Published July 7, 2021 | Version 1

Three‐level hybrid modeling for systematic optimization of biocatalytic synthesis: α‐glucosyl glycerol production by enzymatic trans‐glycosylation from sucrose

  • 1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Graz, Austria
  • 2. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Graz, Austria; Austrian Centre of Industrial Biotechnology (ACIB), Graz, Austria

Description

We provide here the underlying data of the publication "Three‐level hybrid modeling for systematic optimization of biocatalytic synthesis: α‐glucosyl glycerol production by enzymatic trans‐glycosylation from sucrose". Please find the abstract below.

Mechanism-based kinetic models are rigorous tools to analyze enzymatic reactions, but their extension to actual conditions of the biocatalytic synthesis can be difficult. Here, we demonstrate (mechanistic-empirical) hybrid modeling for systematic optimization of the sucrose phosphorylase-catalyzed glycosylation of glycerol from sucrose, to synthesize the cosmetic ingredient α-glucosyl glycerol (GG). The empirical model part was developed to capture nonspecific effects of high sucrose concentrations (up to 1.5 M) on microscopic steps of the enzymatic trans-glycosylation mechanism. Based on verified predictions of the enzyme performance under initial rate conditions (Level 1), the hybrid model was expanded by microscopic terms of the reverse reaction to account for the full-time course of GG synthesis (Level 2). Lastly (Level 3), the application of the hybrid model for comprehensive window-of-operation analysis and constrained optimization of the GG production (~250 g/L) was demonstrated. Using two candidate sucrose phosphorylases (from Leuconostoc mesenteroides and Bifidobacterium adolescentis), we reveal the hybrid model as a powerful tool of “process decision making” to guide rational selection of the best-suited enzyme catalyst. Our study exemplifies a closing of the gap between enzyme kinetic models considered for mechanistic research and applicable in technologically relevant reaction conditions; and it highlights the important benefit thus realizable for biocatalytic process development.

Files

Files (868.5 kB)

Name Size
md5:de5ea27f5e20bd61fce06714acb13ae6
25.1 kB Download
md5:6f2405ced7d652d3135a8f93aa8491cf
28.2 kB Download
md5:d28109a5a22f17357ea1c9a56b96bd98
27.6 kB Download
md5:018c9ee98a2d3a80a039a01376ec8f86
245.3 kB Download
md5:64e29faa31cdd3d1db4a8d30d4c12da4
270.2 kB Download
md5:0e6b124ae5ac8e6ff466edfd1d72d23a
169.0 kB Download
md5:1ed49eef7d93b13e2daa5985b890f8d6
103.1 kB Download

Additional details

Related works

Is cited by
Journal article: 10.1002/bit.27878 (DOI)

Funding

European Commission
CARBAFIN - Carbohydrate-based fine chemicals: Development of a glycosylation platform cell factory and optimization of downstream processing for the sustainable production of glycosides. 761030