Whole-cell catalytic synthesis of cadaverine by recombinant Corynebacterium glutamicum using corncob residue as carbohydrate feedstock

Industrial production of cadaverine primarily relies on whole-cell catalysis of lysine using engineered Escherichia coli as host cells. The growing interest in cadaverine as a monomer of biobased polyamides requires inexpensive, non-food carbohydrate feedstock for its bioproduction, rather than using food-derived sugars as feedstock. This study used corncob residue as the starting carbohydrate feedstock followed by enzymatic hydrolysis to obtain the sugars. Since E. coli was not tolerant to even minor inhibitor residues in corncob residue hydrolysate, the robust Corynebacterium glutamicum was used as the host bacterium followed by the metabolic modifications of secretory expression of lysine decarboxylase via Ncgl1289 and cgR_0949 , and cadaverine degradation pathway knockout. The final whole-cell catalysis of C. glutamicum recombinant using corncob hydrolysate as carbohydrate feedstock achieved a record-high 78.19   g/L of cadaverine with a conversion yield of 91%.