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Low-temperature synthesis of di- and monoolein by enzymatic hydrolysis in a biphasic system using cutinase from <i>Fusarium graminearum</i>.


ABSTRACT: Among functional lipids, oleoylglycerols including 1,2-diolein and 2-monoolein are known for their beneficial activities such as fatty acid metabolism, insulin secretion promotion, antioxidant, and anti-arrhythmic sclerosing activity. To produce these oleoylglycerols through the lipase reaction, cutinase from Fusarium graminearum (FGC) were recombinantly expressed and the properties of the enzyme were analyzed. The enzyme exhibited optimal activity under weak alkaline conditions (pH 8-9) and low temperatures (2-10 °C) for triolein in the water-isooctane biphasic system. The product of the lipase reaction with FGC at a low temperature was analyzed by HPLC, revealing that FGC appeared as sn-1(3) regiospecific lipase and only 2-monoolein was produced in monoolein isomers with 15.7 ± 3.83% conversion at 15% hydrolysis of triolein. These results showed that the FGC can be used to produce 1,2-diolein and 2-monoolein and further suggest its potential as a versatile enzyme in lipid modification in low-temperature environments.

Supplementary information

The online version contains supplementary material available at 10.1007/s10068-025-02062-z.

SUBMITTER: Lee J 

PROVIDER: S-EPMC12894595 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature

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Low-temperature synthesis of di- and monoolein by enzymatic hydrolysis in a biphasic system using cutinase from &lt;i&gt;Fusarium graminearum&lt;/i&gt;.

Lee Juchan J   Lee Juno J   Kim Jihoon J   Chang Pahn-Shick PS  

Food science and biotechnology 20260124 3


Among functional lipids, oleoylglycerols including 1,2-diolein and 2-monoolein are known for their beneficial activities such as fatty acid metabolism, insulin secretion promotion, antioxidant, and anti-arrhythmic sclerosing activity. To produce these oleoylglycerols through the lipase reaction, cutinase from <i>Fusarium graminearum</i> (FGC) were recombinantly expressed and the properties of the enzyme were analyzed. The enzyme exhibited optimal activity under weak alkaline conditions (pH 8-9)  ...[more]

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