메뉴 건너뛰기




Volumn 78, Issue 12, 2013, Pages

Activity of endogenous muscle proteases from 4 australian underutilized fish species as affected by ionic strength, pH, and temperature

Author keywords

Calpain like; Cathepsins; Ionic strength; PH; Temperature

Indexed keywords

KATHETOSTOMA GIGANTEUM; MORA MORO; SERIOLELLA POROSA;

EID: 84890200821     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/1750-3841.12303     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 84874941809 scopus 로고    scopus 로고
    • Proteolytic activities in fillets of selected underutilized Australian fish species
    • Ahmed Z, Donkor O, Street WA, Vasiljevic T. 2013. Proteolytic activities in fillets of selected underutilized Australian fish species. Food Chem 140(1-2):238-44.
    • (2013) Food Chem , vol.140 , Issue.1-2 , pp. 238-244
    • Ahmed, Z.1    Donkor, O.2    Street, W.A.3    Vasiljevic, T.4
  • 3
    • 0030037942 scopus 로고    scopus 로고
    • Spoilage and shelf-life extension of fresh fish and shellfish
    • Ashie INA, Smith JP, Simpson BK. 1996. Spoilage and shelf-life extension of fresh fish and shellfish. Crit Rev Food Sci Nutr 36(1-2):87-121.
    • (1996) Crit Rev Food Sci Nutr , vol.36 , Issue.1-2 , pp. 87-121
    • Ashie, I.N.A.1    Smith, J.P.2    Simpson, B.K.3
  • 5
    • 77349099669 scopus 로고    scopus 로고
    • Evidence of in vivo satietogen effect and control of food intake of smooth hound (Mustelus mustelus) muscle protein hydrolysate in rats
    • Bougatef A, Ravallec R, Nedjar-Arroume N, Barkia A, Guillochon D, Nasri M. 2010. Evidence of in vivo satietogen effect and control of food intake of smooth hound (Mustelus mustelus) muscle protein hydrolysate in rats. J Funct Foods 2(1):10-6.
    • (2010) J Funct Foods , vol.2 , Issue.1 , pp. 10-16
    • Bougatef, A.1    Ravallec, R.2    Nedjar-Arroume, N.3    Barkia, A.4    Guillochon, D.5    Nasri, M.6
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 46949088271 scopus 로고    scopus 로고
    • Peptides from fish and crustacean by-products hydrolysates stimulate cholecystokinin release in STC-1 cells
    • Cudennec B, Ravallec-Plé R, Courois E, Fouchereau-Peron M. 2008. Peptides from fish and crustacean by-products hydrolysates stimulate cholecystokinin release in STC-1 cells. Food Chem 111(4):970-5.
    • (2008) Food Chem , vol.111 , Issue.4 , pp. 970-975
    • Cudennec, B.1    Ravallec-Plé, R.2    Courois, E.3    Fouchereau-Peron, M.4
  • 9
    • 33646572566 scopus 로고    scopus 로고
    • Immunomodulating capacity of commercial fish protein hydrolysate for diet supplementation
    • Duarte J, Vinderola G, Ritz B, Perdigón G, Matar C. 2006. Immunomodulating capacity of commercial fish protein hydrolysate for diet supplementation. Immunobiology 211(5):341-50.
    • (2006) Immunobiology , vol.211 , Issue.5 , pp. 341-350
    • Duarte, J.1    Vinderola, G.2    Ritz, B.3    Perdigón, G.4    Matar, C.5
  • 10
    • 41149111706 scopus 로고    scopus 로고
    • Computer stimulation of animal proteins proteolysis in the aspect of bioactive peptides obtaining
    • Dziuba J, Iwaniaka A, Darewicz M, Niklewicz M. 2002. Computer stimulation of animal proteins proteolysis in the aspect of bioactive peptides obtaining. Pol J Nat Sci 10(1):209-22.
    • (2002) Pol J Nat Sci , vol.10 , Issue.1 , pp. 209-222
    • Dziuba, J.1    Iwaniaka, A.2    Darewicz, M.3    Niklewicz, M.4
  • 11
    • 84864624471 scopus 로고    scopus 로고
    • Food and Agriculture Organization of the United Nations. . Rome: FAO.
    • Food and Agriculture Organization of the United Nations. 2012. The State of World Fisheries and Aquaculture-2012. Rome: FAO.
    • (2012) The State of World Fisheries and Aquaculture-2012
  • 12
    • 0034264486 scopus 로고    scopus 로고
    • Ionic strength-induced inactivation of μ-calpain in postmortem muscle
    • Geesink GH, Koohmaraie M. 2000. Ionic strength-induced inactivation of μ-calpain in postmortem muscle. J Anim Sci 78(9):2336-43.
    • (2000) J Anim Sci , vol.78 , Issue.9 , pp. 2336-2343
    • Geesink, G.H.1    Koohmaraie, M.2
  • 14
    • 49049103352 scopus 로고    scopus 로고
    • Activity of aspargate (Cathepsin D), cysteine proteases (Cathepsins B, B + L, and H), and matrix metallopeptidase (Collagenase) and their influence on protein and water-holding capacity of muscle in commercially farmed Atlantic halibut (Hippoglossus hippoglossus L.)
    • Hagen Ø, Solberg C, Johnston IA. 2008. Activity of aspargate (Cathepsin D), cysteine proteases (Cathepsins B, B + L, and H), and matrix metallopeptidase (Collagenase) and their influence on protein and water-holding capacity of muscle in commercially farmed Atlantic halibut (Hippoglossus hippoglossus L.). J Agric Food Chem 56(14):5953-9.
    • (2008) J Agric Food Chem , vol.56 , Issue.14 , pp. 5953-5959
    • Hagen, Ø.1    Solberg, C.2    Johnston, I.A.3
  • 16
    • 77954387385 scopus 로고    scopus 로고
    • Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization
    • Huff Lonergan E, Zhang W, Lonergan SM. 2010. Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization. Meat Sci 86(1):184-95.
    • (2010) Meat Sci , vol.86 , Issue.1 , pp. 184-195
    • Huff Lonergan, E.1    Zhang, W.2    Lonergan, S.M.3
  • 17
    • 34248999164 scopus 로고    scopus 로고
    • Effects of temperature abuse on textural properties and proteolytic activities during post mortem iced storage of farmed Atlantic cod (Gadus morhua)
    • Hultmann L, Rustad T. 2007. Effects of temperature abuse on textural properties and proteolytic activities during post mortem iced storage of farmed Atlantic cod (Gadus morhua). Food Chem 104(4):1687-97.
    • (2007) Food Chem , vol.104 , Issue.4 , pp. 1687-1697
    • Hultmann, L.1    Rustad, T.2
  • 19
    • 0027356908 scopus 로고
    • Effect of pH and ionic strength on bovine m-calpain and calpastatin activity
    • Kendall TL, Koohmaraie M, Arbona JR, Williams SE, Young LL. 1993. Effect of pH and ionic strength on bovine m-calpain and calpastatin activity. J Anim Sci 71(1):96-104.
    • (1993) J Anim Sci , vol.71 , Issue.1 , pp. 96-104
    • Kendall, T.L.1    Koohmaraie, M.2    Arbona, J.R.3    Williams, S.E.4    Young, L.L.5
  • 20
    • 0034041821 scopus 로고    scopus 로고
    • Neutral calcium-activated proteases from European sea bass (Dicentrarchus labrax L.) muscle: polymorphism and biochemical studies
    • Ladrat C, Chaplet M, Verrez-Bagnis V, Noël J, Fleurence J. 2000. Neutral calcium-activated proteases from European sea bass (Dicentrarchus labrax L.) muscle: polymorphism and biochemical studies. Comp Biochem Physiol B 125(1):83-95.
    • (2000) Comp Biochem Physiol B , vol.125 , Issue.1 , pp. 83-95
    • Ladrat, C.1    Chaplet, M.2    Verrez-Bagnis, V.3    Noël, J.4    Fleurence, J.5
  • 21
    • 0037409612 scopus 로고    scopus 로고
    • In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): effects of cathepsins B, D and L
    • Ladrat C, Verrez-Bagnis V, Noël J, Fleurence J. 2003. In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): effects of cathepsins B, D and L. Food Chem 81(4):517-25.
    • (2003) Food Chem , vol.81 , Issue.4 , pp. 517-525
    • Ladrat, C.1    Verrez-Bagnis, V.2    Noël, J.3    Fleurence, J.4
  • 22
    • 7044234868 scopus 로고    scopus 로고
    • Effects of high-pressure processing on proteolytic enzymes and proteins in cold-smoked salmon during refrigerated storage
    • Lakshmanan R, Patterson MF, Piggott JR. 2005. Effects of high-pressure processing on proteolytic enzymes and proteins in cold-smoked salmon during refrigerated storage. Food Chem 90(4):541-8.
    • (2005) Food Chem , vol.90 , Issue.4 , pp. 541-548
    • Lakshmanan, R.1    Patterson, M.F.2    Piggott, J.R.3
  • 23
    • 22144449926 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on μ- and m-calpain inhibition by calpastatin
    • Maddock KR, Huff-Lonergan E, Rowe LJ, Lonergan SM. 2005. Effect of pH and ionic strength on μ- and m-calpain inhibition by calpastatin. J Anim Sci 83(6):1370-6.
    • (2005) J Anim Sci , vol.83 , Issue.6 , pp. 1370-1376
    • Maddock, K.R.1    Huff-Lonergan, E.2    Rowe, L.J.3    Lonergan, S.M.4
  • 24
    • 1842783296 scopus 로고    scopus 로고
    • ATPase activity, surface hydrophobicity, sulfhydryl content and protein degradation in refrigerated seabass muscle in modified atmosphere packaging
    • Masniyom P, Benjakul S, Visessanguan W. 2004. ATPase activity, surface hydrophobicity, sulfhydryl content and protein degradation in refrigerated seabass muscle in modified atmosphere packaging. J Food Biochem 28(1):43-60.
    • (2004) J Food Biochem , vol.28 , Issue.1 , pp. 43-60
    • Masniyom, P.1    Benjakul, S.2    Visessanguan, W.3
  • 25
    • 57549113122 scopus 로고    scopus 로고
    • Underutilised fish as sources of bioactive peptides with potential health benefits
    • Medenieks L, Vasiljevic T. 2008. Underutilised fish as sources of bioactive peptides with potential health benefits. Food Aust 60(12):581-8.
    • (2008) Food Aust , vol.60 , Issue.12 , pp. 581-588
    • Medenieks, L.1    Vasiljevic, T.2
  • 26
    • 79952353155 scopus 로고    scopus 로고
    • Bovine meat proteins as potential precursors of biologically active peptides - a computational study based on the BIOPEP database
    • Minkiewicz P, Dziuba J, Michalska J. 2011. Bovine meat proteins as potential precursors of biologically active peptides - a computational study based on the BIOPEP database. Food Sci Technol Int 17(1):39-45.
    • (2011) Food Sci Technol Int , vol.17 , Issue.1 , pp. 39-45
    • Minkiewicz, P.1    Dziuba, J.2    Michalska, J.3
  • 27
    • 0031920920 scopus 로고    scopus 로고
    • Proteolytic degradation of myofibrillar components by carp cathepsin L
    • Ogata H, Aranishi F, Hara K, Osatomi K, Ishihara T. 1998. Proteolytic degradation of myofibrillar components by carp cathepsin L. J Sci Food Agric 76(4):499-504.
    • (1998) J Sci Food Agric , vol.76 , Issue.4 , pp. 499-504
    • Ogata, H.1    Aranishi, F.2    Hara, K.3    Osatomi, K.4    Ishihara, T.5
  • 28
    • 0026539218 scopus 로고
    • Proteolytic and physicochemical mechanisms involved in meat texture development
    • Ouali A. 1992. Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie 74(3):251-65.
    • (1992) Biochimie , vol.74 , Issue.3 , pp. 251-265
    • Ouali, A.1
  • 30
    • 0030355661 scopus 로고    scopus 로고
    • Comparison of cathepsin B, D, H and L activity in four species of Pacific fish
    • Porter R, Koury B, Stone F. 1996. Comparison of cathepsin B, D, H and L activity in four species of Pacific fish. J Food Biochem 19(6):429-42.
    • (1996) J Food Biochem , vol.19 , Issue.6 , pp. 429-442
    • Porter, R.1    Koury, B.2    Stone, F.3
  • 32
    • 36148980450 scopus 로고    scopus 로고
    • Autolysis-assisted production of fish protein hydrolysates with antioxidant properties from Pacific hake (Merluccius productus)
    • Samaranayaka AGP, Li-Chan ECY. 2008. Autolysis-assisted production of fish protein hydrolysates with antioxidant properties from Pacific hake (Merluccius productus). Food Chem 107(2):768-76.
    • (2008) Food Chem , vol.107 , Issue.2 , pp. 768-776
    • Samaranayaka, A.G.P.1    Li-Chan, E.C.Y.2
  • 33
    • 0002114424 scopus 로고
    • Comparison of calpain and cathepsin (B, L and D) activities during dry-cured ham processing from heavy and light large white pigs
    • Sárraga C, Gil M, García-Regueiro J. 1993. Comparison of calpain and cathepsin (B, L and D) activities during dry-cured ham processing from heavy and light large white pigs. J Sci Food Agric 62(1):71-5.
    • (1993) J Sci Food Agric , vol.62 , Issue.1 , pp. 71-75
    • Sárraga, C.1    Gil, M.2    García-Regueiro, J.3
  • 34
    • 6944221879 scopus 로고    scopus 로고
    • Bioavailability of angiotensin I converting enzyme inhibitory peptides
    • Vermeirssen V, Van Camp J, Verstraete W. 2004. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J. Nutr 92:357-66.
    • (2004) Br J. Nutr , vol.92 , pp. 357-366
    • Vermeirssen, V.1    Van Camp, J.2    Verstraete, W.3
  • 35
    • 0011496233 scopus 로고
    • Properties of calpain II from tilapia muscle (Tilapia nilotica×Tilapia aurea)
    • Wang J-H, Jiang S-T. 1991. Properties of calpain II from tilapia muscle (Tilapia nilotica×Tilapia aurea). Agric Biol Chem 55(2):339-45.
    • (1991) Agric Biol Chem , vol.55 , Issue.2 , pp. 339-345
    • Wang, J.-H.1    Jiang, S.-T.2
  • 36
    • 84875132229 scopus 로고    scopus 로고
    • Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer
    • Wang R, Peng Z, Hui T, Wang F, Yao Y, Zhang Y, Zhou G. 2013. Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer. CYTA - J Food 11(1):50-9.
    • (2013) CYTA - J Food , vol.11 , Issue.1 , pp. 50-59
    • Wang, R.1    Peng, Z.2    Hui, T.3    Wang, F.4    Yao, Y.5    Zhang, Y.6    Zhou, G.7
  • 37
    • 79952363771 scopus 로고    scopus 로고
    • Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate
    • Wijesekara I, Qian Z-J, Ryu B, Ngo D-H, Kim S-K. 2011. Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate. Food Res Int 44(3):703-7.
    • (2011) Food Res Int , vol.44 , Issue.3 , pp. 703-707
    • Wijesekara, I.1    Qian, Z.-J.2    Ryu, B.3    Ngo, D.-H.4    Kim, S.-K.5
  • 38
    • 10744230552 scopus 로고    scopus 로고
    • Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus)
    • Wu H, Chen H, Shiau C. 2003. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Res Int 36(9-10):949-57.
    • (2003) Food Res Int , vol.36 , Issue.9-10 , pp. 949-957
    • Wu, H.1    Chen, H.2    Shiau, C.3
  • 39
    • 15344345075 scopus 로고    scopus 로고
    • Time-related changes in cathepsin B and L activities during processing of Jinhua ham as a function of pH, salt and temperature
    • Zhao GM, Zhou GH, Wang YL, Xu XL, Huan YJ, Wu JQ. 2005. Time-related changes in cathepsin B and L activities during processing of Jinhua ham as a function of pH, salt and temperature. Meat Sci 70(2):381-8.
    • (2005) Meat Sci , vol.70 , Issue.2 , pp. 381-388
    • Zhao, G.M.1    Zhou, G.H.2    Wang, Y.L.3    Xu, X.L.4    Huan, Y.J.5    Wu, J.Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.