Wei Lu

TL;DR: In this article, a semi-rational design based on site-directed saturation mutagenesis and surface charge modification was used to improve the catalytic efficiency of the diacetylchitobiose deacetylase derived from Pyrococcus horikoshii (PhDac).

TL;DR: In this paper, a construction and application of an engineering bacteria secreting and expressing chitosan deacetylase, belonging to the technical field of fermentation engineering, is described.

TL;DR: In this paper, a signal peptide fragment yncM is added into the recombinant vector for the first time, and the peptide can secrete the target protein diacetylchitobiose deacetylase outside the cells of recombinant B. subtilis, and a mutant of the 5′-end untranslated region is acquired, thereby significantly increasing the expression level of the target proteins, and greatly simplifying the subsequent enzyme separation and purification steps.

TL;DR: This work aimed to achieve high-level secretory production of diacetylchitobiose deacetylase by Bacillus subtilis and perform molecular engineering to improve catalytic performance, and this provides a good foundation for the application of di acetyl chitosan oligosaccharides and monosACcharides.