Effect of High Voltage Cold Plasma on Oxidation, Physiochemical, and Gelling Properties of Myofibrillar Protein Isolate from Asian Sea Bass (Lates calcarifer)

The effects of in-bag dielectric barrier discharge high voltage cold plasma (IB-DBD-HVCP) on myofibrillar protein isolate (MPI) from Asian sea bass (ASB) and its impact on the physiochemical and gelling properties of MPI gels were elucidated. A mixture of argon (90%) and oxygen (10%) was used for generating IB-DBD-HVCP. MPI was subjected to IB-DBD-HVCP for varying times (5-15 min). Total carbonyl content was increased, while total sulfhydryl content was decreased in MPI, especially with augmenting treatment time (TT) (p < 0.05). Surface hydrophobicity initially increased when IB-DBD-HVCP TT of 5 min (DBD-HVCP5) was implemented, followed by subsequent decrease with increasing TT. Based on gel electrophoresis, lower actin and myosin heavy chain (MHC) band intensities were found for MPI subjected to IB-DBD-HVCP, particularly when a TT longer than 10 min was used, compared to those of the control. Gel made from DBD-HVCP5 had higher breaking force, deformation, and highest G ' value compared to others. A more ordered and fibrous network was found in DBD-HVCP5 treated gel. Therefore, IB-DBD-HVCP treatment, particularly for 5 min, enhanced cross-linking of proteins in ASB myofibrillar proteins, which resulted in the improved gel elasticity and strength.

Automated summary

The effects of in-bag dielectric barrier discharge high voltage cold plasma (IB-DBD-HVCP) treatment on myofibrillar protein isolate (MPI) from Asian sea bass (ASB) were investigated, showing that longer treatment times resulted in increased total carbonyl content and decreased total sulfhydryl content in MPI. Gel electrophoresis revealed lower actin and myosin heavy chain band intensities in MPI treated with IB-DBD-HVCP, particularly with longer treatment times, while gels made from DBD-HVCP5 exhibited higher breaking force, deformation, and G' value.