Structure and functionality of Pleurotus geesteranus protein isolate as a function of pH.

Abstract

Edible mushroom proteins hold great potential for food applications, but those extracted using the alkaline extraction-acid precipitation method typically exhibit poor solubility in neutral water, with the structural changes during acid precipitation remaining unclear. In this study, Pleurotus geesteranus protein isolate (PGPI) with high water solubility was prepared with alkaline extraction, followed by dialysis and freeze-drying, and the effects of pH on the structural and functional properties of PGPI were systematically investigated. PGPI was enriched in essential and aromatic amino acids, and the molecular weight of bands in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile was mainly distributed below 45 kDa. The zeta potential of PGPI changed from +16.84 to 17.58 mV when the pH increased from 2 to 9, with a pI of 4.3. At pH 7, PGPI showed a size of 232.7 nm. Away from pH 7, the particle size of PGPI increased. When the pH decreased from 7 to 2, PGPI exhibited a lower α-helix structure content and a higher β-sheet content and a gradual decrease in fluorescence intensity. In addition, as the pH approached 4, H₀ and the content of SS group increased to a peak. These results indicated that lowering the pH induced the development of more ordered protein structure, which could be the primary reason for the poor water solubility of P. geesteranus protein obtained through alkaline extraction and acid precipitation. Additionally, these structural changes result in alterations to its functional properties, including water-holding capacity, oil-holding capacity, foaming capacity, foaming stability, emulsion activity index, and emulsion stability index.