The gelation properties of myofibrillar proteins prepared with malondialdehyde and (-)-epigallocatechin-3-gallate

Impact of malondialdehyde (MDA) and (-)-Epigallocatechin-3-gallate (EGCG) on gelling properties of myofibrillar proteins (MPs) was investigated. Addition of 6 mM MDA enhanced molecular interactions of proteins, thus the strength and elastic modulus (G') of gel were improved. EGCG addition aggravated gel quality deterioration due to further modification of MPs induced by EGCG. Addition of 12 mM MDA jeopardized gel quality according to the increasing of strength and G', but the decreasing of water-holding capacity (WHC), and the collapse of microstructure. Nevertheless, EGCG reacted with MDA forming EGCG-MDA adducts, hence improved gel quality, which was supported by the decreasing of strength, but the increasing of WHC, and the repaired microstructure of gel at 12 mM MDA. Addition of 24 mM MDA severely jeopardized gel quality, which became even worse due to EGCG addition. This work is helpful to understand the impact of MDA and polyphenols on the gel-forming capacity of MPs.

Keywords: EGCG-MDA adducts; ESI-MS/MS; FT-IR spectrum; Heat-induced gel; Microstructure.