메뉴 건너뛰기




Volumn 113, Issue 1, 2009, Pages 146-154

A heat-stable trypsin from the hepatopancreas of the cuttlefish (Sepia officinalis): Purification and characterisation

Author keywords

Biochemical characterisation; Cuttlefish; Hepatopancreas; Purification; Sepia officinalis; Trypsin

Indexed keywords

AMIDASE; AMMONIUM SULFATE; BARIUM ION; BENZAMIDINE; BENZOYLARGININE 4 NITROANILIDE; BENZOYLARGININE ETHYL ESTER; CALCIUM ION; COBALT; EDETIC ACID; ESTERASE; LYSYLGLUTAMYLSERYLSERYLPROLYLTYROSYLASPARAGINYLGLUTAMINE; MAGNESIUM ION; MANGANESE; MERCAPTOETHANOL; OCTAPEPTIDE; PEPSTATIN; POTASSIUM ION; SEPHADEX; SODIUM CHLORIDE; SODIUM ION; SOYBEAN TRYPSIN INHIBITOR; TRYPSIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 52949123627     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.07.059     Document Type: Article
Times cited : (57)

References (45)
  • 1
    • 84872890296 scopus 로고    scopus 로고
    • Balti, R., Bougatef, A., Souissi, N., EL-Hadj Ali, N., Zekri, D., Barkia, A., & Nasri, M. (2008). Influence of the extent of enzymatic hydrolysis on the functional properties and angiotensin I-converting enzyme inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products. In Moncef Nasri (Ed.), Recent research developments in food by-products technology and biotechnology, ISBN: 978-81-308-0259-6. Research Signopost 37/661(2), Fort P.O., Trivandrum-695 023, Kerala, India (2008).
    • Balti, R., Bougatef, A., Souissi, N., EL-Hadj Ali, N., Zekri, D., Barkia, A., & Nasri, M. (2008). Influence of the extent of enzymatic hydrolysis on the functional properties and angiotensin I-converting enzyme inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products. In Moncef Nasri (Ed.), Recent research developments in food by-products technology and biotechnology, ISBN: 978-81-308-0259-6. Research Signopost 37/661(2), Fort P.O., Trivandrum-695 023, Kerala, India (2008).
  • 2
    • 0034178602 scopus 로고    scopus 로고
    • Isolation and characterization of trypsin inhibitors from some Thai legume seeds
    • Benjakul S., Visessanguan W., and Thummaratwasik P. Isolation and characterization of trypsin inhibitors from some Thai legume seeds. Journal of Food Biochemistry 24 (2000) 107-127
    • (2000) Journal of Food Biochemistry , vol.24 , pp. 107-127
    • Benjakul, S.1    Visessanguan, W.2    Thummaratwasik, P.3
  • 4
    • 0024000481 scopus 로고
    • Protecting effects of competitive inhibitors during very intense insolubilized enzyme-activated support multipoint attachments: trypsin (amine)-agarose (aldehyde) system
    • Blanco R.M., and Guisan J.M. Protecting effects of competitive inhibitors during very intense insolubilized enzyme-activated support multipoint attachments: trypsin (amine)-agarose (aldehyde) system. Enzyme and Microbial Technology 10 (1988) 227-232
    • (1988) Enzyme and Microbial Technology , vol.10 , pp. 227-232
    • Blanco, R.M.1    Guisan, J.M.2
  • 5
    • 33751528620 scopus 로고    scopus 로고
    • Purification and characterization of trypsin from the viscera of sardine (Sardina pilchardus)
    • Bougatef A., Souissi N., Fakhfakh N., Ellouz-Triki Y., and Nasri M. Purification and characterization of trypsin from the viscera of sardine (Sardina pilchardus). Food Chemistry 102 (2007) 343-350
    • (2007) Food Chemistry , vol.102 , pp. 343-350
    • Bougatef, A.1    Souissi, N.2    Fakhfakh, N.3    Ellouz-Triki, Y.4    Nasri, M.5
  • 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 M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 0346764650 scopus 로고    scopus 로고
    • Purification and characterization of two anionic trypsins from the hepatopancreas of carp
    • Cao M.J., Osatomi K., Suzuki M., Hara K., Tachibana K., and Ishihara T. Purification and characterization of two anionic trypsins from the hepatopancreas of carp. Fisheries Science 66 (2000) 1172-1179
    • (2000) Fisheries Science , vol.66 , pp. 1172-1179
    • Cao, M.J.1    Osatomi, K.2    Suzuki, M.3    Hara, K.4    Tachibana, K.5    Ishihara, T.6
  • 9
    • 0001092867 scopus 로고
    • Pancreatic proteolytic enzymes from carp (Cyprinus carpio): I. Purification and physical properties of trypsin, chymotrypsin, elastase and carboxipeptidase B
    • Cohen T., Gertler A., and Birk Y. Pancreatic proteolytic enzymes from carp (Cyprinus carpio): I. Purification and physical properties of trypsin, chymotrypsin, elastase and carboxipeptidase B. Comparative Biochemistry and Physiology 69B (1981) 639-646
    • (1981) Comparative Biochemistry and Physiology , vol.69 B , pp. 639-646
    • Cohen, T.1    Gertler, A.2    Birk, Y.3
  • 10
    • 0022545173 scopus 로고
    • Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens
    • Emi M., Nakamura Y., Ogawa M., Yamamoto T., Nishide T., Mori T., and Matsubara K. Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens. Gene 41 (1986) 305-310
    • (1986) Gene , vol.41 , pp. 305-310
    • Emi, M.1    Nakamura, Y.2    Ogawa, M.3    Yamamoto, T.4    Nishide, T.5    Mori, T.6    Matsubara, K.7
  • 12
    • 0014603717 scopus 로고
    • Isolation and comparative properties of shrimp trypsin
    • Gates B.J., and Travis J. Isolation and comparative properties of shrimp trypsin. Biochemistry 8 (1969) 4483-4489
    • (1969) Biochemistry , vol.8 , pp. 4483-4489
    • Gates, B.J.1    Travis, J.2
  • 15
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: molecular approaches and industrial applications
    • Gupta R., Beg Q., and Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Applied Microbiology Biotechnology 59 (2002) 15-32
    • (2002) Applied Microbiology Biotechnology , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.2    Lorenz, P.3
  • 16
    • 33746256084 scopus 로고    scopus 로고
    • Purification and characterization of Trypsin from pyloric caeca of bigeye snapper (Pricanthus macracanthus)
    • Hau P.V., and Benjakul S. Purification and characterization of Trypsin from pyloric caeca of bigeye snapper (Pricanthus macracanthus). Journal of Food Biochemistry 30 (2006) 478-495
    • (2006) Journal of Food Biochemistry , vol.30 , pp. 478-495
    • Hau, P.V.1    Benjakul, S.2
  • 17
    • 0015783856 scopus 로고
    • Determination of the amino acid sequence of porcine trypsin by sequenator analysis
    • Hermodson M.A., Ericsson L.H., Neurath H., and Walsh K.A. Determination of the amino acid sequence of porcine trypsin by sequenator analysis. Biochemistry 12 (1973) 3146-3153
    • (1973) Biochemistry , vol.12 , pp. 3146-3153
    • Hermodson, M.A.1    Ericsson, L.H.2    Neurath, H.3    Walsh, K.A.4
  • 18
    • 0028802456 scopus 로고
    • Comparison of trypsin and chymotrypsin from the viscera of anchovy, Engraulis japonica
    • Heu M.S., Kim H.R., and Pyeun J.H. Comparison of trypsin and chymotrypsin from the viscera of anchovy, Engraulis japonica. Comparative Biochemistry and Physiology 112B (1995) 557-567
    • (1995) Comparative Biochemistry and Physiology , vol.112 B , pp. 557-567
    • Heu, M.S.1    Kim, H.R.2    Pyeun, J.H.3
  • 19
    • 0035988710 scopus 로고    scopus 로고
    • Isolation and characteristics of trypsin from pyloric ceca of the starfish Asterina pectinifera
    • Kishimura H., and Hayashi K. Isolation and characteristics of trypsin from pyloric ceca of the starfish Asterina pectinifera. Comparative Biochemistry and Physiology 132B (2002) 485-490
    • (2002) Comparative Biochemistry and Physiology , vol.132 B , pp. 485-490
    • Kishimura, H.1    Hayashi, K.2
  • 20
    • 0141567499 scopus 로고    scopus 로고
    • N-terminal amino acid sequence of trypsin from the pyloric ceca of the starfish Asterias amurensis
    • Kishimura H., and Hayashi K. N-terminal amino acid sequence of trypsin from the pyloric ceca of the starfish Asterias amurensis. Fisheries science 69 (2003) 867-869
    • (2003) Fisheries science , vol.69 , pp. 867-869
    • Kishimura, H.1    Hayashi, K.2
  • 21
    • 27844606815 scopus 로고    scopus 로고
    • Characteristics of two trypsin isozymes from the viscera of Japanese anchovy (Engraulis japonica)
    • Kishimura H., Hayashi K., Miyashita Y., and Nonami Y. Characteristics of two trypsin isozymes from the viscera of Japanese anchovy (Engraulis japonica). Journal of Food Biochemistry 29 (2005) 459-469
    • (2005) Journal of Food Biochemistry , vol.29 , pp. 459-469
    • Kishimura, H.1    Hayashi, K.2    Miyashita, Y.3    Nonami, Y.4
  • 22
    • 28844501954 scopus 로고    scopus 로고
    • Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus)
    • Kishimura H., Hayashi K., Miyashita Y., and Nonami Y. Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus). Food Chemistry 97 (2006) 65-70
    • (2006) Food Chemistry , vol.97 , pp. 65-70
    • Kishimura, H.1    Hayashi, K.2    Miyashita, Y.3    Nonami, Y.4
  • 23
    • 34548265208 scopus 로고    scopus 로고
    • Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma)
    • Kishimura H., Klomklao S., Benjakul S., and Chun B.S. Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma). Food Chemistry 106 (2008) 194-199
    • (2008) Food Chemistry , vol.106 , pp. 194-199
    • Kishimura, H.1    Klomklao, S.2    Benjakul, S.3    Chun, B.S.4
  • 24
    • 33746508515 scopus 로고    scopus 로고
    • Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization
    • Kishimura H., Tokuda Y., Yabe M., Klomklao S., Benjakul S., and Ando S. Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization. Food Chemistry 100 (2007) 1490-1495
    • (2007) Food Chemistry , vol.100 , pp. 1490-1495
    • Kishimura, H.1    Tokuda, Y.2    Yabe, M.3    Klomklao, S.4    Benjakul, S.5    Ando, S.6
  • 25
    • 33746738184 scopus 로고    scopus 로고
    • Purification and characterisation of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis)
    • Klomklao S., Benjakul S., Visessanguan W., Kishimura H., and Simpson B.K. Purification and characterisation of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis). Food Chemistry 100 (2007) 1580-1589
    • (2007) Food Chemistry , vol.100 , pp. 1580-1589
    • Klomklao, S.1    Benjakul, S.2    Visessanguan, W.3    Kishimura, H.4    Simpson, B.K.5
  • 29
    • 33644902351 scopus 로고    scopus 로고
    • Isolation and characterization of a trypsin fraction from the pyloric ceca of chinook salmon (Oncorhynchus tshawytscha)
    • Kurtovic I., Marshall S.N., and Simpson B.K. Isolation and characterization of a trypsin fraction from the pyloric ceca of chinook salmon (Oncorhynchus tshawytscha). Comparative Biochemistry and Physiology 143B (2006) 432-440
    • (2006) Comparative Biochemistry and Physiology , vol.143 B , pp. 432-440
    • Kurtovic, I.1    Marshall, S.N.2    Simpson, B.K.3
  • 30
    • 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) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0025009050 scopus 로고
    • Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen: structural identity within the trypsin family
    • LeHuerou I., Wicker C., Guilloteau P., Toullec R., and Puigserver A. Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen: structural identity within the trypsin family. European Journal of Biochemistry 193 (1990) 767-773
    • (1990) European Journal of Biochemistry , vol.193 , pp. 767-773
    • LeHuerou, I.1    Wicker, C.2    Guilloteau, P.3    Toullec, R.4    Puigserver, A.5
  • 33
    • 41949139655 scopus 로고    scopus 로고
    • Purification and characterisation of trypsins from pyloric caeca of mandarin fish (Siniperca chuasti)
    • Lu B.J., Zhoo L.G., Cai Q.F., Hara K., Maeda A., Su W.J., and Cao M.J. Purification and characterisation of trypsins from pyloric caeca of mandarin fish (Siniperca chuasti). Food chemistry 110 (2008) 352-360
    • (2008) Food chemistry , vol.110 , pp. 352-360
    • Lu, B.J.1    Zhoo, L.G.2    Cai, Q.F.3    Hara, K.4    Maeda, A.5    Su, W.J.6    Cao, M.J.7
  • 34
    • 0020491017 scopus 로고
    • Two similar but nonallelic rat pancreatic trypsinogens Nucleotide sequences of the cloned cDNAs
    • MacDonald R.J., Stary S.J., and Swift G.H. Two similar but nonallelic rat pancreatic trypsinogens Nucleotide sequences of the cloned cDNAs. The Journal of Biological Chemistry 257 (1982) 9724-9732
    • (1982) The Journal of Biological Chemistry , vol.257 , pp. 9724-9732
    • MacDonald, R.J.1    Stary, S.J.2    Swift, G.H.3
  • 35
    • 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. Comparative Biochemistry and Physiology 91B (1988) 677-684
    • (1988) Comparative Biochemistry and Physiology , vol.91 B , pp. 677-684
    • Martinez, A.1    Olsen, R.L.2    Serra, J.L.3
  • 36
    • 0020410219 scopus 로고
    • Comparative biochemistry of the proteinases of eukaryotic microorganisms
    • North M.J. Comparative biochemistry of the proteinases of eukaryotic microorganisms. Microbiological review 46 (1982) 308-340
    • (1982) Microbiological review , vol.46 , pp. 308-340
    • North, M.J.1
  • 37
    • 0034401320 scopus 로고    scopus 로고
    • Enzymatic properties of a protease from the hepatopancreas of shrimp, Penaeus orientalis
    • Oh E.S., Kim D.S., Kim J.H., and Kim H.R. Enzymatic properties of a protease from the hepatopancreas of shrimp, Penaeus orientalis. Journal of Food Biochemistry 24 (2000) 251-264
    • (2000) Journal of Food Biochemistry , vol.24 , pp. 251-264
    • Oh, E.S.1    Kim, D.S.2    Kim, J.H.3    Kim, H.R.4
  • 38
    • 0021817726 scopus 로고
    • Differential regulation of trypsinogen mRNA translation: full-length mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas
    • Pinsky S.D., LaForge K.S., and Scheele G. Differential regulation of trypsinogen mRNA translation: full-length mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas. Molecular and Cellular Biology 5 (1985) 2669-2676
    • (1985) Molecular and Cellular Biology , vol.5 , pp. 2669-2676
    • Pinsky, S.D.1    LaForge, K.S.2    Scheele, G.3
  • 39
    • 0034624020 scopus 로고    scopus 로고
    • Schistosome invasion of human skin and degradation of dermal elastin are mediated by a single serine protease
    • Salter J.P., Lim K.C., Hansell E., Hsieh I., and McKerrow J.H. Schistosome invasion of human skin and degradation of dermal elastin are mediated by a single serine protease. The Journal of Biological Chemistry 275 (2000) 38667-38673
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 38667-38673
    • Salter, J.P.1    Lim, K.C.2    Hansell, E.3    Hsieh, I.4    McKerrow, J.H.5
  • 40
    • 0033752757 scopus 로고    scopus 로고
    • Anionic trypsin from chum salmon: activity with p-aminophenyl ester and comparison with bovine and Streptomyces griseus trypsins
    • Sekizaki H., Itoh K., Murakami M., Toyota E., and Tanizawa K. Anionic trypsin from chum salmon: activity with p-aminophenyl ester and comparison with bovine and Streptomyces griseus trypsins. Comparative Biochemistry and Physiology 127B (2000) 337-346
    • (2000) Comparative Biochemistry and Physiology , vol.127 B , pp. 337-346
    • Sekizaki, H.1    Itoh, K.2    Murakami, M.3    Toyota, E.4    Tanizawa, K.5
  • 41
    • 0035746634 scopus 로고    scopus 로고
    • Enzymes from fish and aquatic invertebrates and their application in the food industry
    • Shahidi F., and Kamil J.Y.V.A. Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends in Food Science and Technology 12 (2001) 435-464
    • (2001) Trends in Food Science and Technology , vol.12 , pp. 435-464
    • Shahidi, F.1    Kamil, J.Y.V.A.2
  • 43
    • 44849136814 scopus 로고    scopus 로고
    • Preparation and use of media for protease-producing bacterial strains based on by-products from Cuttlefish (Sepia officinalis) and wastewaters from marine-products processing factories
    • Souissi N., Ellouz-Triki Y., Bougatef A., Blibech M., and Nasri M. Preparation and use of media for protease-producing bacterial strains based on by-products from Cuttlefish (Sepia officinalis) and wastewaters from marine-products processing factories. Microbiological Research 163 (2008) 473-480
    • (2008) Microbiological Research , vol.163 , pp. 473-480
    • Souissi, N.1    Ellouz-Triki, Y.2    Bougatef, A.3    Blibech, M.4    Nasri, M.5
  • 45
    • 5744235228 scopus 로고
    • Trypsinogens and trypsins of various species
    • Gertrude E., and Lorand P.L. (Eds), Academic Press, New York
    • Walsh K.A. Trypsinogens and trypsins of various species. In: Gertrude E., and Lorand P.L. (Eds). Methods in Enzymology (1970), Academic Press, New York 41-63
    • (1970) Methods in Enzymology , pp. 41-63
    • Walsh, K.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.