Year: 2026
Type: article
Abstract: The production of sequence-defined partially acetylated chitooligosaccharides (paCOS) is a promising strategy for the valorization of chitin-rich waste into high-value bioactive compounds. The catalytic domain of a deacetylase from Bacillus subtilis ( Bs PdaC-CD), known to act on N-acetylglucosamine (GlcNAc) residues of chitooligosaccharides, represents a promising biocatalyst for paCOS production. In this work, a fed-batch process to produce the recombinant Bs PdaC-CD in Escherichia coli BL21 was developed and optimized using a Taguchi L9 (3 4 ) design of experiments. Across nine independent fed-batch processes, Bs PdaC-CD titters and space-time yield (STY) varied widely, ranging from 167 to 1197 mg Bs PdaC-CD/L and 2.2 to 22.5 mg Bs PdaC-CD/(L*h), respectively. Temperature and feed rate were identified as the most influential factors affecting these outcomes. In both cases, the main variability was observed at low feeding rate and temperature, 5 mL/L/h and 22 °C respectively, which showed lower Bs PdaC-CD productions. Subsequent experiments at 10 mL/L/h and 30 °C confirmed the robustness of the optimized conditions, consistently yielding 1.2 g/L of Bs PdaC-CD within 50 h. These results highlight the utility of Taguchi-based experimental design for rapid identification of critical parameters in recombinant protein bioprocess optimization.
Source: Scientific Reports
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,690
OpenAlex ID: W7162873669
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