Effects Of Arginine Assisted By Ultrasound On Physicochemical Properties And Gel Properties Of Nemipterus Virgatus Myofibrillar Protein

With the improvement of consumers' health awareness and suffering from various chronic diseases,the development of low-sodium foods is of great significance to consumers.Ultrasound is an emerging technology that enhances the functional properties of proteins by altering the structure of proteins.L-Arg has the ability to improve the solubility of proteins at low ionic strength,thereby improving the gel properties of proteins,but there are few studies on the interaction between amino acid and protein gel properties in deep-sea fish.Therefore,in this paper,Nemipterus virgatus was used as experimental material to study the effects of ultrasonic assisted by L-Arg on the physicochemical properties,protein structure and gel properties of the Nemipterus virgatus myofibrillar protein,which is a high quality protein resource for deep sea fish.This paper provide a new way for the development and utilization of aquatic protein resources.At the same time,it also provides theoretical basis and technical guidance for the production of low sodium gel surimi products of good quality.The main results are as follows:1.L-Arg assisted by ultrasound had different effects on the physicochemical properties of Nemipterus virgatus myofibrillar protein,The main results were as follows:L-Arg assisted by ultrasound could obviously increase the solubility of myofibrillar protein,the potential value of the solution,and decrease the particle size and turbidity of the solution.The addition of 60 mmol/L L-Arg could obviously increase the pH value of the solution.However,there was no obviously change in the pH value of the myofibrin solution after ultrasonic treatment.2.L-Arg assisted by ultrasound had different effects on the structure of myofibrillar protein of Nemipterus virgatus,Ultrasonicassisted by L-Arg treatment could increase the surface hydrophobicity,sulfhydryl content and decrease the fluorescence intensity of myofibrillar protein solution at low ionic strength.At the same time,Ultrasound assisted by L-Arg treatment changed the secondary structure of the myofibrillar protein under low ionic strength,in which the ?-helix content was reduced to 47.38%,and the ?-sheet content was increased to25.46%,?-turn the content increased to 16.42%,and the content of the random coil structure increased to 10.75%.In addition,ultrasonic treatment of myofibrillar protein under low ionic strength could increase the ultraviolet absorption intensity,but had no obvious change on the molecular weight of myofibrillar protein.3.The effects of L-Arg assisted by ultrasound on the gel properties of Nemipterus virgatus myofibrillar protein were mainly shown in the following aspects: L-Arg assisted by ultrasound could obviously improve the gel strength,hardness,water holding capacity and rheological properties of myofibrillar protein under low ionic strength,the loss of cooking loss was reduced,but there was no effect in the gel's color.At the same time,the network structure of myofibrillar protein gel was denser.Uniform,free water in the gel is converted into water that is not easily flowing or bound to water.According to the chemical force of gel,hydrophobic interaction and disulfide bond can be increased,and ionic bond and hydrogen bond could be reduced.In conclusion,L-Arg assisted by ultrasound treatment of myofibrillar protein can improve gel quality fission induced by low salt and the meat product quality characteristics,which can maximize the functional characteristics of meat protein.The development of low-salt meat products will have a good application prospects.