| Title : Engineering the Thermostability of the Mono- and Diacylglycerol Lipase SMG1 for the Synthesis of Diacylglycerols - Li_2022_Foods_11_4069 |
| Author(s) : Li L , Wang Y , Cui R , Wang F , Lan D |
| Ref : Foods , 11 :4069 , 2022 |
| Abstract : Diacylglycerols (DAGs) display huge application prospectives in food industries. Therefore, new strategies to produce diacylglycerides are needed. Malassezia globose 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 degreesC increase in the melting temperature (T(m)), 5 degreesC in the optimal temperature, and 1154.3-fold in the half-life (t(1/2)) at 55 degreesC. 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. |
| ESTHER : Li_2022_Foods_11_4069 |
| PubMedSearch : Li_2022_Foods_11_4069 |
| PubMedID: 36553811 |
| Gene_locus related to this paper: malgo-a8puy1 |
| Gene_locus related to this paper: malgo-a8puy1 |
Li L, Wang Y, Cui R, Wang F, Lan D (2022)
Engineering the Thermostability of the Mono- and Diacylglycerol Lipase SMG1 for the Synthesis of Diacylglycerols
Foods
11 :4069
Li L, Wang Y, Cui R, Wang F, Lan D (2022)
Foods
11 :4069