Localization of trypsin-like protease in postmortem tissue of white shrimp (Litopenaeus vannamei) and its effect in muscle softening

Peng, Yuanhuai; Chen, Shiyan; Ji, Hongwu; Liu, Shucheng

doi:10.1016/j.foodchem.2019.03.147

Cited by 22 publications

(12 citation statements)

References 38 publications

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“…Peng et al. (2019) found that a trypsin‐like protease was released from the shrimp hepatopancreas and likely migrated to the first segment and then proceeded to the other sections during chilled storage, thus causing the enzymatic dissociation/degradation of the muscle proteins in intact shrimp to occur to a much greater extent than in beheaded shrimp. Herein, the article inferred that the amount of extracted MPs was remarkably reduced by series proteases (e.g., cathepsin B and L) in the tissues during cold storage.…”

Section: Resultsmentioning

confidence: 99%

“…Additionally, previous study speculated that endogenous protease (e.g., trypsin‐like protease) located in the hepatopancreas of shrimp might transfer to the shrimp muscle after postmortem (Peng et al., 2019). The release and/or transfer of protease in shrimp were most likely responsible for the deterioration of muscle proteins during chilled and frozen storage.…”

Section: Introductionmentioning

confidence: 99%

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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

Zhou

et al. 2022

Journal of Food Science

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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.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Zhou

et al. 2022

Journal of Food Science

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“…The best working pH for most umami substances was 6–7 [ 42 , 43 ]. Meanwhile, endogenous protease plays a key role in the degradation of protein and nucleotide-flavor compounds [ 44 ]. The changes in pH and enzymatic activity of SH during autolysis were studied ( Figure 5 ).…”

Section: Resultsmentioning

confidence: 99%

“…In addition, the trend of change in enzyme activity was similar to pH ( Figure 5 ). The native protein of SH could be degraded rapidly by endogenous protease in digestive organs during autolysis [ 44 ]. Therefore, the total free amino acids were increased in SH ( Figure 2 ).…”

Section: Resultsmentioning

confidence: 99%

Change Regularity of Taste and the Performance of Endogenous Proteases in Shrimp (Penaens vannamei) Head during Autolysis

Zhao

Gao

et al. 2021

Foods

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This study evaluated the food safety and proximate composition of shrimp head (SH). Potentially toxic elements in SH were below European Union legislation limits. SH had a high content of tasting amino acids (sweet and umami amino acids was 57%) and a high content of functional amino acids (essential amino acids was 37%). Moreover, the changes of flavor and key umami molecules in SH were studied by sensory evaluation, electronic tongue, electronic nose, automated amino acid analyzer, and high performance liquid chromatography (HPLC). The results showed that the significant difference of flavor in SH happened during autolysis. SH with autolysis had the best umami taste at 6 h, which may result from the synergistic work of free amino acids and nucleotide related compounds. Additionally, the performance of endogenous proteases in SH was investigated to efficiently analyze autolysis. The optimum pH and temperature of endogenous proteases in SH were 7.5 and 50 °C, respectively. The autolysis of SH depends on two endogenous proteases (~50 kDa and ~75 kDa). These results suggest that the formation of flavor in SH during autolysis can be controlled, which could provide guidance for SH recycle. SH could consider as one of the food materials for producing condiments.

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“…The analysis of protease activity is an important step in the research and application of protease development and validation of a simple titration method for studying the heat-activated; endogenous protease in arrow tooth flounder fillet mince is described. Protease activity has been detected by the fluorescence method, , but detection based on calorimetry, mass spectrometry (MS), immunoassay, electrophoresis, , amperometry, optics, , and so on.…”

Section: Introductionmentioning

confidence: 99%

Novel Method for the Quantitative Analysis of Protease Activity: The Casein Plate Method and Its Applications

et al. 2021

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No simple methods are used for the quantitative analysis of the protease activity in colored food up till now. Thus, this study aims to establish a new and simple method for the quantitative detection of protease activity, especially in colored food. The detection accuracy, detection limit, and repeatability of the casein plate method were analyzed. Then, the application of the casein plate method in sample detection and recovery was further evaluated. The results showed that the casein plate method for the quantitative detection of protease activity has high accuracy, high precision, and low detection limit. The recoveries of eight kinds of colored samples were in the range of 92.26−97.84%, and the relative standard deviation (RSD) was in the range of 3.56−10.88%. The results of the casein plate method exhibited high accuracy. This indicated that the method was suitable for the detection of colored samples. The casein plate method for the quantitative detection of protease activity is simple. The newly constructed casein plate method has broad potential application value in food industry, especially for the detection of dark food.

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Localization of trypsin-like protease in postmortem tissue of white shrimp (Litopenaeus vannamei) and its effect in muscle softening

Cited by 22 publications

References 38 publications

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

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

Change Regularity of Taste and the Performance of Endogenous Proteases in Shrimp (Penaens vannamei) Head during Autolysis

Novel Method for the Quantitative Analysis of Protease Activity: The Casein Plate Method and Its Applications

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