Comparative proteomic analysis reveals negative pressure airflow drying preserves protein structure and nutritional quality in Oviductus ranae, indicating an optimal processing method.
Key Points
To examine changes in protein composition, secondary structure, and physical quality in Oviductus ranae processed by negative pressure airflow drying compared to traditional drying methods.
Compared negative pressure airflow combined desiccator drying (NPAD) with natural drying (ND) and hot-air drying (HAD).
Evaluated physicochemical properties, microstructure, and protein secondary structure alterations.
Quantified proteome differences using label-free data-independent acquisition (DIA) proteomics.
NPAD best preserved protein secondary structure, maintaining an α-helix content of 39.62% compared to 38.71% for ND and 25.14% for HAD.
Identified drying-sensitive candidate indicator proteins, including glutathione S-transferase ω, β-enolase, fructose-diphosphate aldolase, paralbumin, and actin β chain.