Abstract
The pulsed light (PL) technique is used for food and surface decontamination widely. The sterilization effect of PL is well known and identified as the photo-chemical effect. Besides, PL is used to inactivate enzymes, reduce the immunoreactivity of proteins, and change protein function properties at a laboratory level. The current study aims to review the effect of PL on proteins by highlighting the differences between proteins in buffer solutions or food systems. Although PL is known as a non-thermal technique, most studies done on food systems, food temperature raised considerably. Therefore, PL inactivated many enzymes in buffer solution non-thermally, while mostly with a high increase in temperature of a food system. PL reduced food allergens several folds in some foods. However, immunoreactivity responses of some protein were increased after PL treatment. Also, the current study covers the conformational changes of proteins that occur because of PL treatment. Therefore, some techniques used to follow proteins structural changes such as polyacrylamide gel electrophoresis (SDS-PAGE), high-performance liquid chromatography (HPLC), Fourier-transform infrared spectroscopy (FTIR), etc. were defined. Studies reported that PL altered proteins structure differently. For example, some studies reported that PL degraded some proteins, while other studies suggested that PL aggregated proteins. Also, there were contrary results regarding α-helix and ß-sheet concentration for the treated proteins. In conclusion, some techniques, such as amino acid sequencing, specially when some small new fragments proteins appeared on SDS-PAGE, should be used to detect the effect of PL on proteins precisely.