Effects of temperature on the denaturation and aggregation of ( Lateolabrax japonicus ) myosin from sea bass surimi

Abstract

This study aimed to investigate the effects of temperatures of 30-90°C on myosin denaturation and aggregation in sea bass (Lateolabrax japonicus) during setting. The result indicated that the myosin of sea bass began to form gels at 60°C, and surface hydrophobicity increased by around 8.9% at 40°C and reached its maximun at 60°C. During setting at 40°C and 60°C, the ratios of α-helix of myosin reduced gradually and finally decreasing by 17.1% and 25.2%, respectively. Incubating at 90°C, α-helix continued to transform into random coil. Association with the results of surface morphology, it further confirmed that the temperatures of 40°C and 60°C were two important denaturation and aggregation temperatures. At 90°C, myosin of sea bass formed a fine and dense gel network under the joint action of nondisulfide covalent bond, disulfide bond and hydrophobic interaction. Practical applicationsThe raw materials for marine surimi are becoming scarcer with marine overfishing and the increasing demand for surimi. Sea bass, an important economic mariculture fish in China, has white meat and less bone spur and is advantageous for the development of surimi products as raw materials. During heating of surimi, the change of myosin structure is a main important key to forming a gel network. This research revealed the changes of sea bass myosin from denaturation, aggregation to gel formation during heating and provided a theoretical basis for the processing of sea bass surimi. 2 of 11 | LIU et aL.ionic bonds on protein structure increase, forming larger molecular agglomerates, and an irreversibly stable three-dimensional network structure is gradually assembled (Lanier et al., 2005;Liu et al., 2008).However, the denaturation and aggregation properties of myosin are known to be different in different fish species (Ogawa et al., 1993;Riebroy et al., 2008), as these properties are determined by the stability of the protein, which depends on the temperature of the fish habitat (Shu-Fang et al., 1989). Yongsawatdigul and Park (2003) reported that the denaturation and aggregation of myosin from threadfin bream (Nemipterus bleekeri) occurred simultaneously at 34.5°C. Formation of protein aggregates and three-dimensional network structures of actomyosin and myosin from yellowcheek carp at 25-30°C was far less than those at 40-45°C (Ding et al., 2014).Hence, it is important to study the aggregation behavior of myosin in different fish species to improve the quality of surimi processing.Marine fishes, with better gel properties and lack of foul odor, are used as raw materials for surimi. However, due to marine overfishing and the increasing demand for surimi, the raw materials for marine surimi are becoming scarcer. (Lin et al., 2020). Sea bass (Lateolabrax japonicus) is an important economic mariculture fish in China. The output of sea bass in China was 180,200 t in 2019, an increase of 8.16% over 2018, with the output increasing annually (Ministry of Agriculture and Rural Affairs of the People's Republic of China, 2020). Additionally, sea...

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“…It is in a 'Y' shape. 57 Myosin denatures during freezing storage, which is manifested by increased surface hydrophobicity, sulfhydryl oxidation, decreased salt solubility and loss of Ca 2+ -ATPase activity. 58 Myosin denaturation results in a weakening of the gelling ability of surimi.…”

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