Fishprotein powders were produced from silvercarp myofibrillar proteins using vacuum freeze-drying and vacuum spray-drying. Biochemical properties and functionalities of freeze-dried and spray-dried powders were determined. The myofibrillar proteins were partially denatured under both the drying methods which were evidenced by the increase of free sulfhydryl content,surface hydrophobicity, and intrinsic fluorescence while the decrease of the Ca2+-ATPase activity and percentage of the α-helical structure. With respect to vacuum freeze-drying, the proteins were denatured to a higher degree by vacuum spray-drying. The spray-driedfishproteinpowdershowedahigherwaterretentioncapacityandemulsifyingstabilityindex,butthesamesolubility andemulsifyingactivityindex.Themicrographsindicatethatvacuumfreeze-driedpowderformedaspongystructure,whilethe powderundervacuumspray-dryingmostlyappearedsphericalinshapewithhollowinside.Thus,thetwodryingmethodscanbe used to manufacture fish protein powders with varied molecular structures and functionalities