## 1 Introduction  
The use of high-pressure processing (HPP) for the gelation of fish muscle has been studied in various fish species such as barramundi and golden threadfin bream [1, 2]. HPP followed by heating resulted in gels with improved texture, glossier, and smoother appearance compared to those formed by heat-only gelation [3]. In addition, HPP has been applied to produce reduced salt surimi/gels from fish muscle with comparable quality to heat-treated gels containing 2% added salt [4, 5].  
Conventionally, thermal gels are prepared with 2% added salt to enhance functionalities such as improved texture, better water-holding capacity and fat retention, and inhibition of microbial growth during storage [6]. Under salt-added conditions, more proteins responsible for the physical stability and functionality of the product are extracted and solubilized, leading to an increase in the connection between protein and protein-lipid structures. Upon heating, these structures denature and aggregate, forming a gel matrix [7]. The reduction in salt concentration in gels may lead to lower quality due to inadequate solubilization of gel proteins. However, the addition of a high salt concentration of 2% could cause many adverse effects on the gel product, such as oxidative reactions in the gel product or high blood pressure in susceptible individuals [8]. Thus, there is a high demand to find alternative methods to reduce salt in gel products.  
HPP has recently emerged as a promising method for producing high-quality gels under low salt conditions. Several mechanisms have been proposed to explain the improved quality of reduced salt gelation induced by HPP. One explanation is that high-pressure processing (HPP) strengthens interactions between myofibrillar proteins, enhancing the solubilization of muscle proteins for gel formation under low-salt conditions [9; 10]. [PERSON] et al. [11] also suggested that HPP disrupts the myofibrillar structure and depolymerizes the thin filament, contributing to increased gel strength in low salt conditions. Additionally, HPP is believed to promote the formation of ionic, hydrogen, and hydrophobic interactions, which reinforce the gel structure [6]. Several studies have also reported that hydrogen bonding occurs at pressures below 150 MPa, while ionic and hydrophobic interactions dominate at pressures above 200 MPa [12; 13].  
Pangasius catfish (_Pangasianodon hypophthalmus_) is one of the commercially important aquaculture species in several Asian countries and is commonly formed in Vietnam, Thailand, Indonesia, India, and Bangladesh [14]. It is traded globally, particularly in the United States, European Union, China, Australia, and other markets, primarily in the form of frozen white fillets [14; 15]. Pangasius fish muscle has also been utilized to produce various value-added products, such as fish fingers, fish cakes, fish sausages, surimi, and fish patties [16]. However, the application of novel processing technologies like HPP on pangasius fish muscle products remains limited. Therefore, the primary objective of this study is to investigate the effects of HPP on the quality of pangasius gels, particularly in the salt-reduced condition.