The quality change of shrimp is inevitable during storage, while shrimp preservation is extremely important in the fishery and food industries. Many efforts have been devoted to explore preservation strategies to maintain shrimp quality and develop sensitive freshness indicators to monitor shrimp quality during storage in the last decade. This review provides an update on the current knowledge of the mechanisms of shrimp quality changes, active films/coatings used to maintain shrimp quality, and smart films used to indicate the shrimp freshness during low-temperature storage. The enzymatic activities of trypsin-like protease, cathepsin B, polyphenoloxidase, prophenoloxidase, and ATPase play important roles in protein hydrolysis, formation of melanin and degradation of ATP in shrimp, resulting in muscle softening, melanosis and loss of umami. More importantly, the microbial activity is the main reason for forming off-flavor in shrimp during low-temperature storage. In addition, lipid and protein oxidation, astaxanthin degradation and cell wall damage caused by ice crystals during frozen storage can also contribute to the quality changes of shrimp. The use of active coatings/films is an effective method to maintain the shrimp quality during storage, because the encapsulated functional compounds (e.g., protein hydrolysates, essential oil and plant extracts) can act as anti-melanosis, antibacterial and antioxidant agents. In addition, smart pH-responsive films, as a simple and effective technique to monitor the quality changes of shrimp, have received increased interest in recent years, and natural pigments (e.g., anthocyanin) can be used as freshness sensors in such films to enhance its convenience for application. 

Shrimp spoilage mechanisms and functional films/coatings used to maintain and monitor its quality during storage

Shrimp is a popular internationally traded shellfish due to its unique taste, texture, and nutritional value. Shrimp is highly perishable because it has enough free amino acids, high moisture levels, non-nitrogenous compounds used for microbial growth, and melanosis. Shrimp spoilage after death is caused by various reasons, like autolysis (endogenous proteinases actions during shrimp storage), growth of spoilage microorganisms, ATP degradation, melanin formation, and lipid peroxidation. A microbial byproduct, total volatile basic nitrogen, is one of the major reasons for the generation of foul odors from shrimp spoilage. Shrimp freshness monitoring is crucial for market sellers and exporters. Traditional methods for estimating shrimp freshness are expensive and inaccessible to the general public. Sensors are rapid, sensitive, selective, and portable food toxins' detection tools, devoid of expensive instruments, skilled people, sample pretreatment, and a long detection time. This review addresses shrimp spoilage causes. The mechanisms of different stages of shrimp spoilage after death, like rigor mortis, dissolution of rigor mortis, autolysis, and microbial spoilage mechanisms, are discussed. This review highlights the last five years' advances in shrimp freshness detection sensors and indicators like colorimetric pH indicators, fluorescence sensors, electronic noses, and biosensors, their working principles, and their sensitivities. Commercially available indicators and sensors for shrimp spoilage monitoring are also discussed. A review highlighting the applications of the different sensors and indicators for monitoring shrimp freshness is unavailable to date. Challenges and future perspectives in this field are explained at the end.

A comprehensive review of the spoilage of shrimp and advances in various indicators/sensors for shrimp spoilage monitoring

Muscle deterioration caused by endogenous enzymes can greatly impact the quality of shrimp products during their processing and storage. In this study, the changes in trypsin, calpain, and cathepsin activity and their effects on muscle proteins in the intact and beheaded shrimp during 120 days of frozen storage were investigated. The results showed that the hardness, stretching force, chewiness, myofibrillar protein (MP) content, and Ca2+-ATPase activity significantly decreased in both the intact and beheaded shrimp samples with the prolonged storage period. Notably, the beheaded shrimp exhibited more stable characteristics than the intact shrimp samples throughout frozen storage. The endogenous enzyme analysis showed that the variations in the trypsin, calpain, and cathepsin activities were significantly pronounced in the intact shrimp compared to those in the beheaded samples. Furthermore, the myofibrillar fragmentation index, SDS-PAGE, and histological structure analysis revealed that the beheading treatment on the shrimp greatly inhibited the dissociation of muscle proteins during frozen storage. Our findings showed that the trypsin in the head of shrimp could be transferred to muscle tissues through the first abdominal segment during long-term storage, thus accelerating the degradation of MPs in the muscle tissues. Therefore, the beheading treatments effectively prolonged the shelf-life of stored shrimp products. 

Characterization of endogenous enzymes in sword prawn (Parapenaeopsis hardwickii) and their effects on the quality of muscle proteins during frozen storage

Properties of Pacific white shrimp (Litopenaeus vannamei) collagen and its degradation by endogenous proteinases during cold storage.

Changes in the autolysis level, muscle stability, and myofibrillar protein properties of Antarctic krill (
 Euphausia superba
 ) during refrigerated storage

Cathepsin B is a cysteine protease that has important effects on the quality of muscle products. In this study, the changes of cathepsin B activity and its relation to muscle proteins were investigated in intact and beheaded shrimp during chilled and frozen storage. The obtained results indicated that the water holding capacity (WHC), shear force, hardness, and myofibrillar protein (MP) content all significantly decreased in both the intact and beheaded shrimp samples with increasing storage period (p < 0.05). Specifically, beheading shrimp exhibited much more stable characteristics than intact shrimp samples during both chilled and frozen storage. The enzyme activity results suggested that cold temperature and storage induced the release of cathepsin B from the lysosomes to the mitochondria, sarcoplasm, and myofibrils in the muscle tissues. Furthermore, SDS-PAGE and transmission electron microscopy (TEM) analysis revealed that beheading the shrimp greatly inhibited the dissociation of shrimp muscle proteins during storage. The current findings suggest that cathepsin B located in the head of shrimp was likely transferred to the muscle through the first abdominal segment during storage, accelerating the dissociation of the muscle proteins. Therefore, beheading the shrimp was conducive to prolonging the shelf-life of stored shrimp products.

Investigation of the activity of cathepsin B in red shrimp (Solenocera crassicornis) and its relation to the quality of muscle proteins during chilled and frozen storage.

This study aimed to investigate the effect of trypsin-like protease (TLP) on the quality of muscle proteins in red shrimp (Solenocera crassicornis) during cold storage. The results indicated that the activity of TLP decreased significantly in the head of shrimp but increased significantly in the muscle tissues during the cold storage. The myofibril fragmentation index (MFI) value of intact shrimp was significantly higher than that of beheaded shrimp, while the Ca2+-ATPase activity of intact shrimp was significantly lower than that of beheaded shrimp. SDS-PAGE analysis showed that the molecular weight of purified TLP from the shrimp head was about 24 kDa, and the TLP showed high activity at 50 °C and pH 8, indicating that the TLP belongs to the trypsin family. Results from in vitro simulation experiments indicated that the process of TLP incubation significantly reduced the particle size and enlarged the distribution of myofibrillar proteins (MPs) in shrimp muscle tissues. The comparisons were made with respect to the control samples. It can be inferred that TLP migrated from the shrimp head to the muscle tissues during storage and thus promoted the degradation of MPs in red shrimp. The beheading treatment could be an effective mean to maintain better quality and extend the commercialization of shrimp products. 

Investigating the migration hypothesis: Effects of trypsin-like protease on the quality of muscle proteins of red shrimp (Solenocera crassicornis) during cold storage

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Investigation of the activity of cathepsin B in red shrimp (Solenocera crassicornis) and its relation to the quality of muscle proteins during chilled and frozen storage.

Investigating the migration hypothesis: Effects of trypsin-like protease on the quality of muscle proteins of red shrimp (Solenocera crassicornis) during cold storage