Keywords

Pleurotus Eryngii, Protein Isolate, Albumin, Physical And Chemical Properties, Functional Properties

Abstract

Using Pleurotus eryngii as raw material, Pleurotus eryngii protein isolate (PEPI) was extracted by alkali-soluble acid precipitation method and the main protein components were separated by Osborne method, and its physical and chemical properties and functional analysis were studied. The results showed that the protein mass fraction of Pleurotus eryngii was 17.57% (based on dry mass), with Pleurotus eryngii albumin (PEA) as the main protein, accounting for 81.12% of the total isolated protein components. Both PEPI and PEA contain 18 kinds of amino acids, and the essential amino acid content accounts for 40.80% and 40.51% of the total amino acid content respectively. Compared with PEPI, the surface hydrophobicity of PEA (265.25) is significantly higher than that of PEPI (164.27) (P<0.05), while the total thiol and disulfide bond contents are lower, 61.53?¦Ìmol/g and 10.39?¦Ìmol/g respectively. ; Thermal denaturation temperature (100.98?¡æ) is lower than PEPI (108.27?¡æ), and PEA water holding capacity (1.64?mL/g) and oil holding capacity (5.59?mL/g) are significantly lower than PEPI (3.58, 8.36?mL/g) g) (P<0.05). The solubility, foaming property, foam stability, emulsifying property and emulsifying stability of PEPI and PEA have similar trends with pH value, and are all lowest at the isoelectric point. Fourier transform infrared spectroscopy showed that the secondary structures of PEPI and PEA were mainly ¦Â-sheets and ¦Â-turns, and PEPI showed a honeycomb structure under scanning electron microscopy. Compared with PEA, PEPI has better physical and chemical properties and functional characteristics   For further details regarding this article and its research, please do not hesitate to contact our team for assistance. Original research done by Feng Li, Zhang Ruoxi, Xu Huaide, Wang Xiaojing, Xue Yuan, Lei Hongjie, Wei Junhui  

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