{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wu H"],"funding":["Scientific Research Foundation of Hunan Provincial Education Department","National Natural Science Foundation of China"],"pagination":["323-330"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10165151"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(2)"],"pubmed_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."],"journal":["Synthetic and systems biotechnology"],"pubmed_title":["Engineering the thermostability of d-lyxose isomerase from <i>Caldanaerobius polysaccharolyticus</i> via multiple computer-aided rational design for efficient synthesis of d-mannose."],"pmcid":["PMC10165151"],"funding_grant_id":["32201963","22C0137"],"pubmed_authors":["Zhang W","Ding Y","Pu M","Wen L","Yi M","Mu W","Cheng Y","Wu H","Wu X"],"additional_accession":[]},"is_claimable":false,"name":"Engineering the thermostability of d-lyxose isomerase from <i>Caldanaerobius polysaccharolyticus</i> via multiple computer-aided rational design for efficient synthesis of d-mannose.","description":"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.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-06-20T03:15:20.814Z","creation":"2025-04-05T10:55:26.257Z"},"accession":"S-EPMC10165151","cross_references":{"pubmed":["37168606"],"doi":["10.1016/j.synbio.2023.04.003"]}}