Abstract
SummaryIn the present work, the physicochemical and functional properties, as well as the digestion behaviour of Pleurotus geesteranus mycelium protein isolates (PMPI), were investigated. SDS‐PAGE results found that the molecular weight of PMPI was mainly concentrated in >100 kDa and <25 kDa and a total of 365 proteins were detected with proteome analysis. The contents of secondary structures in PMPI were as follows: β‐sheet (27.15%) > α‐helix (23.23%) > random coil (21.92%) > β‐turn (17.21%) > β‐antiparallel (10.48%). The total sulphydryl, free sulphydryl and disulphide bond content of PMPI were 29.88, 9.77 and 10.05 μmol/g respectively. The denaturation temperature of PMPI was measured at 92.94 °C, with an enthalpy change of 39.76 J/g. However, PMPI showed poor solubility, leading to relatively low foaming properties and emulsion activity. The nitrogen release rate of PMPI was 21.78% after pepsin digestion and 74.60% at the end of trypsin digestion.
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