Effects of Vacuum Freeze-Drying and Vacuum Spray-Drying on Biochemical Properties and Functionalities of Myofibrillar Proteins from Silver Carp

Abstract

Fish protein powders were produced from silver carp myo brillar proteins using vacuum freeze-drying and vacuum spray-drying. Biochemical properties and functionalities of freeze-dried and spray-dried powders were determined. e myo brillar proteins were partially denatured under both the drying methods which were evidenced by the increase of free sulfhydryl content, surface hydrophobicity, and intrinsic uorescence while the decrease of the Ca 2+ -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. e spray-dried sh protein powder showed a higher water retention capacity and emulsifying stability index, but the same solubility and emulsifying activity index. e micrographs indicate that vacuum freeze-dried powder formed a spongy structure, while the powder under vacuum spray-drying mostly appeared spherical in shape with hollow inside. us, the two drying methods can be used to manufacture sh protein powders with varied molecular structures and functionalities.

Effect of Drying Methods on Physicochemical Characteristics and Functional Properties of Duck Blood Gel

“…These results indicated that the prolonged heat-drying process affected protein exposure to tryptophan residues and were consistent with the results of a previous study using gelatin ( Feng et al, 2021 ). Another prior study noted that the fluorescence intensity of silver carp ( Hypophthalmichthys molitrix ) myofibrillar protein increased significantly after FD and vacuum SD ( Niu et al, 2019 ). Exposure of amino acids with fluorescent properties, such as tyrosine and tryptophan, can result in an increase in fluorescence intensity ( Jiang et al., 2017 ).…”

“…The drying process of blood can eliminate disadvantages such as spoilage ( Hou et al, 2019 ; Wang et al, 2018 ). In addition, dry form of blood powder has many commercial merits, such as low storage costs, enhancement of storage and transportation, and the ease of mixing with other materials ( Jin and Choi, 2021 ; Niu et al, 2019 ). However, depending on the drying conditions and methods, the biochemical characteristics and functional properties of the product may vary ( Lewicki, 2006 ).…”

“…SD has the advantage of continuous and fast drying at a low cost. FD maintains a low temperature throughout the drying process, which is suitable for drying thermally sensitive ingredients ( Niu et al, 2019 ). VD can reduce protein denaturation due to contact with oxygen and has been investigated as a method to overcome some of the disadvantages of FD ( Parikh, 2015 ).…”

Enhancement of storage stability of surimi particles stabilized novel pickering emulsions: Effect of different sequential ultrasonic processes

“…It was noteworthy that there existed remarkable differences between the surimi particles and myofibrillar proteins directly extracted from various raw materials in many aspects such as physical state, hydration capacity, conformation, emulsification, etc. [20] , [21] . However, the effects of different sequential ultrasonic processes on the physical properties and stabilization mechanisms of Pickering emulsions stabilized by surimi particles especially with low concentrations are unclear.…”

Comparative study of two types of pre-extraction treatment (drying or non-drying) on physicochemical, structural and functional properties of extracted insect proteins from Tenebrio molitor larvae

“…At the same time, the content of the β-sheet is positively correlated with the α-helical content. Some studies found that the secondary structure of a protein was determined by electrostatic interactions and hydrogen bonds between amino acids ( Niu et al, 2019 ), and when the α-helical structure was denatured by heat, freezing, or oxidation, α-helical structures usually turned into β-sheet ( Guo et al, 2019 ). This result suggests that the MD group has weakened electrostatic interactions, and the stable hydrogen bonds due to heating destroyed the secondary structure of the protein and transformed the α-helical structures into β-sheet.…”