The food packaging sector has experienced much development since its inception. In the past few decades, innovations in packaging sector have led to the development of smart packaging (SP) systems that carve a niche in a highly competitive food industry. SP systems have great potential for improving the shelf‐life, and safety of food products apart from their basic roles of protecting the products against unwanted biological, chemical, and physical damage and keeping them clean. Indicators and sensors, SP components, are used for real‐time monitoring of meat quality and subsequently inform the retailers and consumers about the freshness, microbiological, temperature, and shelf life status of the products. Barcodes and radio‐frequency identification tags are employed in meat packaging for real‐time information about the authenticity, and traceability of the products in the supply chain. Recently, innovations in SP technologies resulted in fast, sensitive, and effective detection, sensing, and record keeping of freshness, microbiological, and shelf life status of meat and meat products. The SP system shows promise for extensive utilization in the meat industry in response to the consumer appreciation for safe, and quality meat products, as well as their waste reduction notions. This paper gives an updated overview of ongoing scientific research, and recent technological advances that offer the perspectives of developing smart meat packaging systems that are capable of monitoring the physical, microbial, and chemical changes of the package contents from producer to the point of sale and even beyond, and remediating potential adverse reactions.

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β-Lactoglobulin (β-LG) is recognized as the major milk allergen. In this study, the effects of transglutaminase (TGase) and glucosamine (GlcN)-catalyzed glycosylation and glycation on the conformational structure and allergenicity of β-LG were investigated. The formations of cross-linked peptides were demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and GlcN-conjugated modification was identified using matrix-assisted laser desorption ionization-time of flight-mass spectrometry (MALDI-TOF-MS). Structural analysis revealed that glycosylation and glycation of β-LG induced unfolding of the primary protein structure followed by a loss of the secondary structure. As revealed by circular dichroism (CD) spectroscopy, glycosylated β-LG exhibited the highest increase in the β-sheets from 32.6% to 40.4% (25 °C) and 44.2% (37 °C), and the percentage of α-helices decreased from 17.7% to 14.4% (25 °C) and 12.3% (37 °C), respectively. The tertiary and quaternary structures of β-LG also changed significantly during glycosylation and glycation, along with reduced free amino groups and variation in surface hydrophobicity. Immunoblotting and indirect enzyme-linked immuno sorbent assay (ELISA) analyses demonstrated that the lowest IgG- and IgE-binding capacities of β-LG were obtained following glycosylation at 37 °C, which were 52.7% and 56.3% lower than that of the native protein, respectively. The reduction in the antigenicity and potential allergenicity of glycosylated β-LG was more pronounced compared to TGase treated- and glycated β-LG, which correlated well with the structural changes. These results suggest that TGase-catalyzed glycosylation has more potential compared to glycation for mitigating the allergenic potential of milk products.

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