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Article Abstract
Diacylglycerols (DAGs) display huge application prospectives in food industries. Therefore, new strategies to produce diacylglycerides are needed. lipase (SMG1) could be used to synthesize DAGs. However, the poor thermostability of SMG1 seriously hampers its application. Herein, a rational design was used to generate a more thermostable SMG1. Compared with the wild type (WT), the M5D mutant (Q34P/A37P/M176V/G177A/M294R/ G28C-P206C), which contains five single-point mutations and one additional disulfide bond, displayed a 14.0 °C increase in the melting temperature (), 5 °C in the optimal temperature, and 1154.3-fold in the half-life () at 55 °C. Meanwhile, the specific activity towards DAGs of the M5D variant was improved by 3.0-fold compared to the WT. Molecular dynamics (MD) simulations revealed that the M5D mutant showed an improved rigid structure. Additionally, the WT and the M5D variants were immobilized and used for the production of DAGs. Compared with the WT, the immobilized M5D-catalyzed esterification showed a 9.1% higher DAG content and a 22.9% increase in residual activity after nine consecutive cycles. This study will pave the way for the industrial application of SMG1.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9778158 | PMC |
| http://dx.doi.org/10.3390/foods11244069 | DOI Listing |
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Article Synopsis
- Researchers developed a process using an immobilized lipase to efficiently reduce the fatty acid content in high-acid rice bran oil (RBO) through esterification/transesterification with methanol.
- Molecular docking simulations showed that methanol binds more effectively to the enzyme, which may explain its superior efficiency compared to ethanol and glycerol.
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