Participation of cathepsin L in modori phenomenon in carp (Cyprinus carpio) surimi gel

Hu, Yaqin; Ji, Rong; Jiang, Hai Yan; Zhang, Jinjie; Chen, Jianchu; Ye, Xingqian

doi:10.1016/j.foodchem.2012.04.060

Cited by 37 publications

(33 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Based on the above‐mentioned results, the cathepsin L in sturgeon surimi exhibited the highest activity at 40 °C, which seemed to be a partial reason that the modori phenomenon of sturgeon surimi occurred at 40 °C. According to the previous reports, the modori phenomenon of other fish surimi occurred at 50 to 70 °C, suggesting that the modori phenomenon of surimi has high species specificity (Hu et al., ; Singh & Benjakul, ).…”

Section: Resultsmentioning

confidence: 87%

“…Similarly, Hu et al. () found that when the purified cathepsin Lfrom the back muscle of carp ( Cyprinus carpio ) was added to the carp surimi gels, the MHC was rapidly hydrolyzed and the breaking force was reduced by 24.33%. Cathepsin L could strongly bind to muscle proteins, and contributed to degradation of surimi gel texture at 40 °C, resulting in rapid and severe degradation of myofibrillar proteins, particularly MHC, and leading to a weakened gel with poor WHC.…”

Section: Resultsmentioning

confidence: 92%

See 1 more Smart Citation

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Tang

Feng

Gao

et al. 2019

Journal of Food Science

View full text Add to dashboard Cite

Sturgeon meat has been found to be suitable as surimi raw materials. The present study determined the modori phenomenon in sturgeon surimi gels and identified its relationship with cathepsins. In all heat-treated gels (25 to 90°C, at 5°C intervals), the 40°C-incubated sturgeon surimi gel showed the weakest gel properties and water-holding capacity (P < 0.05), a rough protein gel network under SEM, and the highest protein solubility and trichloroacetic acid-soluble peptides content (P < 0.05). SDS-PAGE indicated that the myosin heavy chain band of sturgeon surimi gels was almost completely degraded at 40°C. Moreover, the highest cathepsin L activity was observed in 40°C-treated sturgeon surimi gels (P < 0.05). Our results suggested that the modori phenomenon in sturgeon surimi gels occurred at 40°C, which was partially attributed to cathepsin L, thereby allowing for the better exploitation and utilization of sturgeon surimi.

show abstract

Section: Resultsmentioning

confidence: 87%

Section: Resultsmentioning

confidence: 92%

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Tang

Feng

Gao

et al. 2019

Journal of Food Science

View full text Add to dashboard Cite

show abstract

“…Endogenous proteases play a role in the textural properties of mince or surimi gel. When purified cathepsin L from dorsal muscle of carp ( Cyprinus carpio ) was incorporated into carp surimi gel, MHC was drastically hydrolyzed, and the breaking force was decreased by 24.33% (Hu et al., ). Similarly, cathepsins L and B from silver carp muscle reduced gel strength by a respective 38% and 25% compared to the control.…”

Section: Postmortem Proteolysis Of Aquatic Animal Musclesmentioning

confidence: 99%

Proteolysis and Its Control Using Protease Inhibitors in Fish and Fish Products: A Review

Singh

Benjakul

2018

Comp Rev Food Sci Food Safe

147

101

View full text Add to dashboard Cite

Texture is one of the food quality attributes affecting the consumer's acceptability and the market value. Fish and shellfish undergo weakening or softening of muscle, particularly during extended storage under inappropriate conditions. The phenomenon is governed by endogenous proteases, both digestive and muscle proteases. Proteases present in the gastrointestinal tract that leach out to muscle tissue can induce proteolysis of myofibrillar and collagenous proteins. Furthermore, the muscle proteins present in gels fabricated from fish or shellfish meat also encounter degradation during thermal processing. Endogenous heat-activated proteases strongly bind to muscle proteins and are activated during heating, thereby degrading myofibrillar proteins, which are abundant in muscle tissue. This deterioration of the proteins directly leads to a weakened gel with poor water-holding capacity. Both cysteine and serine proteases are responsible for the degradation of myofibrillar proteins in several aquatic animals. Effective pretreatment of fish and shellfish, as well as the use of food-grade protease inhibitors (PIs), have been implemented to inactivate endogenous muscle and digestive proteases. For this review, proteolysis of muscle proteins and its control by food-grade PIs are revisited. Improved and effective lowering of proteolysis should be gained, thereby maintaining the quality of fish and their products.

show abstract

“…However, when surimi is exposed to temperatures of 40-60 • C, its protein components, Molecules 2021, 26,1901 2 of 11 particularly MHC, may be degraded. The resulting weak gel tends to disintegrate, reducing product quality and value; this is known as the modori phenomenon [11,12]. The degradation is caused by endogenous proteases in fish muscle, particularly cysteine-and serine-type proteases [13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel

Kwon

Chang

2021

Molecules

View full text Add to dashboard Cite

We investigated the effect of endogenous cathepsin L on surimi gel produced from olive flounder (Paralichthys olivaceus). The amino acid sequences of six proteins predicted or identified as cathepsin L were obtained from the olive flounder genome database, and a phylogenetic analysis was conducted. Next, cathepsin L activity toward N-α-benzyloxycarbonyl-l-phenylalanyl-l-arginine-(7-amino-4-methylcoumarin) (Z-F-R-AMC) was detected in crude olive flounder extract and a crude enzyme preparation. A considerable decrease in the level of myosin heavy chain (MHC) in surimi occurred during autolysis at 60 °C. In contrast, the levels of actin, troponin-T, and tropomyosin decreased only slightly. To prevent protein degradation by cathepsin L, a protease inhibitor was added to surimi. In the presence of 1.0% protease inhibitor, the autolysis of olive flounder surimi at 60 °C was inhibited by 12.2%; the degree of inhibition increased to 44.2% as the inhibitor concentration increased to 3.0%. In addition, the deformation and hardness of modori gel increased as the inhibitor concentration increased to 2.0%. Therefore, cathepsin L plays an important role in protein degradation in surimi, and the quality of surimi gel could be enhanced by inhibiting its activity.

show abstract

Participation of cathepsin L in modori phenomenon in carp (Cyprinus carpio) surimi gel

Cited by 37 publications

References 21 publications

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Proteolysis and Its Control Using Protease Inhibitors in Fish and Fish Products: A Review

Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel

Contact Info

Product

Resources

About