AI Article Synopsis
- d-Mannose is a functional sugar with health benefits, and there’s a growing market for low-calorie sweeteners, but the enzyme d-lyxose isomerase (d-LIase) struggles with thermal stability, limiting its use.
- Researchers used computer-aided design tools to create mutants of d-LIase that have better thermostability, with one promising mutant (M5) demonstrating significantly enhanced stability and efficiency compared to the original enzyme.
- Molecular dynamics simulations revealed that the improved stability of mutant M5 is due to a more rigid protein structure, new hydrogen bonds, and changes in electrostatic properties, making it a potential candidate for industrial production of d-mannose from d-fructose.
Article Abstract
d-Mannose is an attractive functional sugar that exhibits many physiological benefits on human health. The demand for low-calorie sugars and sweeteners in foods are increasingly available on the market. Some sugar isomerases, such as d-lyxose isomerase (d-LIase), can achieve an isomerization reaction between d-mannose and d-fructose. However, the weak thermostability of d-LIase limits its efficient conversion from d-fructose to d-mannose. Nonetheless, few studies are available that have investigated the molecular modification of d-LIase to improve its thermal stability. In this study, computer-aided tools including FireProt, PROSS, and Consensus Finder were employed to jointly design d-LIase mutants with improved thermostability for the first time. Finally, the obtained five-point mutant M5 (N21G/E78P/V58Y/C119Y/K170P) showed high thermal stability and catalytic activity. The half-life of M5 at 65 °C was 10.22 fold, and the catalytic efficiency towards 600 g/L of d-fructose was 2.6 times to that of the wild type enzyme, respectively. Molecular dynamics simulation and intramolecular forces analysis revealed a thermostability mechanism of highly rigidity conformation, newly formed hydrogen bonds and π-cation interaction between and within protein domains, and redistributed surface electrostatic charges for the mutant M5. This research provided a promising d-LIase mutant for the industrial production of d-mannose from d-fructose.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10165151 | PMC |
| http://dx.doi.org/10.1016/j.synbio.2023.04.003 | DOI Listing |
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