Immobilization of Lecitase & REG; Ultra for production of flaxseed oil-based diacylglycerols by glycerolysis and its operational stability

Lecitase & REG; Ultra (LU) was immobilized by adsorption on a macroporous resin and characterized. Meanwhile, the obtained immobilized lipase LXTE-1000-LU was applied in diacylglycerol (DAG) preparation, and the glycerolysis catalytic stability was also investigated. At pH 7.0, resin amount 2.5 g, and adsorption time of 2 h, an immobilization efficiency (IE) of 89.98% could be achieved. The storage stability was promoted after immobilization, in which the lipase activity reached more than 85% after 60 days of storage at 4 degrees C and 25 degrees C individually compared to its initial state. Furthermore, 41.31% of flaxseed oil-based DAG was obtained after the glycerolysis reaction using LXTE-1000-LU as the catalyst. Under prolonged reaction, the lipase protein content decreased from 17.91 mg/g to 6.99 mg/g, and significant changes in the secondary confirmation of the protein were also observed, leading to the catalytic activity being reduced.

Automated summary

Lecitase & REG; Ultra (LU) was immobilized on a macroporous resin by adsorption and characterized. The obtained immobilized lipase LXTE-1000-LU was used in the preparation of diacylglycerol (DAG), and the catalytic stability during glycerolysis was investigated. An immobilization efficiency (IE) of 89.98% was achieved at pH 7.0, with a resin amount of 2.5 g and an adsorption time of 2 h. After storage for 60 days at 4 degrees C and 25 degrees C, the lipase activity remained over 85% compared to the initial state. Furthermore, the glycerolysis reaction using LXTE-1000-LU as the catalyst yielded 41.31% flaxseed oil-based DAG. However, prolonged reaction led to a decrease in lipase protein content and changes in the protein's secondary confirmation, resulting in reduced catalytic activity.