Gelation properties and protein conformation of grass carp fish ball as influenced by egg white protein

J Texture Stud. 2022 Apr;53(2):277-286. doi: 10.1111/jtxs.12668. Epub 2022 Mar 12.

Abstract

Dried egg white powder (EWP) and purified ovalbumin (OVA, 98%) were used as supplements to improve grass carp (GC) fish balls (FB) quality. The effects of EWP and/or OVA contents on the gel strength, water holding capacity (WHC), moisture migration and distribution, and rheological properties of GC-FB, as well as on myofibrillar protein (MfP) structures in the GC-FB were evaluated. The results showed that with the increase of EWP addition from 0 to 4% (w/w), the gel strength, and WHC of the GC-FB samples were increased from 34.28 to 66.63 N × mm, and 83.02 to 88.36%, respectively, but the increases were insignificant between 3 and 4% EWP-added GC-FBs (p > .05). As the EWP increased, the T2 relaxation time shifted toward lower values, indicating a general decline in water mobility. The effects of EWP on rheological properties were insignificant. Addition of OVA and/or EWP led to changes in secondary structural units in the FB, with α-helix (27.53%) reaching the highest value in OVA-added GC-FB, β-sheet (46.07%) reaching the highest value in GC-FB, and β-turn (33.54%) reaching the highest value in EWP-added GC-FB, respectively. Raman spectroscopy revealed that OVA-added GC-FB had the lowest hydrophobic interlinkages. Protein pattern analysis suggested that the OVA (1.58%) might contribute to the decrease in the myosin heavy chain band intensity through cross-linked with MfP. These results suggested that EWP could improve the quality of GC-FBs and OVA played an important role with MfP gelation.

Keywords: Ctenopharyngodon idellus; egg white powder; gel properties; ovalbumin; protein structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carps*
  • Egg Proteins* / chemistry
  • Eggs
  • Hydrophobic and Hydrophilic Interactions
  • Protein Conformation

Substances

  • Egg Proteins