Inhibitory effect of edible natural compounds with di- and tri-carboxyl moiety on endogenous protease inducing disassembly and degradation of myofibrils from grass carp (Ctenopharyngodon idella)

Ge, Lihong; Zhao, Nan; Miao, Yuzhi; Zhang, Siyuan; Zhao, Minhui; Luo, Yongyuan; Lai, Haimei; Huang, Yatao; Wang, Yali

doi:10.1016/j.foodres.2020.109457

Cited by 7 publications

(12 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…According to Ge, et al . (2020), 5 grams of fillets were mixed with 3 volumes of distilled water. After homogenisation at 12,000 rpm for 1 min and extraction for 10 min at 4 °C, the mixture was centrifuged at 14600 g , 4 °C for 20 min, with obtained supernatant being crude enzyme.…”

Section: Preparation Of Crude Enzyme and Enzyme Activity Assaymentioning

confidence: 99%

“…Contents of heat shock protein (HSP) were measured according to Ge, et al . (2020). After dilution of myofibrils to 4 μg/mL with coating buffer (10 mM Na 2 HPO4, 15 mM NaCl, pH 7.4), the HSP90 and HSP27 contents in extracted myofibrils were measured by enzyme‐linked immunosorbent assay using anti‐HSP90 and anti‐HSP27 (Proteintech, Shanghai, China).…”

Section: Concentration Of Heat Shock Protein In Myofibrilsmentioning

confidence: 99%

“…3a showed the cathepsin B activity of fish treated with different di‐ and tri‐carboxylic acids. All the tested carboxylic acids were able to inhibit endogenous cysteine proteases of grass carp fillets, which certified the effectiveness of these compounds reported by previous in vitro studies (Manohar, et al ., 2018; Ge, et al ., 2020). The most excellent inhibition towards cathepsin B was exhibited by citric acid, maleic acid, fumaric acid and tartaric acid, with a decline of cathepsin activity by 90%.…”

Section: Endogenous Cathepsin Activitiesmentioning

confidence: 99%

“…However, aspartic acid and glutamic acid did not alter the fragmentation of MHC and actin, as revealed by the lowest band density of intact MHC and actin not significantly different from that of control. Previous in vitro studies have differentiated the contribution of cathepsin B and L in myofibrillar degradation, with cathepsin B responsible for MHC degradation and cathepsin L responsible for actin degradation (Ge, et al ., 2018a, 2020). Hence, the suppressed myofibrillar degradation (MHC & actin) of fish fillets by treatments with di‐ and tri‐carboxylic acids was in correspondence with their inhibitory effect on cathepsin B and B + L activities (Fig.…”

Section: Myofibrillar Degradationmentioning

confidence: 99%

See 3 more Smart Citations

Inhibition of endogenous protease activity and protection of histomorphical integrity during refrigerated storage of grass carp fillets by treatment with natural edible di‐ and tri‐carboxylic acids

Huang

et al. 2022

Int J of Food Sci Tech

Self Cite

View full text Add to dashboard Cite

Summary In this study, by dipping grass carp fillets with 10 mM di‐ and tri‐carboxylic acid solutions individually before storage at 4 °C for 10 days, the application potential of these acids in mitigating softening of fish was investigated through analysing shear force, pH, endogenous cathepsin activities, myofibrillar proteolysis and histomorphological characteristics. The results suggested that maleic acid, fumaric acid and tartaric acid were significantly effective against softening of grass carp muscle, as shown by shear force 26%–31% higher than that of control after storage. Acid treatments led to a decline in the pH of muscle. Besides, the inhibitory effect of these acids on cathepsins was demonstrated by activity reduction by 20%–90%. Further, sodium dodecyl sulphate–polyacrylamide gel electrophoresis and heat shock protein (HSP) analysis supported the protection of these acids against degradation and dissociation of myosin and actin through suppressing HSP loss. Moreover, histomorphological images with higher intensity of acridine orange fluorescence in muscle revealed the improvement of tissue integrity by acid treatments. The inhibitory potential of these acids in suppressing softening of fish muscle is particularly relevant to their capacity of mitigating cathepsin‐induced proteolysis and improving lysosome stability. Therefore, di‐ and tri‐carboxylic acids could play pleiotropic functions in the quality control of fish fillets.

show abstract

Section: Preparation Of Crude Enzyme and Enzyme Activity Assaymentioning

confidence: 99%

Section: Concentration Of Heat Shock Protein In Myofibrilsmentioning

confidence: 99%

Section: Endogenous Cathepsin Activitiesmentioning

confidence: 99%

Section: Myofibrillar Degradationmentioning

confidence: 99%

See 2 more Smart Citations

Inhibition of endogenous protease activity and protection of histomorphical integrity during refrigerated storage of grass carp fillets by treatment with natural edible di‐ and tri‐carboxylic acids

Huang

et al. 2022

Int J of Food Sci Tech

Self Cite

View full text Add to dashboard Cite

show abstract

“…Softening is defined as the phenomenon in which the weakened intramuscular connective tissues (IMCTs) lose their ability to connect muscle fibers, leading to fillet gaping 4 . It is generally recognized that softening is a consequence of the hydrolysis of structural elements, including collagen and myofibrillar proteins 5,6 . Collagen, the main component of IMCTs, provides networks integrating muscle fibers and plays a critical role in the mechanical properties 7,8 .…”

Section: Introductionmentioning

confidence: 99%

Assessment of gelatinolytic proteinases in chilled grass carp (Ctenopharyngodon idellus) fillets: characterization and contribution to texture softening

et al. 2021

View full text Add to dashboard Cite

BACKGROUND Texture softening is always a problem during chilling of grass carp fillets. To solve this problem and provide for better quality of flesh, understanding the mechanism of softening is necessary. Gelatinolytic proteinases are suspected to play an essential role in the disintegration of collagen in softening of fish flesh. In the present study, the types and contribution of gelatinolytic proteinases in chilled fillets were investigated. RESULTS Four active bands (G1, 250 kDa; G2, 68 kDa; G3, 66 kDa; G4, 29 kDa) of gelatinolytic proteinases were identified in grass carp fillets by gelatin zymography. The effect of inhibitors and metal ions revealed that G1 was possibly a serine proteinase, G2 and G3 were calcium‐dependent metalloproteinases and G4 was a cysteine proteinase. The effect of the inhibitors phenylmethanesulfonyl fluoride (PMSF), l‐3‐carboxy‐trans‐2,3‐epoxy‐propionyl‐l‐leucine‐4‐guanidinobutylamide (E‐64) and 1,10‐phenanthroline (Phen) on chilled fillets revealed that gelatinolytic proteinase activities were significantly suppressed. Collagen solubility indicated that metalloproteinase and serine proteinase played critical roles in collagen breakdown during the first 3 days, and cysteine proteinase revealed its effect after 3 days. Meanwhile, during chilled storage for 11 days, the final values of shear force increased 19.68% and 24.33% in PMSF and E‐64 treatments when compared to control fillets respectively, whereas the increase after Phen treatment was 49.89%. CONCLUSION Our study concluded that the disintegration of collagen in post‐mortem softening of grass carp fillets was mainly mediated by metalloproteinase and to a lesser extent by serine proteinase and cysteine proteinase. © 2021 Society of Chemical Industry.

show abstract

Phosphoproteomic insight into the changes in structural proteins of muscle architecture associated with texture softening of grass carp (Ctenopharyngodon idella) fillets during chilling storage

Wang

et al. 2023

Food Chemistry

View full text Add to dashboard Cite

Inhibitory effect of edible natural compounds with di- and tri-carboxyl moiety on endogenous protease inducing disassembly and degradation of myofibrils from grass carp (Ctenopharyngodon idella)

Cited by 7 publications

References 28 publications

Inhibition of endogenous protease activity and protection of histomorphical integrity during refrigerated storage of grass carp fillets by treatment with natural edible di‐ and tri‐carboxylic acids

Inhibition of endogenous protease activity and protection of histomorphical integrity during refrigerated storage of grass carp fillets by treatment with natural edible di‐ and tri‐carboxylic acids

Assessment of gelatinolytic proteinases in chilled grass carp (Ctenopharyngodon idellus) fillets: characterization and contribution to texture softening

Phosphoproteomic insight into the changes in structural proteins of muscle architecture associated with texture softening of grass carp (Ctenopharyngodon idella) fillets during chilling storage

Contact Info

Product

Resources

About