Gelatinolytic Serine Proteinases From the Wing Muscle of Red Stingray

Bae, Inwoo; Shimazoe, Yoshimi; Yoshida, Asami; Yamaguchi, Atsuko; Osatomi, Kiyoshi; Hara, Kenji

doi:10.1111/j.1745-4514.2010.00338.x

Cited by 7 publications

(11 citation statements)

References 27 publications

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“…Gelatinolytic serine proteinases were detected in the red stingray wing muscle by gelatin zymography [7]. In our previous study, we also found gelatinolytic enzymes including a trypsin-type serine proteinase (G1) and two metalloproteinases (G2 and G3) in red sea bream muscle [8].…”

Section: Introductionmentioning

confidence: 76%

“…The solubilization of type V collagen was reported to be involved in softening of sardine muscle during chilled storage [3]. Also, gelatinolytic enzymes which degrades gelatin, denatured collagen, have been investigated in various fish [4][5][6][7][8]. Metalloproteinases and serine proteinases have been detected in various organs of yellowtail [4] and Atlantic cod [5].…”

Section: Introductionmentioning

confidence: 99%

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A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood

et al. 2009

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Collagen degradation is known to be involved in post mortem tenderization of fish muscle. A serine proteinase which is assumed to be related to collagen degradation after fish death was purified from sarcoplasmic fraction of red sea bream Pagrus major by ammonium sulfate fractionation and column chromatographies on Sephacryl S-300, Q Sepharose and Phenyl Sepharose CL-4B. The enzyme hydrolyzed gelatin and was obtained as a protein band of approximately 38 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing condition. N-terminal amino acid sequence of the enzyme was determined for 32 residues. The protein having the same N-terminal amino acid sequence of the enzyme for 10 residues was purified from the serum of red sea bream and showed the same characteristics as the enzyme. Therefore, the serine proteinase was suggested to migrate from blood to muscle and to degrade muscle proteins after fish death.

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Section: Introductionmentioning

confidence: 76%

Section: Introductionmentioning

confidence: 99%

A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood

et al. 2009

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“…2), which is similar to the gelatinolytic proteinases from common carp muscle (Wu et al . 2008), red stingray muscle (Bae et al . 2010) and red sea bream muscle (Wu et al .…”

Section: Discussionmentioning

confidence: 99%

“…2000), Atlantic cod ( Gadus morhua ), spotted wolfish ( Anarhichas minor ) and Atlantic salmon ( Salmo salar ) (Lødemel and Olsen 2003). Gelatinolytic serine proteinases were detected in many fish species by gelatin zymography, including red stingray wing ( Dasyatis akajei ) (Bae et al . 2010), red sea bream ( Pagrus major ) (Yoshida et al .…”

Section: Introductionmentioning

confidence: 99%

“…(Bracho and Haard 1995), muscles of ayu (Plecoglossus altivelis) (Kubota et al 2000), Atlantic cod (Gadus morhua), spotted wolfish (Anarhichas minor) and Atlantic salmon (Salmo salar) (Lødemel and Olsen 2003). Gelatinolytic serine proteinases were detected in many fish species by gelatin zymography, including red stingray wing (Dasyatis akajei) (Bae et al 2010), red sea bream (Pagrus major) (Yoshida et al 2009;Wu et al 2010a), ayu (Plecoglossus altivelis) (Kubota et al 2000) and so on.…”

Section: Introductionmentioning

confidence: 99%

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PARTIAL CHARACTERIZATION OF GELATINOLYTIC PROTEINASES FROM THE SKELETAL MUSCLE OF GRASS CARP (CTENOPHARYNGODON IDELLUS)

Chen

Cai

et al. 2011

Journal of Food Biochemistry

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Two gelatin‐hydrolyzing proteinases with molecular masses of 85 and 72 kDa in the sarcoplasmic fraction of grass carp muscle were detected using gelatin zymography. The gelatinolytic activity in dark muscle was obviously higher than that in white muscle. Optimum pH and temperature of the two enzymes were around 8.0 and 40C. The proteinase inhibitor leupeptin entirely inhibited GP‐I, but E‐64 did not inhibit it. Only EDTA completely suppressed GP‐II, and Ca2+ is essential for the activity of GP‐II. All these facts indicated that GP‐I was matrix serine proteinase, and GP‐II was matrix metalloproteinase. When grass carp muscle was stored for 15 days at 4C, GP‐I and GP‐II were detected during the whole stored period. Therefore, the two gelatinolytic proteinases may be proposed to participate in the tenderization of fish muscle during postmortem stage. PRACTICAL APPLICATIONS Gelatinolytic proteinases from grass carp can effectively hydrolyze gelatin. These proteinases may be used to hydrolyze gelatin for peptide that has been added to food products as additive to improve texture. In addition, this study will be significant to learn and comparatively study the properties of gelatinolytic proteinases in fresh fish. Furthermore, this study will surely be beneficial for understanding the mechanism of postmortem tenderization of fish muscle.

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

et al. 2021

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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.

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Gelatinolytic Serine Proteinases From the Wing Muscle of Red Stingray

Cited by 7 publications

References 27 publications

A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood

A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood

PARTIAL CHARACTERIZATION OF GELATINOLYTIC PROTEINASES FROM THE SKELETAL MUSCLE OF GRASS CARP (CTENOPHARYNGODON IDELLUS)

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

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