Thermal and physicochemical properties of red tilapia (Oreochromis niloticus) surimi gel as affected by microbial transglutaminase

Abstract

Thermal and physicochemical properties of red tilapia (Oreochromis niloticus) surimi gel incorporated with different levels of microbial transglutaminase (MTGase) were investigated. Surimi samples mixed with various concentrations of MTGase were subjected to two-stages heating (at 45°C followed by 90°C) to prepare surimi gel. Samples formulated with 0.30 MTGase (units/g surimi) showed the highest breaking force and deformation, and lowest expressible water content among treatments. Highest storage modulus was found in the gels mixed with 0.30 MTGase (units/g surimi). Compared with control surimi gel, addition of microbial transglutaminase to levels 0.10, 0.20 and 0.30 (units/g surimi) increased the enthalpy and maximum transition temperature of myosin. Results suggest that up to 0.30 MTGase (units/g surimi) could improve texture, colour, water-holding capacity, elasticity and thermal stability of red tilapia surimi gel.

The influence of additives on frozen snakehead fish surimi and the application of transglutaminase to fish cakes

“…At the same time, the results have also shown that increasing the rate of excess transglutaminase results in a breakdown of the gel structure of the product. These results are in accord with those obtained by Jiang et al (2000) who reported that the gel structure of surimi gels from threadfin bream (Nemipterus virgatus) and pollock (Rastrelliger kanagurta) increased when transglutaminase increased up to a certain level, and a further increase in transglutaminase decreased the gel structure of the product (Seighalani et al, 2017).…”

“…The study by Seighalani et al (2017), and Duangmal and Taluengphol (2010) also showed similar results with transglutaminase supplementation at 0.3 U/g surimi and 3 g/kg surimi, respectively. As transglutaminase catalyzes the cross-linking reaction of myosin and leads to the formation of protein intra-and intermolecular covalent bonds, it was concluded that differences in the whiteness value could correspond to the increased turbidity of gels because of transglutaminase activity.…”

“…Reactions catalysed by transglutaminase result in significant changes in the physicochemical properties of gel, such as changes in viscosity, thermal stability and elasticity. Yongsawatdigul et al (2002) investigated the residual transglutaminase activity in threadfin bream surimi wash water, confirming that 44% of the original transglutaminase activity remained in the final surimi after the washing process (Seighalani et al, 2017). All this has shown the need for transglutaminase supplementation during protein gel formation from fish surimi.…”

“…As transglutaminase catalyzes the cross-linking reaction of myosin and leads to the formation of protein intra-and intermolecular covalent bonds, it was concluded that differences in the whiteness value could correspond to the increased turbidity of gels because of transglutaminase activity. Moreover, an increase in whiteness could be caused by other compounds (lactose, maltodextrin) in commercial transglutaminase www.food.actapol.net/ powder, which cause a light scattering effect, as shown by Seighalani et al (2017). Besides whiteness, the water holding capacity and gel strength are also important indicators in evaluating fried fish cake quality.…”

Effect of gellan and calcium chloride on properties of surimi gel with low and high setting phenomena

“…Those products include sh balls, sh cakes, crab meat analogues, etc. 3 The prime factor in achieving the desired texture is the gel-forming ability of myobrillar sh proteins. 4 The textural property of gel is the most important attribute, which determines the price of surimi.…”