Produção Nacional
Revisado por pares
Structural features of myofibrillar fish protein interacting with phosphatidylcholine liposomes
2020; Elsevier BV; Volume: 137; Linguagem: Inglês
10.1016/j.foodres.2020.109687
ISSN1873-7145
AutoresCristian Mauricio Barreto Pinilla, Adriano Brandelli, M.E. López‐Caballero, P. Montero, M.C. Gómez‐Guillén,
Tópico(s)Silk-based biomaterials and applications
Resumo• Interactions of phosphatidylcholine liposomes with surimi protein were investigated. • FTIR indicates that liposomes induce denaturation and aggregation of surimi protein. • Exposure of tyrosine residues revealed by intrinsic fluorescence analysis of protein. • Increased size and modified surface charge of liposomes interacting with surimi. • The interactions were influenced by the purification degree of phosphatidylcholine . The interactions between liposomes and fish myofibrillar protein (surimi ground salted protein, SURP) were evaluated. Liposomes prepared with ultrapure phosphatidylcholine (UPC) or partially purified phosphatidylcholine (PPC) were dispersed at different weight ratio on SURP. Changes in protein stability and structure were evaluated using FTIR, intrinsic fluorescence and free sulfhydryl groups, and changes in liposome properties were studied by dynamic light scattering and electron microscopy. PPC promoted denaturation and aggregation of SURP, reflected in secondary structure loss, exposure of tyrosine residues and increment of free sulfhydryl. UPC produced partial unfolding and changes in the secondary structure of SURP from α-helical to β-strand. Liposome size increased by about 40% and showed modified surface charge after SURP exposure, indicating the formation of protein corona. Surface charge and composition of liposomes influence SURP stability and could exert different effects on the myofibrillar protein network, which is important for liposome applications in surimi products.
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