Effect of high pressure processing and heat treatment on the gelation properties of blue crab meat proteins

Effects of high‐pressure‐modified soy 11S globulin on the gel properties and water‐holding capacity of pork batter

“…The myosin tails in the batter were denatured, destroying the gel network formed at low temperatures, resulting in a sharp decrease in G′ in pork batter at 54–62 °C, which was the second stage (Lv et al ., 2021). In the third stage, from 63 to 80 °C, the continuous increase in temperature led to the transformation of pork batter from a sticky sol state to an elastic gel structure; thus, the G′ value continued to rise (Velazquez et al ., 2021). Moreover, the G′ values of pork batter with soy 11S globulin treated by 200 and 400 MPa were lower than those of the sample of 0.1 MPa from 20 to 52 °C, and the result indicated that the soy 11S globulin treated at high pressure had a negative effect on the strength of weak gel.…”

Combined effects of high-pressure processing and pre-emulsified sesame oil incorporation on physical, chemical, and functional properties of reduced-fat pork batters

“…A possible reason for this is that high-pressure processing can unfold muscle proteins, prompting more proteins to dissolve and form a three-dimensional network that entraps water molecules during heating ( Wang et al, 2019 ; Carballo et al, 2000 ). Some researchers have reported that because of the improvement in the solubilisation and denaturation of muscle proteins, there is an increase in water- and fat-holding capacity in meat batter treated under high-pressure processing occurred ( Kang et al, 2021 ; Yang et al, 2016 ; Velazquez et al, 2021 ). Nevertheless, excessive pressure destroys the hydrogen bonds of partially denatured protein polymers and divides them into oligomers or monomers structures ( Souza et al, 2011 ).…”

The structural rearrangement and depolymerisation induced by high‐pressure homogenisation inhibit the thermal aggregation of myofibrillar protein

“…1b. After heat treatment at 50 °C for 10 min, the HTMP also displayed high G′ value, while increasing the temperature would lead a rapid decrease in G′ value, which may be due to HPH treatment‐induced protein structure rearrangement and decreased MP denaturation temperature (Velazquez et al ., 2021), thus promoting aggregates to dissociate into smaller size at a higher temperature.…”