Site-specific incorporation of sodium tripolyphosphate into myofibrillar protein from mantis shrimp (Oratosquilla oratoria) promotes protein crosslinking and gel network formation

Chen, Jinyu; Ren, Yong; Zhang, Kunsheng; Xiong, Youling L.; Wang, Qing; Shang, Kun; Zhang, Dian

doi:10.1016/j.foodchem.2019.126113

Cited by 68 publications

(31 citation statements)

References 37 publications

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“…Generally, an MFI value in chicken breast meat of more than 75 could positively contribute for the enhancement of meat tenderness ( Kim et al., 2016 ). In addition, the high MFI value for AMP-treated samples, as explained by Chen et al. (2020) , might be attributed to the ability of the AMP phosphate chain to dissociate the sarcomere protein that ultimately modifies muscle cell integrity.…”

Section: Resultsmentioning

confidence: 99%

Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage

Barido

Lee

2021

Poultry Science

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A mechanism of postmortem tenderization by adenosine 5′-monophosphate ( AMP ) on spent hen meat was investigated. Breast meat samples were made into a rectangular size of 7.5 × 5 × 2 cm and grouped into 5 different treatments, followed by immersion for 24 h at 4 ± 2°C in AMP marinade solutions of 0, 15, 30, 45, and 60 mmol/L that dissolved in 0.9% (w/v) saline solution. To investigate the enzymatic changes and tenderness-related traits, samples were stored until day 5 at a temperature of 2 ± 2°C. Result showed that each increase of 15 mmol/L AMP within marinade solution remarkably improved the myofibril fragmentation index and texture properties. The upregulation of tenderness-related enzymes was found for caspase-3 at 1 to 20.4 fold and 1 to 1.2 fold higher for the cathepsin-B, while a slight effect on calpains enzyme was observed. When compared with day 0 as a reference sample, the activity of the caspase-3 enzyme was more stable, as was cathepsin-B on the ultimate storage day, while the calpains enzyme showed a declining activity even after treatment. The flavor enhancement of 2.16- to 5.10-fold seemed to be a consequence of the AMP conversion into IMP that was responsible for the intensification of the umami-like flavor. No adverse effect was observed for instrumental surface color during the postmortem period. Therefore, this study suggested that the synergistic results after AMP treatment strongly contributed to postmortem tenderization mainly through cathepsin-B and caspase-3 enzyme upregulation, which led to more myofibrillar fragmentation and structural alteration of myofibrillar protein.

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Section: Resultsmentioning

confidence: 99%

Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage

Barido

Lee

2021

Poultry Science

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“…The Fourier-transformed infrared spectra (FTIR) of the trehalose, COS, MP, MP + trehalose, and MP + COS are shown in Figure 1 . For trehalose, the peak at 3271 cm −1 is characteristic of the stretching vibration of -OH, the peak at 2928 cm −1 is the stretching vibration of C-H, the peak at 1452 cm −1 is the bending vibration of -CH, the peak at 1240 cm −1 is the stretching vibration of C-O, and the peak at 995 cm −1 is C-H connected to glycosidic bonds [ 33 ]. For COS, the characteristic peaks mainly appeared at 3255 cm −1 , 2885 cm −1 , 1623 cm −1 , 1520 cm −1 , 1418 cm −1 , and 1066 cm −1 , which were similar to trehalose.…”

Section: Resultsmentioning

confidence: 99%

Myofibrillar Protein Interacting with Trehalose Elevated the Quality of Frozen Meat

Han

et al. 2022

Foods

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This work studied the interactions between trehalose/chitooligosaccharide (COS) and myofibrillar protein (MP), and the effect of such interactions on the quality of meat after freezing was also evaluated. Fourier transform infrared spectroscopy showed that both trehalose and COS could enhance the content of hydrogen bonds of MP. Zeta potential measurement displayed trehalose/COS reduced the absolute value of the surface potential of MP. The results of Raman spectroscopy suggested that the hydrophobic residues of MP were more exposed after treatment with trehalose/COS. Thus, trehalose and COS could both interact with MP through non-covalent bonds. Subsequently, the evaluation of the effect of trehalose and COS on the physicochemical properties of frozen meat was conducted. Results showed that both trehalose and COS significantly reduced thawing loss of frozen meat, and sensory evaluation showed that trehalose had a better performance from the perspective of smell, texture, and overall consumer acceptance. In conclusion, trehalose/COS interacting with MP can reduce meat thawing loss, which might provide technical guidance in the quality control of frozen meat.

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“…24 The peak width of the CLEAs at 2900-3300 cm À1 became slight wider than that of the free lipase, which might be due to the interaction between the phosphate group and the hydroxyl group. 11,25 The characteristic peaks at 963, 905, and 551 cm À1 were due to P O, 26,27 C O P, 25 and P N, 11,25 respectively. However, there were almost no characteristic peaks at these positions for the free lipase, indicating the interaction between the amino groups or hydroxyl group of enzyme and the phosphate group of TPP.…”

Section: Sem Ftir Characterizationmentioning

confidence: 97%

“…Chen et al confirmed that the introduction of TPP led to an increase in the content of α-helical structure of myofibrillar protein. 26 Nadar et al ascertained an increase in the content of α-helix and a decrease in the content of random coil in α-amylase-CLEAs. 10 According to Cao et al, increasing in the α-helix content and decreasing in the random coil content improved the structure rigidity and stability of enzyme molecules.…”

Section: Sem Ftir Characterizationmentioning

confidence: 99%

Preparation and characterization of a nontoxic cross‐linked lipase aggregate by using sodium tripolyphosphate and chitosan

Yan

Shi

Ding

et al. 2021

J of Applied Polymer Sci

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Cross-linked enzyme aggregates (CLEAs) have the advantages of high-enzyme activity and stability, and have an application potential in food and feed processing. In order to address the food and feed safety of CLEAs and have ideal enzymatic properties, a new design of CLEAs of lipase from Aspergillus niger is developed by using sodium tripolyphosphate (TPP) as a cross-linking agent and chitosan as an auxiliary agent. The enzyme activity recovery of the developed CLEAs reaches 126%. The half-life of the CLEAs is 11.4-fold higher than that of free enzyme at the optimum reaction temperature of CLEAs. The surface structure of the CLEAs reveals cluster and porous structure. The variations of the secondary structures of the CLEAs indicate an increase of α-helix and decrease of β-sheet, β-turn, and random coil. The adding of chitosan is beneficial to enzyme activity recovery and thermal stability of the CLEAs. TPP and chitosan are safe and nontoxic, and the CLEAs prepared with TPP and chitosan is suitable for the food and feed industries.

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Site-specific incorporation of sodium tripolyphosphate into myofibrillar protein from mantis shrimp (Oratosquilla oratoria) promotes protein crosslinking and gel network formation

Cited by 68 publications

References 37 publications

Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage

Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage

Myofibrillar Protein Interacting with Trehalose Elevated the Quality of Frozen Meat

Preparation and characterization of a nontoxic cross‐linked lipase aggregate by using sodium tripolyphosphate and chitosan

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