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Volumn 42, Issue C, 2004, Pages 425-439

Properties of proteases responsible for degradation of muscle proteins during anchovy sauce fermentation

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EID: 77957797124     PISSN: 01674501     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0167-4501(04)80042-6     Document Type: Article
Times cited : (9)

References (45)
  • 1
    • 0026700712 scopus 로고
    • Purification and characterization of anionic trypsins from the hepatopancreas of crayfish, Procambarus clarkii
    • Kim H.R., Meyers S.P., and Godber J.S. Purification and characterization of anionic trypsins from the hepatopancreas of crayfish, Procambarus clarkii. Comp. Biochem. Physiol. 103B (1992) 391-398
    • (1992) Comp. Biochem. Physiol. , vol.103 B , pp. 391-398
    • Kim, H.R.1    Meyers, S.P.2    Godber, J.S.3
  • 2
    • 0028031778 scopus 로고
    • Enzymatic properties of anionic trypsins from the hepatopancreases of crayfish, Procambarus clarkii
    • Kim H.R., Meyers S.P., Pyeun J.H., and Godber J.S. Enzymatic properties of anionic trypsins from the hepatopancreases of crayfish, Procambarus clarkii. Comp. Biochem. Physiol. 107B (1994) 197-203
    • (1994) Comp. Biochem. Physiol. , vol.107 B , pp. 197-203
    • Kim, H.R.1    Meyers, S.P.2    Pyeun, J.H.3    Godber, J.S.4
  • 3
    • 0024189838 scopus 로고
    • Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus
    • Martinez A., Olsen R.L., and Serra J.L. Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus. Comp. Biochem. Physiol. 91B (1988) 677-684
    • (1988) Comp. Biochem. Physiol. , vol.91 B , pp. 677-684
    • Martinez, A.1    Olsen, R.L.2    Serra, J.L.3
  • 4
    • 0001043282 scopus 로고
    • A comparison of dogfish and bovine chymotrypsins in relation to protein hydrolysis
    • Ramakrishn M., Hultin H.O., and Atallah M.T. A comparison of dogfish and bovine chymotrypsins in relation to protein hydrolysis. J. Food Sci 52 (1987) 1198-1202
    • (1987) J. Food Sci , vol.52 , pp. 1198-1202
    • Ramakrishn, M.1    Hultin, H.O.2    Atallah, M.T.3
  • 6
    • 3743051463 scopus 로고
    • The protease distributed in the intestinal organs of fish 2. Characterization of the three alkaline proteinases from the pyloric caeca of mackerel Scomber japonicus
    • Kim H.R., and Pyeun J.H. The protease distributed in the intestinal organs of fish 2. Characterization of the three alkaline proteinases from the pyloric caeca of mackerel Scomber japonicus. Bull. Korean Fish. Soc. 19 (1986) 547-557
    • (1986) Bull. Korean Fish. Soc. , vol.19 , pp. 547-557
    • Kim, H.R.1    Pyeun, J.H.2
  • 7
    • 0020024015 scopus 로고
    • Characteristics of two trypsin type isozymes isolated from the arctic fish capelin (Mallotus villosus)
    • Hjelmeland K., and Raa J. Characteristics of two trypsin type isozymes isolated from the arctic fish capelin (Mallotus villosus). Comp. Biochem. Physiol. 71B (1982) 557-562
    • (1982) Comp. Biochem. Physiol. , vol.71 B , pp. 557-562
    • Hjelmeland, K.1    Raa, J.2
  • 8
    • 0001092867 scopus 로고
    • Pancreatic proteolytic enzymes from carp (Cyprinus carpio). Purification and physical properties of trypsin, chymotrypsin, elastase and carboxypeptidase n
    • Cohen T., Gertler A., and Birk Y. Pancreatic proteolytic enzymes from carp (Cyprinus carpio). Purification and physical properties of trypsin, chymotrypsin, elastase and carboxypeptidase n. Comp. Biochem. Physiol. 69B (1981) 639-646
    • (1981) Comp. Biochem. Physiol. , vol.69 B , pp. 639-646
    • Cohen, T.1    Gertler, A.2    Birk, Y.3
  • 9
    • 0001092869 scopus 로고
    • Pancreatic proteolytic enzymes from carp (Cyprinus carpio)-II. Kinetic properties and inhibition studies of tyrpsin, chymotrypsin and elastase
    • Cohen T., Gertler A., and Birk Y. Pancreatic proteolytic enzymes from carp (Cyprinus carpio)-II. Kinetic properties and inhibition studies of tyrpsin, chymotrypsin and elastase. Comp. Biochem. Physiol. 69B (1981) 647-653
    • (1981) Comp. Biochem. Physiol. , vol.69 B , pp. 647-653
    • Cohen, T.1    Gertler, A.2    Birk, Y.3
  • 10
    • 0011130177 scopus 로고
    • Purification and characterization of alkaline proteinases from the viscera of anchovy Engraulis japonica
    • Heu M.S., Pyeun J.H., Kim H.R., and Godber J.S. Purification and characterization of alkaline proteinases from the viscera of anchovy Engraulis japonica. J. Food Biochem. 15 (1991) 51-66
    • (1991) J. Food Biochem. , vol.15 , pp. 51-66
    • Heu, M.S.1    Pyeun, J.H.2    Kim, H.R.3    Godber, J.S.4
  • 11
    • 0005412539 scopus 로고
    • Comparative studies on the enzymatic properties of two trypsin-like enzymes from menhaden, Brevoortia tyranus
    • Pyeun J.H., Kim H.R., and Godber J.S. Comparative studies on the enzymatic properties of two trypsin-like enzymes from menhaden, Brevoortia tyranus. Bull. Korean Fish Soc. 23 (1990) 12-20
    • (1990) Bull. Korean Fish Soc. , vol.23 , pp. 12-20
    • Pyeun, J.H.1    Kim, H.R.2    Godber, J.S.3
  • 12
    • 0347389084 scopus 로고
    • The proteinase distributed in the intestinal organs of fish. 3. Purification and some enzymatic properties of the alkaline proteinases from the pyloric caeca of skipjack, Katsuwonus vagans
    • Pyeun J.H., Kim H.R., and Heu M.S. The proteinase distributed in the intestinal organs of fish. 3. Purification and some enzymatic properties of the alkaline proteinases from the pyloric caeca of skipjack, Katsuwonus vagans. Bull. Korean Fish. Soc 21 (1988) 85-96
    • (1988) Bull. Korean Fish. Soc , vol.21 , pp. 85-96
    • Pyeun, J.H.1    Kim, H.R.2    Heu, M.S.3
  • 13
    • 85005665571 scopus 로고
    • The use of bromelain in the hydrolysis of mackerel and the investigation of fermented fish aroma
    • Beddows C.G., Ismail M., and Steinkraus K.H. The use of bromelain in the hydrolysis of mackerel and the investigation of fermented fish aroma. J. Food Technol. 11 (1976) 379-388
    • (1976) J. Food Technol. , vol.11 , pp. 379-388
    • Beddows, C.G.1    Ismail, M.2    Steinkraus, K.H.3
  • 14
    • 84986776512 scopus 로고
    • Biochemical changes occurring during the manufacture of Budu
    • Beddows CG., Ardeshir A.G., and Daud W.J. Biochemical changes occurring during the manufacture of Budu. J. Sci. Food Agric. 30 (1979) 1097-1103
    • (1979) J. Sci. Food Agric. , vol.30 , pp. 1097-1103
    • Beddows, CG.1    Ardeshir, A.G.2    Daud, W.J.3
  • 15
    • 0007711073 scopus 로고
    • Scandinavian anchovies and tidbits
    • Borgstrom G. (Ed), Academic Press, New York
    • Alm F. Scandinavian anchovies and tidbits. In: Borgstrom G. (Ed). Fish as Food (1965), Academic Press, New York 195-198
    • (1965) Fish as Food , pp. 195-198
    • Alm, F.1
  • 16
    • 0001116094 scopus 로고
    • Salting of herring
    • Borgstrom G. (Ed), Academic Press, New York
    • Voskresensky N.A. Salting of herring. In: Borgstrom G. (Ed). Fish as Food (1965), Academic Press, New York 107-108
    • (1965) Fish as Food , pp. 107-108
    • Voskresensky, N.A.1
  • 17
    • 84985287386 scopus 로고
    • Agents of proteolysis and its inhibition in patis (fish sauce) fermentation
    • Orejana F.M., and Liston J. Agents of proteolysis and its inhibition in patis (fish sauce) fermentation. J. Food Sci. 47 (1982) 198-203
    • (1982) J. Food Sci. , vol.47 , pp. 198-203
    • Orejana, F.M.1    Liston, J.2
  • 18
    • 84985287386 scopus 로고
    • Agents of proteolysis and its inhibition in patis (fish sauce) fermentation
    • Orejana F.M., and Liston J. Agents of proteolysis and its inhibition in patis (fish sauce) fermentation. J. Food Sci. 47 (1982) 209
    • (1982) J. Food Sci. , vol.47 , pp. 209
    • Orejana, F.M.1    Liston, J.2
  • 19
    • 0039711981 scopus 로고
    • Biochemistry of Patis formation I. Activity of cathepsins in Patis hydrolysates
    • Del Rosario R.R., and Maldo S.M. Biochemistry of Patis formation I. Activity of cathepsins in Patis hydrolysates. Phil. Agr. 67 (1984) 167-175
    • (1984) Phil. Agr. , vol.67 , pp. 167-175
    • Del Rosario, R.R.1    Maldo, S.M.2
  • 20
    • 77957803481 scopus 로고    scopus 로고
    • Autolytic activity of enzymes in Pacific whiting and surimi by-product (SBP) during fish sauce production
    • Lopetcharat K., and Park J.W. Autolytic activity of enzymes in Pacific whiting and surimi by-product (SBP) during fish sauce production. Abstract book of 1999 IFT annual meeting (1999) 149
    • (1999) Abstract book of 1999 IFT annual meeting , pp. 149
    • Lopetcharat, K.1    Park, J.W.2
  • 21
    • 0344788840 scopus 로고
    • The proteinase distributed in the intestinal organs of fish 1. Purification of the three alkaline proteinases from the pyloric caeca of mackerel, Scomber japonicus
    • Pyeun J.H., and Kim H.R. The proteinase distributed in the intestinal organs of fish 1. Purification of the three alkaline proteinases from the pyloric caeca of mackerel, Scomber japonicus. Bull. Korean Fish. Soc. 19 (1986) 537-546
    • (1986) Bull. Korean Fish. Soc. , vol.19 , pp. 537-546
    • Pyeun, J.H.1    Kim, H.R.2
  • 22
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger B.F., Kokowsky N., and Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem Biophys. 95 (1961) 271-278
    • (1961) Arch. Biochem Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 23
    • 0013924977 scopus 로고
    • The action of cymotrypsin on two new chromogenic substrates
    • Erlanger B.F., Edel F., and Cooper A.G. The action of cymotrypsin on two new chromogenic substrates. Arch. Biochem. Biophys. 155 (1966) 206-210
    • (1966) Arch. Biochem. Biophys. , vol.155 , pp. 206-210
    • Erlanger, B.F.1    Edel, F.2    Cooper, A.G.3
  • 24
    • 0001243390 scopus 로고
    • A modified spectrophotometric determination of chymotrypsin, trypsin and thrombin
    • Hummel B.C. A modified spectrophotometric determination of chymotrypsin, trypsin and thrombin. Can. J. Physiol. 37 (1959) 1393-1399
    • (1959) Can. J. Physiol. , vol.37 , pp. 1393-1399
    • Hummel, B.C.1
  • 25
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrypsin
    • Schwert G.W., and Takenaka Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim. Biophys. Acta 16 (1955) 570-575
    • (1955) Biochim. Biophys. Acta , vol.16 , pp. 570-575
    • Schwert, G.W.1    Takenaka, Y.2
  • 26
    • 0015338074 scopus 로고
    • 1 and other thiol proteinases
    • 1 and other thiol proteinases. Anal. Biochem. 47 (1972) 280-293
    • (1972) Anal. Biochem. , vol.47 , pp. 280-293
    • Barrett, A.J.1
  • 27
    • 0017142632 scopus 로고
    • An improved color reagent for use in Barrett's assay of cathepsin B
    • Barrett A.J. An improved color reagent for use in Barrett's assay of cathepsin B. Anal. Biochem. 76 (1976) 374-376
    • (1976) Anal. Biochem. , vol.76 , pp. 374-376
    • Barrett, A.J.1
  • 28
    • 0010434845 scopus 로고
    • Purification and characterization of protease from milkfish muscle (Chanos chanos)
    • Jiang S.T., Tsao C.Y., Wang T., and Chen C.S. Purification and characterization of protease from milkfish muscle (Chanos chanos). J. Agric. Food Chem. 38 (1990) 1458-1463
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1458-1463
    • Jiang, S.T.1    Tsao, C.Y.2    Wang, T.3    Chen, C.S.4
  • 30
    • 78651153791 scopus 로고
    • Disc-electrophoresis II, method and application to human serum protein
    • Davis B.J. Disc-electrophoresis II, method and application to human serum protein. Ann. N.Y.Acad. Sci. 121 (1964) 404-427
    • (1964) Ann. N.Y.Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227 (1970) 680-686
    • (1970) Nature , vol.227 , pp. 680-686
    • Laemmli, U.K.1
  • 32
    • 33947484782 scopus 로고
    • Determination of molecular weights of proteins by gel filtration on Sephadex
    • Whitaker J.R. Determination of molecular weights of proteins by gel filtration on Sephadex. Anal. Chem. 35 (1963) 1950-1953
    • (1963) Anal. Chem. , vol.35 , pp. 1950-1953
    • Whitaker, J.R.1
  • 33
    • 0015500932 scopus 로고
    • Determination of tryptophan content of protein by ion exchange Chromatograph of alkaline hydrolysates
    • Hugli T.E., and Moore S.J. Determination of tryptophan content of protein by ion exchange Chromatograph of alkaline hydrolysates. J. Biol. Chem. 247 (1972) 2828-2834
    • (1972) J. Biol. Chem. , vol.247 , pp. 2828-2834
    • Hugli, T.E.1    Moore, S.J.2
  • 34
    • 0014679375 scopus 로고
    • A new convenient method for estimation of total cystine-cysteine in proteins
    • Spencer R.L., and Wald F. A new convenient method for estimation of total cystine-cysteine in proteins. Anal. Biochem. 32 (1969) 185-190
    • (1969) Anal. Biochem. , vol.32 , pp. 185-190
    • Spencer, R.L.1    Wald, F.2
  • 35
    • 0012640417 scopus 로고
    • Purification and characterization of Pacific whiting proteases
    • Seymour T.A., Morrissey M.T., Peters M.Y., and An H. Purification and characterization of Pacific whiting proteases. J. Agric. Food Chem. 42 (1994) 2421-2427
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2421-2427
    • Seymour, T.A.1    Morrissey, M.T.2    Peters, M.Y.3    An, H.4
  • 36
    • 85008070248 scopus 로고
    • Participation of cathepsin L in extensive softening of the muscle of chum salmon caught during spawning migration
    • Yamashita M., and Konagaya S. Participation of cathepsin L in extensive softening of the muscle of chum salmon caught during spawning migration. Nippon Suisan Gakkaishi 56 (1990) 1271-1277
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1271-1277
    • Yamashita, M.1    Konagaya, S.2
  • 37
    • 0021313131 scopus 로고
    • The purification and properties of cathepsin L from rabbit liver
    • Mason R.W., Taylor M.A., and Etherington D.J. The purification and properties of cathepsin L from rabbit liver. Biochem. J. 217 (1984) 209-217
    • (1984) Biochem. J. , vol.217 , pp. 209-217
    • Mason, R.W.1    Taylor, M.A.2    Etherington, D.J.3
  • 38
    • 0346128071 scopus 로고    scopus 로고
    • Digestive proteinases from marine animals
    • Haard N.F., and Simpson B.K. (Eds), Marcel Dekker, New York
    • Simpson K. Digestive proteinases from marine animals. In: Haard N.F., and Simpson B.K. (Eds). Seafood Enzymes (2000), Marcel Dekker, New York 411-450
    • (2000) Seafood Enzymes , pp. 411-450
    • Simpson, K.1
  • 39
    • 77957773738 scopus 로고
    • Purification and characterization of proteinases identified as cathepsin L and L-like (58Kda) proteinase from mackerel (Scomber australasicus)
    • Lee J.J., Chen H.C., and Jiang S.-T. Purification and characterization of proteinases identified as cathepsin L and L-like (58Kda) proteinase from mackerel (Scomber australasicus). Biosci. Biotechnol. Biochem. 57 (1993) 683-690
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 683-690
    • Lee, J.J.1    Chen, H.C.2    Jiang, S.-T.3
  • 41
    • 0000183485 scopus 로고
    • Characterization of cathepsin D from the skeletal muscle of fresh water fish, Tilapia mossambicca. Agric
    • 1980
    • 1980. Doke S., Ninjoor V., and Nadkarni G.B. Characterization of cathepsin D from the skeletal muscle of fresh water fish, Tilapia mossambicca. Agric. Biol. Chem. 44 (1980) 1521-1528
    • (1980) Biol. Chem. , vol.44 , pp. 1521-1528
    • Doke, S.1    Ninjoor, V.2    Nadkarni, G.B.3
  • 42
    • 0021120203 scopus 로고
    • Acid proteinase activity in fish-II. Purification and characterization of cathepsin B and D fromMujil auratus
    • Boneto M.J., Manjon A., Liorca F., and Iborra J.L. Acid proteinase activity in fish-II. Purification and characterization of cathepsin B and D fromMujil auratus. Comp. Biochem. Physiol. 78B (1984) 207-213
    • (1984) Comp. Biochem. Physiol. , vol.78 B , pp. 207-213
    • Boneto, M.J.1    Manjon, A.2    Liorca, F.3    Iborra, J.L.4
  • 45
    • 0014117822 scopus 로고
    • On the average hydrophobicity of protein and the relation between it and protein structure
    • Bigelow C.C. On the average hydrophobicity of protein and the relation between it and protein structure. J. Theoret. Biol. 16 (1967) 187-211
    • (1967) J. Theoret. Biol. , vol.16 , pp. 187-211
    • Bigelow, C.C.1


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