Lipid oxidation and colour in pressure‐ and heat‐treated minced chicken thighs

Abstract

Lipid oxidation and colour in pressurised and heated chicken samples were evaluated. In a preliminary test, raw and overcooked (100 • C/60 min) minced chicken thighs were pressurised (500 MPa/50 • C/30 min). Samples were stored at 4 • C in contact with air. Thiobarbituric acid reactive substances (TBARS) were quantified at 1, 6 and 9 days. Pressure induced oxidation in chicken, but overcooking generated many more secondary oxidation compounds. In a second experiment, raw minced chicken thighs were pressurised (500 MPa/−10, 5, 20 and 50 • C/30 and 60 min) or cooked (90 • C/15 min). Samples were vacuum stored at 4 • C. TBARS were measured at 1 and 9 days, whereas colour parameters (L, a, b and E) were determined at 1 day. No differences in TBARS values were observed between untreated and pressurised samples, whereas cooked samples presented the highest values. Pressurisation for 30 and 60 min generated similar TBARS contents. At 9 days, oxidation values did not increase. Pressurisation and cooking induced marked colour changes. Pressurised samples were lighter and less red than untreated ones. Samples pressurised at 50 • C were the palest and, together with cooked samples, presented the lowest a values. Therefore pressurised chicken thigh cannot be marketed as a fresh product but can be incorporated as an ingredient in ready-to-eat meals.

Effect of single-cycle and multiple-cycle high-pressure treatments on the colour and texture of chicken breast fillets

“…Lightness of minced chicken thighs treated at 500 MPa for 60 min at different temperatures increased, and redness and yellowness declined, with increasing temperature (Beltran et al, 2004). In the present work, the behaviour of L* and b* during HP treatments resembled that occurring during cooking of chicken breast meat (Young, Northcutt, & Lyon, 1996).…”

“…Information on the effect of HP on the colour and texture of chicken meat is scarce. Regarding the colour, it has been shown that treatments at 500 MPa for 60 min at different temperatures increased lightness and reduced redness and yellowness of minced chicken thighs (Beltran, Pla, Capellas, Yuste, & Mor-Mur, 2004). Hardness of chicken breast muscle increased with both HP and heat treatments, which acted synergistically at temperatures from 20 to 50°C, although it decreased when pressures above 200 MPa were applied at temperatures of 60 or 70°C (Zamri, Ledward, & Frazier, 2006).…”

New Insights into the High‐Pressure Processing of Meat and Meat Products

“…In most of these studies, oxidation was evaluated by measuring secondary lipid oxidation products, such as thiobarbituric acid‐reactive substances (TBARS) or hexanal content. In several studies, oxidation was not increased immediately after the pressure treatment, but pressure induced lipid oxidation during subsequent storage of the meat (Dissing and others 1997; Orlien and others 2000; Beltran and others 2003, 2004a). However, Tuboly and others (2003) observed an increase in oxidation just after the pressure treatment.…”

“…In the study by Dissing and others (1997), a pressure treatment of vacuum‐packed turkey thigh muscle at 500 MPa for 30 min at 10 °C was equivalent to a heat treatment at 100 °C for 10 min in terms of TBARS found after 6 d of storage at 5 °C. Interestingly, for raw minced chicken thighs treated at 500 MPa and 50 °C for 30 or 60 min, vacuum‐packaging prevented oxidation during 9 d of subsequent storage at 4 °C (Beltran and others 2004a). Nevertheless, in the latter study, oxidation was shown to significantly increase after 6 d if samples were stored in contact with air.…”

Multi-criteria framework as an innovative tradeoff approach to determine the shelf-life of high pressure-treated poultry

“…An increase of the colorimetric L* component associated to lightening was observed following HHP and especially for pressures above 400 MPa. Although this is most documented for red meat, it has also been observed in poultry meat from 300 MPa (Beltran et al, 2004;Del Olmo et al, 2010;Kruk et al, 2011;Tintchev et al, 2010). This lightening effect has been attributed to myoglobin denaturation or oxidation and/or to heme displacement or release, at or above 400 MPa (Carlez et al, 1995), or to protein coagulation with a resulting loss of solubility of sarcoplasmic and/or myofibrillar proteins (Goutefongea et al, 1995).…”