Application of differential scanning calorimetry in food research and food quality assurance

Abstract

Differential scanning calorimetry (DSC) is the most widely used thermal analytical technique in food research and it has a great utility in quality assurance of food. Proteins are the most studied food components by thermal analysis including studies on conformation changes of food proteins as affected by various environmental factors, thermal denaturation of tissue proteins, food enzymes and enzyme praparations for the food industry, as well as effects of various additives on their thermal properties. Freezing-induced denaturation of food proteins and the effect of cryoprotectants are also monitored by DSC. Polymer characterization based on DSC of polysaccharides, gelatinization behaviour of starches and interaction of starch with other fbod components can be determined, and phase transitions during baking processes can be studied by DSC. Studies on crystallization and melting behaviour of fats observed by DSC indicate changes in lipid composition or help characterizing products. Thermal oxidative decomposition of edible oils examined by DSC can be used for predicting oil stability. Using DSC in the freezing range has a great potential for measuring and modelling frozen food thermal properties, and to estimate the state of water in foods and food ingredients. Research in food microbiology utilizes DSC in better understanding thermoadaptive mechanisms or heat killing of food-borne microorganisms. lsothermic mierocalorimetric techniques provide informative data regarding microbial growth and microbial metabolism.

Some physicochemical and functional properties of alfalfa soluble leaf proteins

“…Two peaks are distinct for 0.5/100 g (around 68 and 77 1C), and 0.8/100 g (around 70 and 75 1C) protein CAJ, whereas three peaks (at around 58, 65, and 75 1C) are prominent for 1.8/100 g protein CAJ. The leftward shift in peak temperature is consistent with SLP protein gelling behavior , which seemed to contradict Farkas and Mohacsi-Farkas (1996). They reported that soy protein isolates became stable towards heat when the water content was lower.…”

“…The exposed hydrophobic patches come together and form aggregates. DSC analysis of protein measures the net changes between endothermic denaturation process and the exothermic process of aggregation (Farkas & Mohacsi-Farkas, 1996). Tomimatsu (1980) obtained single endothermic DSC peak at 76.2 1C for purified alfalfa rubisco at 0.11/100 g concentration.…”

Study of macromolecular interactions in low‐fat brined cheese modified with Zedu gum

“…In the present work, an increase in the T d of AS 0.25 was observed at the end of ripening. According to Farkas and Mohácsi‐Farkas () and Hägerdal and Martens (), this would be due to protein hydration. When the moisture available is only related to protein hydration, the amount of T d increases.…”

Application of differential scanning calorimetry to estimate quality and nutritional properties of food products

“…Its ability to study these processes under the dynamic temperature conditions occurring during processing, as well as to provide both thermodynamic and kinetic data, constitute the main advantages of this technique. Using DSC in the freezing range has a great potential for measuring and modelling frozen food thermal properties, as well as to estimate the state of water in foods and food ingredients (Farkas and Mohacsi-Farkas, 1996). DSC method can be easily used as an alternative technique for the measurement of oxidative stability in edible oil processing industries where mostly oxidative stability index technique is used.…”