Potato patatin is considered a valuable plant protein by the food industry for its exceptional functional properties and nutritional value. Nonetheless, it has not been widely used due to its low abundance in potatoes and high cost. Pichia pastoris was utilized for expression of patatin to overcome agricultural limitations. Biochemical and biophysical characterization of Patatin-B2 (rPatB2) and Patatin-17 (rPat17) is described. rPatB2 and rPat17 had higher zeta potential and superior solubility at various pH conditions in comparison with commercial patatin, whereas particle size distribution was similar. Inflection temperatures were higher than potato isolated patatins. Antioxidant capacity of rPatB2 and rPat17 was similar to that of commercial patatin and the specific enzymatic activity of rPatB2 was 5-fold higher than rPat17 and patatins isolated from potato. Results indicate yeast-derived patatin properties are comparable to patatins from potatoes, suggesting their potential use in various plant-based products such as meat and dairy analogues.
Keywords: Food biotechnology; Patatin; Pichia pastoris; Protein isolate; Recombinant protein.
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