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Volumn 88, Issue 15, 2008, Pages 2654-2662

Isolation and characterisation of trypsin from sardinelle (Sardinella aurita) viscera

Author keywords

Biochemical characterisation; Purification; Sardinelle; Trypsin; Viscera

Indexed keywords

SARDINELLA AURITA;

EID: 57149109157     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3386     Document Type: Article
Times cited : (36)

References (33)
  • 1
    • 0026808118 scopus 로고
    • Recovery of proteinase and protein hydrolysate from fish viscera
    • Gildberg A, Recovery of proteinase and protein hydrolysate from fish viscera. Bioresource Technol 39:271-276 (1992).
    • (1992) Bioresource Technol , vol.39 , pp. 271-276
    • Gildberg, A.1
  • 2
    • 84952490376 scopus 로고
    • A review of proteolytic enzymes from marine organisms and their application in the food industry
    • Haard NF, A review of proteolytic enzymes from marine organisms and their application in the food industry. J Aquat Food Prod Technol 1:17-35 (1992).
    • (1992) J Aquat Food Prod Technol , vol.1 , pp. 17-35
    • Haard, N.F.1
  • 3
    • 0035746634 scopus 로고    scopus 로고
    • Enzymes from fish and aquatic invertebrates and their application in the food industry
    • Shahidi F and Kamil JYVA, Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol 12:435-464 (2001).
    • (2001) Trends Food Sci Technol , vol.12 , pp. 435-464
    • Shahidi, F.1    Kamil, J.Y.V.A.2
  • 4
    • 0002284639 scopus 로고    scopus 로고
    • Specialty enzymes from marine organisms
    • Haard NF, Specialty enzymes from marine organisms. Food Technol 52:64-67 (1998).
    • (1998) Food Technol , vol.52 , pp. 64-67
    • Haard, N.F.1
  • 5
    • 0346128071 scopus 로고    scopus 로고
    • Digestive proteases from marine animals
    • ed. by Haard NF and Simpson BK. Marcel Dekker, New York, NY, pp
    • Simpson BK, Digestive proteases from marine animals, in Seafood Enzymes, ed. by Haard NF and Simpson BK. Marcel Dekker, New York, NY, pp. 191-213 (2000).
    • (2000) Seafood Enzymes , pp. 191-213
    • Simpson, B.K.1
  • 6
    • 0030694054 scopus 로고    scopus 로고
    • Catalytic activities of crude enzyme fractions from Monterey sardine
    • Lugo-Sanchez ME, Pacheco-Aguilar R and Yepiz-Plascencia G, Catalytic activities of crude enzyme fractions from Monterey sardine. J Food Sci 62:976-979 (1997).
    • (1997) J Food Sci , vol.62 , pp. 976-979
    • Lugo-Sanchez, M.E.1    Pacheco-Aguilar, R.2    Yepiz-Plascencia, G.3
  • 8
    • 0346058040 scopus 로고    scopus 로고
    • Characterization of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caerulea) viscera
    • Castillo-Yanez FJ, Pacheco-Aguilar R, Garcia-Carreno FL and Toro MAN, Characterization of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caerulea) viscera. Food Chem 85:343-350 (2004).
    • (2004) Food Chem , vol.85 , pp. 343-350
    • Castillo-Yanez, F.J.1    Pacheco-Aguilar, R.2    Garcia-Carreno, F.L.3    Toro, M.A.N.4
  • 9
    • 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 Chem 97:65-70 (2006).
    • (2006) Food Chem , vol.97 , pp. 65-70
    • Kishimura, H.1    Hayashi, K.2    Miyashita, Y.3    Nonami, Y.4
  • 10
    • 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 Chem 102:343-350 (2007).
    • (2007) Food Chem , vol.102 , pp. 343-350
    • Bougatef, A.1    Souissi, N.2    Fakhfakh, N.3    Ellouz-Triki, Y.4    Nasri, M.5
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 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. Anal Biochem 72:248-254 (1976).
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 13
    • 0027352759 scopus 로고
    • Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64
    • Kembhavi AA, Kulkarni A and Pant A, Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64. Appl Biochem Biotechnol 38:83-92 (1993).
    • (1993) Appl Biochem Biotechnol , vol.38 , pp. 83-92
    • Kembhavi, A.A.1    Kulkarni, A.2    Pant, A.3
  • 14
    • 0024000481 scopus 로고
    • Protecting effects of competitive inhibitors during very intense insolubilized enzyme-activated support multipoint attachments: Trypsin (amine)-agarose (aldehyde) system
    • Blanco RM and Guisan JM, Protecting effects of competitive inhibitors during very intense insolubilized enzyme-activated support multipoint attachments: trypsin (amine)-agarose (aldehyde) system. Enzyme Microb Technol 10:227-232 (1988).
    • (1988) Enzyme Microb Technol , vol.10 , pp. 227-232
    • Blanco, R.M.1    Guisan, J.M.2
  • 15
    • 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. J Food Biochem 24:107-127 (2000).
    • (2000) J Food Biochem , vol.24 , pp. 107-127
    • Benjakul, S.1    Visessanguan, W.2    Thummaratwasik, P.3
  • 16
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H and Burk D, The determination of enzyme dissociation constants. J Am Chem Soc 56:665-666 (1934).
    • (1934) J Am Chem Soc , vol.56 , pp. 665-666
    • Lineweaver, H.1    Burk, D.2
  • 17
    • 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 Chem 100:1490-1495 (2007).
    • (2007) Food Chem , vol.100 , pp. 1490-1495
    • Kishimura, H.1    Tokuda, Y.2    Yabe, M.3    Klomklao, S.4    Benjakul, S.5    Ando, S.6
  • 19
    • 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 BK, Purification and characterisation of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis). Food Chem 100:1580-1589 (2007).
    • (2007) Food Chem , vol.100 , pp. 1580-1589
    • Klomklao, S.1    Benjakul, S.2    Visessanguan, W.3    Kishimura, H.4    Simpson, B.K.5
  • 20
    • 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). J Food Biochem 29:459-469 (2005).
    • (2005) J Food Biochem , vol.29 , pp. 459-469
    • Kishimura, H.1    Hayashi, K.2    Miyashita, Y.3    Nonami, Y.4
  • 21
    • 33746265426 scopus 로고    scopus 로고
    • Enzymatic characteristics of trypsin from the pyloric ceca of spotted mackerel (Scomber australasicus)
    • Kishimura H, Tokuda Y, Klomklao S, Benjakul S and Ando S, Enzymatic characteristics of trypsin from the pyloric ceca of spotted mackerel (Scomber australasicus). J Food Biochem 30:466-477 (2006).
    • (2006) J Food Biochem , vol.30 , pp. 466-477
    • Kishimura, H.1    Tokuda, Y.2    Klomklao, S.3    Benjakul, S.4    Ando, S.5
  • 22
    • 33749005389 scopus 로고    scopus 로고
    • Comparative study on enzymatic characteristics of trypsins from the pyloric ceca of yellow tail (Seriola quinqueradiata) and brown hakeling (Physiculus japonicus)
    • Kishimura H, Tokuda Y, Klomklao S, Benjakul S and Ando S, Comparative study on enzymatic characteristics of trypsins from the pyloric ceca of yellow tail (Seriola quinqueradiata) and brown hakeling (Physiculus japonicus). J Food Biochem 30:521-534 (2006).
    • (2006) J Food Biochem , vol.30 , pp. 521-534
    • Kishimura, H.1    Tokuda, Y.2    Klomklao, S.3    Benjakul, S.4    Ando, S.5
  • 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 Chem 106:194-199 (2008).
    • (2008) Food Chem , vol.106 , pp. 194-199
    • Kishimura, H.1    Klomklao, S.2    Benjakul, S.3    Chun, B.-S.4
  • 24
    • 0020410219 scopus 로고
    • Comparative biochemistry of the proteinases of eukaryotic microorganisms
    • North MJ, Comparative biochemistry of the proteinases of eukaryotic microorganisms. Microb Rev 46:308-340 (1982).
    • (1982) Microb Rev , vol.46 , pp. 308-340
    • North, M.J.1
  • 25
    • 0019879026 scopus 로고
    • Studies on proteinases from the digestive organs of sardine. Purification and characterization of three alkaline proteinases from the pyloric caeca
    • Murakami K and Noda M, Studies on proteinases from the digestive organs of sardine. Purification and characterization of three alkaline proteinases from the pyloric caeca. Biochim Biophys Acta B 65:17-26 (1981).
    • (1981) Biochim Biophys Acta B , vol.65 , pp. 17-26
    • Murakami, K.1    Noda, M.2
  • 26
    • 0025971420 scopus 로고
    • Isolation, purification and characterization of a trypsin from the pyloric caeca of mullet (Mugil cephalus)
    • Guizani N, Rolle RS, Marshall MR and Wie CI, Isolation, purification and characterization of a trypsin from the pyloric caeca of mullet (Mugil cephalus). Comp Biochem Physiol B 98:517-521 (1991).
    • (1991) Comp Biochem Physiol B , vol.98 , pp. 517-521
    • Guizani, N.1    Rolle, R.S.2    Marshall, M.R.3    Wie, C.I.4
  • 27
    • 0037566099 scopus 로고    scopus 로고
    • Partial purification and characterization of trimethylamine-N-oxide demethylase from lizardfish kidney
    • Benjakul S, Visessanguan Wand Tanaka M, Partial purification and characterization of trimethylamine-N-oxide demethylase from lizardfish kidney. Comp Biochem Physiol B 135:359-371 (2003).
    • (2003) Comp Biochem Physiol B , vol.135 , pp. 359-371
    • Benjakul, S.1    Visessanguan2    Wand Tanaka, M.3
  • 28
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases from a bioindustrial viewpoint
    • Kumar CG and Takagi H, Microbial alkaline proteases from a bioindustrial viewpoint. Biotechnol Adv 17:561-594 (1999).
    • (1999) Biotechnol Adv , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 29
    • 0032950882 scopus 로고    scopus 로고
    • Bleach-stable, alkaline protease from Bacillus sp
    • Gupta R, Gupta K, Saxena RK and Khan S, Bleach-stable, alkaline protease from Bacillus sp. Biotechnol Lett 21:135-138 (1999).
    • (1999) Biotechnol Lett , vol.21 , pp. 135-138
    • Gupta, R.1    Gupta, K.2    Saxena, R.K.3    Khan, S.4
  • 30
    • 33746755993 scopus 로고    scopus 로고
    • Trypsin-like enzyme from intestine and pyloric caeca of spotted goatfish (Pseudupeneus maculatus)
    • Souza AAG, Amaral IPG, Espirito Santo AR, Carvalho JRLB and Bezerra RS, Trypsin-like enzyme from intestine and pyloric caeca of spotted goatfish (Pseudupeneus maculatus). Food Chem 100:1429-1434 (2007).
    • (2007) Food Chem , vol.100 , pp. 1429-1434
    • Souza, A.A.G.1    Amaral, I.P.G.2    Espirito Santo, A.R.3    Carvalho, J.R.L.B.4    Bezerra, R.S.5
  • 31
    • 0024189838 scopus 로고
    • Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus
    • Martinez A, Olsen RL and Serra JL, Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus. Comp Biochem Physiol B 91:677-684 (1988).
    • (1988) Comp Biochem Physiol B , vol.91 , pp. 677-684
    • Martinez, A.1    Olsen, R.L.2    Serra, J.L.3
  • 32
    • 57149111217 scopus 로고    scopus 로고
    • Cohen T and Gertler A, Pancreatic proteolytic enzymes from carp (Cyprinus carpio). I. Purification and physical properties of trypsin, chymosin, elastase and carboxypeptidase B. Comp Biochem Physiol B98:647-653 (1981).
    • Cohen T and Gertler A, Pancreatic proteolytic enzymes from carp (Cyprinus carpio). I. Purification and physical properties of trypsin, chymosin, elastase and carboxypeptidase B. Comp Biochem Physiol B98:647-653 (1981).
  • 33
    • 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. Comp Biochem Physiol B 127:337-346 (2000).
    • (2000) Comp Biochem Physiol B , vol.127 , pp. 337-346
    • Sekizaki, H.1    Itoh, K.2    Murakami, M.3    Toyota, E.4    Tanizawa, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.