and n -hexane were the optimal biocatalyst and solvents for forming IOs with 80.17% conversion yield. These IOs comprised two distinct monoesters, the C3 or C22 ester forms of inotodiol. Intriguingly, no diesters were detected. The IOs had a melting point of 53.48 °C, much lower than that of inotodiol (192.06 °C). The in vitro digestion rate of IOs (25–28%) was significantly (p < 0.05) lower than that of cholesteryl-oleate (60%). Additionally, IOs exhibited much lower in vivo absorption than inotodiol when orally administered using different formulations (p < 0.05). The results indicated that IOs were resistant to enzymatic digestion in the small intestine, which could be advantageous in targeting the large intestine for disease treatments. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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