Effect of soy protein isolate on the techno‐functional properties and protein conformation of low‐sodium pork meat batters treated by high pressure

Abstract

In this study, the changes of color, emulsion stability, rheological property, and protein secondary structure attributes of pork meat batters (1% sodium chloride) treated by high pressure with different soy protein isolate were investigated. Three batters with 0, 2, and 4% soy protein isolate were prepared under 200 MPa for 10 min, respectively.The pH, emulsion stability, L* and b* values were significantly improved when added soy protein isolate, the a* value was significantly (p < .05) decreased. The pH and color were not significantly different (p > .05) with soy protein isolate increased, but emulsion stability was increased (p < .05). Added soy protein isolate and treated by high pressure delayed the thermal denaturation of meat protein and declined the pre-gel effects generated by the denaturation of myosin tails from 53 C to 59 C, and induced the α-helix structure changed into β-sheet, β-turn, and random coil structures. Especially, the content of the random coil structure was significantly increased (p < .05) from 11.42 ± 0.26% to 14.22% ± 0.29 with soy protein isolate increased. Overall, the 2% soy protein isolate addition could improve the techno-functional properties and emulsion stability of pork meat batters treated by high pressure. Practical applicationsThe pork meat batters with soy protein isolate treated by high-pressure processing should be adopted for lowering sodium content in meat processing industry.

Technological and functional properties of reduced‐salt pork batter incorporated with soy protein isolate after pressure treatment

“…Meanwhile, the L* value was significantly increased, and a* and b* values were significantly decreased ( P < 0.05) at 200, 300 and 400 MPa, compared to those at 0.1 MPa; however, all L* , a* and b* values showed no significant differences. A possible reason is that HP processing can induce changes in the molecular interactions (hydrogen bonds, hydrophobic interactions, sulphydryl and electrostatic bonds) and conformation of the myofibrillar protein and SPI, which presents altered functional properties, including improved solubility and water‐holding capacity (Li et al ., 2020). In addition, HP processing could change the oxidative states of the pigment myoglobin, and the occurrence of redox reaction can be visualised using the L* , a* and b* values.…”

“…Storage modulus is a key index for rheological properties of meat proteins, which is in line with the elastic behaviour of the solid‐like components and directly affects the gel properties of meat batter (Li et al ., 2020). The effects of G′ on raw batters supplemented with SPI treated at different pressures from 20 to 80 °C are shown in Fig.…”

“…Glycinin (11S) and β‐conglycinin (7S) are the major components of SPI, comprising approximately 76%, and their properties are affected by pressures (Sha & Xiong, 2020). Our previous study found that adding 2% soy protein isolate could improve the techno‐functional properties and emulsion stability of pork meat batters treated at 200 MPa (Li et al ., 2020); however, only a few studies have reported the effect of different pressures on techno‐functional properties, water distribution and mobility of reduced‐salt pork batters supplemented with SPI. Therefore, this study aimed to evaluate the colour, textural and rheological properties, and water distribution and mobility of reduced‐salt pork batters (1% NaCl) supplemented with SPI (2%) treated at different pressures to obtain a method that improves the water‐holding capacity and texture of reduced‐salt pork batter.…”

Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

“…Soy protein isolate (SPI) is the main component of soy protein, and its protein content is generally higher than 90 %. Studies have shown that SPI has several functional properties, such as gelation, emulsification, and foaming [2] , [3] , and is widely used in the field of food processing [4] , [5] . However, SPI is easily affected by harsh processing conditions during processing and storage, resulting in quality deterioration.…”

Effects of β-alanine and L-histidine supplementation on carnosine contents in and quality and secondary structure of proteins in slow-growing Korat chicken meat

“…Residual amino acids from carnosine synthesis, free amino acids, might induce the oxidative modification of proteins ( Zhang et al, 2013 ). Protein oxidation causes the unfolding of its secondary structure, which is transformed into β-sheets, β-turns ( Li et al, 2020 ), and aliphatic bending groups ( Herrero, 2008 ). Katemala et al (2021) reported that the β-sheet relative content positively correlated with the shear force of KRC, and the result was confirmed by Beattie et al (2004) .…”