Development of a time-temperature integrator system using Burkholderia cepacia lipase

Abstract

A time-temperature integrator (TTI) is a device used to show a time-temperature dependent change that reflects the temperature history and quality status of the food to which it is attached. An enzymatic TTI system based on the reaction between Burkholderia cepacia lipase and tricaprylin, which causes a pH change, was developed. The temperature dependence of the response rate of this new lipase-type TTI was modeled using the Arrhenius equation, and the estimated activation energy was calculated as 70.61±11.10 kJ/mol (±95% confidence interval). The TTI response was validated under dynamic storage conditions with independent variable temperature experiments, and a good agreement was obtained between the predicted and measured values.

Enzymatic Time-Temperature Indicator Prototype Developed by Immobilizing Laccase on Electrospun Fibers to Predict Lactic Acid Bacterial Growth in Milk during Storage

“…The laccase TTI prototype and milk were incubated to simulate normal and abnormal storage temperatures 4 and 25 °C, and the temperature was switched every 8 h; 8 h of 4 °C followed by 8 h of 25 °C was regarded as one cycle, and three cycles were performed over 48 h. The results showed that the reaction rate ( k ) of laccase at 4 °C was lower than that at 25 °C in all cycles, except the first ( Figure 6 ), which indicated that the laccase TTI prototype exhibited a favorable response to temperature, and that the coloration was reproducible under temperature fluctuations. Temperature sensitivity was thus retained by the immobilized laccase during temperature fluctuations, and dynamic modeling performed through kinetic parameters and numerical analysis was effective; the present findings are similar to the results of a reaction kinetics study of a lipolytic enzyme TTI examined under dynamic temperature profiles [ 30 ]. Because the coloration of the laccase TTI prototype was considered to follow a first-order reaction, the initial reaction occurred quickly.…”

Development and characterization of an enzymatic time-temperature indicator (TTI) based on Aspergillus niger lipase

“…Yan et al (2008) developed a new amylase-based TTI used for the food cold chain. Kim, Park, and Hong (2012) described an enzymatic TTI system based on the reaction between Burkholderia cepacia lipase and tricaprylin. Kim, Kim, and Lee (2012) developed an enzyme based TTI prototype that used laccase.…”

Application of mixture rule to determine arrhenius activation energy of time temperature integrator using mixture of laccase from Pleurotus ostreatus and PEGylated laccase from Trametes versicolor

“…Because laccase follows simple discoloration kinetics (Huber and Carré, 2012), the color response to time-temperature variation was linearly proportional to the rate of color change, allowing direct and intuitive determination of the remaining shelf-life of food quality losses (Park et al, 2013). However, the major drawback of enzymatic TTI for monitoring chilled food shelf life is not only the narrow range of Ea, but also the Ea value is by no means comparable to that of food spoilage and deterioration (Tsoka et al, 1998;Bobelyn et al, 2006;Kim et al, 2012a;Kim et al, 2012b). Taoukis (2001) suggested that any TTI device with Ea within 25 kJ/mol from a food quality factor of interest could be acceptable to ensure accuracy of an enzyme TTI for prediction of the remaining shelf-life of food.…”