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

Lecitase® 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 ads...

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Bibliographic Details
Published in:Food science & technology 2023-06, Vol.183, p.114964, Article 114964
Main Authors: Sun, Xiaoxue, Zou, Shuo, Xie, Xiaodong, Wang, Yong, Zhang, Zhen
Format: Article
Language:English
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Summary:Lecitase® 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 °C and 25 °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. •Lecitase® Ultra was immobilized on a macroporous resin using an efficiency adsorption method.•Immobilized lipase showed a decent environmental and storage stability.•Immobilized lipase can be catalyzed in glycerolysis for diacylglycerols production.•Immobilized lipase catalytic activity reduced as verified by the protein's leaking and conformational change.
ISSN:0023-6438
1096-1127
DOI:10.1016/j.lwt.2023.114964