In the process of synthesizing αGG, due to the long reaction time, it is usually necessary to keep the temperature at 30 ☌ (Bolivar et al. mesenteroides ATCC 12,291 ( LmSPase) was reported to have high activity to synthesize α-arbutin but poor thermostability, restricting its industrial applications (Yao et al. During the production process, SPase with a high thermostability would reduce the production time under high temperatures and remain active after prolonged continuous catalysis. Industrial carbohydrate conversion is preferably performed at a higher temperature to avoid microbial contamination (Haki and Rakshit 2003). The αGG has a beneficial function as a humectant in cosmetics and has potential as a healthy food material and therapeutic agent (Bolivar et al. For instance, SPase can be used to synthesize fine chemicals such as α-D-glucosylglycerol (αGG), which is synthesized from one molecule of sucrose and one glycerol. SPase has outstanding potential for biocatalytic conversion of ordinary table sugar into products with attractive properties (Franceus and Desmet 2020), and it is widely used in the fields of food, medicine, and cosmetics (O’Neill and Field 2015). Sucrose phosphorylase (SPase, EC 2.4.1.7) can catalyze the phosphorolysis of sucrose into α-D-glucose 1-phosphate (α-D-G1P) and D-fructose, and it can glycosylate a broad range of acceptors other than phosphate (Goedl et al. This study provides an effective strategy for improving the thermostability of an industrial enzyme. Furthermore, the two variants T219L and Mut4 were used to produce α-D-glucosylglycerol (αGG) from sucrose and glycerol by incubating with 40 U/mL crude extracts at 37 ☌ for 60 h and achieved the product concentration of 193.2 ± 12.9 g/L and 195.8 ± 13.1 g/L, respectively, which were approximately 1.3-fold higher than that of WT (150.4 ± 10.0 g/L). The half-lives at 50 ☌ of T219L and Mut4 both increased approximately two-fold compared to that of wild-type LmSPase (WT).
Finally, one single-point mutation T219L and a combination mutation I31F/T219L/T263L/S360A (Mut4) with improved thermostability were obtained. A semi-rational design strategy that combined the FireProt (a web server designing thermostable proteins), structure–function analysis, and molecular dynamic simulations was used to improve the thermostability of LmSPase. In this study, a SPase gene from Leuconostoc mesenteroides ATCC 12,291 ( LmSPase) was synthesized with optimized codons and overexpressed successfully in Escherichia coli. However, the low thermostability of SPase has been a bottleneck for its industrial application. The actual native artifact is a klib ultimately, but it's all managed with gradle and dependency metadata.Sucrose phosphorylase (SPase) can specifically catalyze transglycosylation reactions and can be used to enzymatically synthesize α-D-glycosides. I then publish that whole thing as a multiplatform library. The cinterops sets up where the def files are and params. The native and interop config live in the multiplatform config.
I just created an example but it's not public yet, so this is the best one I have off hand: There was a separate plugin for that last year, but you definitely don't want to be using that. Konan is the name of the native platform/compiler. In Link #2 it says that platform plugin is deprecated. If you're building a klib separately, you're creating some extra steps (probably). In general, you'll want to use the multiplatform plugin.
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