Zhao_2026_Bioresour.Technol_458_135114

Patatin, a multifunctional protein derived from potato, exhibits outstanding physicochemical properties, high nutritional quality, and diverse biological activities, positioning it as a promising candidate for applications in food ingredients, biomaterials, and industrial enzyme preparations. However, the commercial production of patatin is constrained by the inefficiency and time-consuming nature of traditional extraction methods. Herein, we employed consensus sequence engineering to design a novel potato patatin variant, designated ConPatatin. This protein was expressed efficiently and stably, achieving a yield of up to 200 mg/L, approximately five times that of other recombinant patatins. Notably, recombinant ConPatatin adopted a fully folded conformation, conferring high solubility as well as excellent structural and enzymatic stability. Moreover, it exhibited significantly enhanced antioxidant and esterase hydrolytic activities compared with naturally extracted or other recombinant patatins, underscoring its potential for practical applications. Mechanistic investigation revealed that Gln289 is critical for achieving high-level soluble expression of ConPatatin, likely due to its role in preventing the formation of unfavorable salt bridges. Collectively, this work not only offers a promising strategy for the sustainable industrial production of patatin but also provides a valuable reference for the rational design of other proteins.