Low-moisture foods such as spices, grains, and seeds constitute an important part of the human diet. Increased consumer concern for food safety and food quality has focused on the decontamination technologies required for low-moisture foods. Cold plasma treatment has been a promising novel technology in the food processing industry due to its advantages in safety, efficiency, versatility, and environmentally friendly nature. It has shown various capabilities on safety and quality control in low-moisture foods. This paper comprehensively reviewed the application of cold plasma in low-moisture foods, including inactivation of microorganisms, degradation of mycotoxins, influences on the quality of low-moisture foods, and promotion of seed germination. Cold plasma can inactivate the pathogenic microorganisms on the surface of low-moisture foods, by generating active species, ultraviolet radiation, and electric fields, which helps to extend the shelf life of foods while having minimal impact on food quality. Cold plasma technology is also an effective approach to detoxify mycotoxin-contaminated low-moisture foods by degrading various mycotoxins. With the manipulation of parameters for cold plasma generation, target functional properties of food products may be obtained. In addition, the application of cold plasma in seed germination is promising and could be of great significance to the global food crisis. This review also suggests that more systematic studies are needed to employ cold plasma in the low-moisture foods industry for selected applications.

This study assessed the gel properties and conformational changes of duck myofibrillar protein (DMP) affected by plasma-activated water (PAW) generated at various discharge times (0 s, 10 s, 20 s, 30 s, and 40 s). With the treatment of PAW-20 s, the gel strength and water-holding capacity (WHC) of DMP gels were significantly increased when compared to the control group. Throughout the heating process, dynamic rheology revealed that the PAW-treated DMP had a higher storage modulus than the control. The hydrophobic interactions between protein molecules were significantly improved by PAW, resulting in a more ordered and homogeneous gel microstructure. The increased sulfhydryl and carbonyl content in DMP indicated a higher degree of protein oxidation with PAW treatment. Additionally, the circular dichroism spectroscopy demonstrated that PAW induced α-helix and β-turn transformed to β-sheet in DMP. Surface hydrophobicity, fluorescence spectroscopy, and UV absorption spectroscopy suggested that PAW altered DMP’s tertiary structure, although the electrophoretic pattern indicated that the primary structure of DMP was mostly unaffected. These results suggest that PAW can improve the gel properties of DMP through mild alteration in its conformation.