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Volumn 89, Issue 1, 2011, Pages 73-80

The partitioning of protease from Calotropis procera latex by aqueous two-phase systems and its hydrolytic pattern on muscle proteins

Author keywords

Aqueous two phase; Calotropis procera; Latex; Muscle protein; Protease

Indexed keywords

AQUEOUS TWO PHASE; AQUEOUS TWO PHASE SYSTEM; CALOTROPIS PROCERA; MUSCLE PROTEIN; MUSCLE PROTEINS; MYOFIBRILLAR PROTEINS; MYOSIN HEAVY CHAIN; POLYACRYLAMIDE GELS; PROTEASE; PROTEIN PATTERNS; RICH PHASE; SDS-PAGE; SODIUM DODECYL SULPHATE;

EID: 78751582332     PISSN: 09603085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fbp.2010.02.001     Document Type: Article
Times cited : (39)

References (39)
  • 1
    • 0036689388 scopus 로고    scopus 로고
    • Effects of papain and a microbial enzyme on meat proteins and beef tenderness
    • I.N.A. Ashie, T.L. Sorensen, and P.M. Nielsen Effects of papain and a microbial enzyme on meat proteins and beef tenderness J Food Sci 67 2002 2138 2142
    • (2002) J Food Sci , vol.67 , pp. 2138-2142
    • Ashie, I.N.A.1    Sorensen, T.L.2    Nielsen, P.M.3
  • 2
    • 35448929407 scopus 로고    scopus 로고
    • Liquid-liquid extraction of bromelain and polyphenol oxidase using aqueous two-phase system
    • B. Babu, N.K. Rastogi, and K.S.M.S. Raghavarao Liquid-liquid extraction of bromelain and polyphenol oxidase using aqueous two-phase system Chem Eng Process 47 2008 83 89
    • (2008) Chem Eng Process , vol.47 , pp. 83-89
    • Babu, B.1    Rastogi, N.K.2    Raghavarao, K.S.M.S.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 3042669270 scopus 로고    scopus 로고
    • Studies on anti-diarrhoeal activity of Calotropis gigantean R.BR. in experimental animals
    • H.R. Chitme, R. Chandra, and S. Kaushik Studies on anti-diarrhoeal activity of Calotropis gigantean R.BR. in experimental animals J Pharm Pharm Sci 7 2004 70 75
    • (2004) J Pharm Pharm Sci , vol.7 , pp. 70-75
    • Chitme, H.R.1    Chandra, R.2    Kaushik, S.3
  • 5
    • 0037376207 scopus 로고    scopus 로고
    • Procerain, a stable cysteine protease from the latex of Calotropis procera
    • V.K. Dubey, and M.V. Jagannadham Procerain, a stable cysteine protease from the latex of Calotropis procera Phytochemistry 62 2003 1057 1071
    • (2003) Phytochemistry , vol.62 , pp. 1057-1071
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 6
    • 4143072465 scopus 로고    scopus 로고
    • Influence of high concentration monovalent cations on the protein partitioning in polyethyleneglycol 1500-phosphate aqueous two-phase systems
    • B. Farruggia, R. Rigatuso, L. Capezio, V. Diez, and G. Pico Influence of high concentration monovalent cations on the protein partitioning in polyethyleneglycol 1500-phosphate aqueous two-phase systems J Chromatogr B 809 2004 301 306
    • (2004) J Chromatogr B , vol.809 , pp. 301-306
    • Farruggia, B.1    Rigatuso, R.2    Capezio, L.3    Diez, V.4    Pico, G.5
  • 8
    • 0027485558 scopus 로고
    • Substrate gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors
    • F.C. Garcia-Carreno, C.E. Dimes, and N.F. Haard Substrate gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors Anal Biochem 214 1993 65 69
    • (1993) Anal Biochem , vol.214 , pp. 65-69
    • Garcia-Carreno, F.C.1    Dimes, C.E.2    Haard, N.F.3
  • 9
    • 0031149715 scopus 로고    scopus 로고
    • Production of alkaline protease by Bacillus thuringiensis H 14 in aqueous two phase systems
    • S. Hotha, and R.M. Banik Production of alkaline protease by Bacillus thuringiensis H 14 in aqueous two phase systems J Chem Technol Biotechnol 69 1997 5 10
    • (1997) J Chem Technol Biotechnol , vol.69 , pp. 5-10
    • Hotha, S.1    Banik, R.M.2
  • 10
  • 13
    • 9644289558 scopus 로고
    • Effect of bacterial enzyme preparation on the solubility and electrophoretic properties of muscle proteins
    • V.K. Jorgova, S. Danchev, and A. Kostov Effect of bacterial enzyme preparation on the solubility and electrophoretic properties of muscle proteins Proc Int Congr Meat Sci Technol 35 1989 913 917
    • (1989) Proc Int Congr Meat Sci Technol , vol.35 , pp. 913-917
    • Jorgova, V.K.1    Danchev, S.2    Kostov, A.3
  • 14
    • 84987332280 scopus 로고
    • Tenderization of meat with papaya latex proteases
    • C.K. Kang, and W.D. Warner Tenderization of meat with papaya latex proteases J Food Sci 39 1974 812 818
    • (1974) J Food Sci , vol.39 , pp. 812-818
    • Kang, C.K.1    Warner, W.D.2
  • 15
    • 22544434368 scopus 로고    scopus 로고
    • Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems
    • S. Klomklao, S. Benjakul, W. Visessanguan, B.K. Simpson, and H. Kishimura Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems Process Biochem 40 2005 3061 3067
    • (2005) Process Biochem , vol.40 , pp. 3061-3067
    • Klomklao, S.1    Benjakul, S.2    Visessanguan, W.3    Simpson, B.K.4    Kishimura, H.5
  • 16
    • 33746738184 scopus 로고    scopus 로고
    • Purification and characterisation of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis)
    • S. Klomklao, S. Benjakul, W. Visessanguan, H. Kishimura, and B.K. Simpson Purification and characterisation of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis) Food Chem 100 2007 1580 1589
    • (2007) Food Chem , vol.100 , pp. 1580-1589
    • Klomklao, S.1    Benjakul, S.2    Visessanguan, W.3    Kishimura, H.4    Simpson, B.K.5
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0033380785 scopus 로고    scopus 로고
    • Tenderization of beef with pineapple juice monitored by Fourier transform infrared spectroscopy and chemometric analysis
    • K. Lizuka, and T. Aishima Tenderization of beef with pineapple juice monitored by Fourier transform infrared spectroscopy and chemometric analysis J Food Sci 64 1999 973 977
    • (1999) J Food Sci , vol.64 , pp. 973-977
    • Lizuka, K.1    Aishima, T.2
  • 19
    • 0032877729 scopus 로고    scopus 로고
    • Partial purification of penicillin acylase from Esherichia coli in poly(ethyleneglycol)-sodium citrate aqueous two-phase systems
    • J.C. Marcos, L.P. Fonseea, M.T. Ramalho, and J.M.S. Cabrae Partial purification of penicillin acylase from Esherichia coli in poly(ethyleneglycol)- sodium citrate aqueous two-phase systems J Chromatogr B 734 1999 15 22
    • (1999) J Chromatogr B , vol.734 , pp. 15-22
    • Marcos, J.C.1    Fonseea, L.P.2    Ramalho, M.T.3    Cabrae, J.M.S.4
  • 20
    • 0003692166 scopus 로고
    • The Benjamin/Cummings Publishing Company, Inc. New York
    • C.K. Mathews, and K.E. Holde Biochemistry 1990 The Benjamin/Cummings Publishing Company, Inc. New York
    • (1990) Biochemistry
    • Mathews, C.K.1    Holde, K.E.2
  • 21
    • 0030298253 scopus 로고    scopus 로고
    • Limited proteolysis of myofibrillar proteins by bromelain decreased toughness of coarse dry sausage
    • J.A. Melendo, J.A. Beltran, I. Jaime, R. Sancho, and P. Roncales Limited proteolysis of myofibrillar proteins by bromelain decreased toughness of coarse dry sausage Food Chem 57 1996 429 433
    • (1996) Food Chem , vol.57 , pp. 429-433
    • Melendo, J.A.1    Beltran, J.A.2    Jaime, I.3    Sancho, R.4    Roncales, P.5
  • 22
    • 0031422518 scopus 로고    scopus 로고
    • Tenderization of squid (Loligo vulgaris and Illex coindetii) with bromelain and a bovine spleen lysosomal-enriched extract
    • J.A. Melendo, J.A. Beltran, and P. Roncales Tenderization of squid (Loligo vulgaris and Illex coindetii) with bromelain and a bovine spleen lysosomal-enriched extract Food Res Int 30 1997 335 341
    • (1997) Food Res Int , vol.30 , pp. 335-341
    • Melendo, J.A.1    Beltran, J.A.2    Roncales, P.3
  • 23
    • 2342576244 scopus 로고    scopus 로고
    • Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles
    • J.L. Melody, S.M. Lonergan, L.J. Rowe, T.W. Huiatt, M.S. Mayes, and E. Huff-Lonergan Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles J Anim Sci 82 2004 1195 1205
    • (2004) J Anim Sci , vol.82 , pp. 1195-1205
    • Melody, J.L.1    Lonergan, S.M.2    Rowe, L.J.3    Huiatt, T.W.4    Mayes, M.S.5    Huff-Lonergan, E.6
  • 24
    • 73549115553 scopus 로고    scopus 로고
    • Staining of glycoproteins/proteoglycans in SDS-Gels
    • H.J. Moller, and J.H. Poulsen Staining of glycoproteins/proteoglycans in SDS-Gels J.M. Walker, The Protein Protocols Handbook 2002 Humann Press Springer-Verlag Berlin 627 631
    • (2002) The Protein Protocols Handbook , pp. 627-631
    • Moller, H.J.1    Poulsen, J.H.2
  • 25
    • 3142519772 scopus 로고    scopus 로고
    • Proteolytic property of Funastrum clausum latex, Ireland
    • S.R. Morcelle, N.O. Caffini, and N. Priolo Proteolytic property of Funastrum clausum latex, Ireland J Fitot 75 2004 480 483
    • (2004) J Fitot , vol.75 , pp. 480-483
    • Morcelle, S.R.1    Caffini, N.O.2    Priolo, N.3
  • 26
    • 62349127671 scopus 로고    scopus 로고
    • Partitioning of protease from stomach of albacore tuna (Thunnus alalunga) by aqueous-two phase systems
    • S. Nalinanon, S. Benjakul, W. Visessanguan, and H. Kishimura Partitioning of protease from stomach of albacore tuna (Thunnus alalunga) by aqueous-two phase systems Process Biochem 44 2009 471 476
    • (2009) Process Biochem , vol.44 , pp. 471-476
    • Nalinanon, S.1    Benjakul, S.2    Visessanguan, W.3    Kishimura, H.4
  • 27
    • 9644275379 scopus 로고    scopus 로고
    • Tenderizaiton of buffalo meat using plant proteases from Cucumis trigounus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome)
    • B.M. Naveena, S.K. Mendiratta, and A.S.R. Anjaneyulu Tenderizaiton of buffalo meat using plant proteases from Cucumis trigounus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome) Meat Sci 68 2004 363 369
    • (2004) Meat Sci , vol.68 , pp. 363-369
    • Naveena, B.M.1    Mendiratta, S.K.2    Anjaneyulu, A.S.R.3
  • 28
    • 33745959045 scopus 로고    scopus 로고
    • Purification of papain from Carica papaya latex: Aqueous two-phase extraction versus two-step salt precipitation
    • S. Nitsawang, R. Hatti-Kaul, and P. Kanasawuda Purification of papain from Carica papaya latex: aqueous two-phase extraction versus two-step salt precipitation Enzyme Microb Technol 39 2006 1103 1107
    • (2006) Enzyme Microb Technol , vol.39 , pp. 1103-1107
    • Nitsawang, S.1    Hatti-Kaul, R.2    Kanasawuda, P.3
  • 29
    • 0002674514 scopus 로고    scopus 로고
    • Recent developments in aqueous two-phase extraction in bioprocessing
    • K.S.M.S. Raghavarao, M.R. Ruinn, and P. Todd Recent developments in aqueous two-phase extraction in bioprocessing Sep Purif Method 27 1998 1 49
    • (1998) Sep Purif Method , vol.27 , pp. 1-49
    • Raghavarao, K.S.M.S.1    Ruinn, M.R.2    Todd, P.3
  • 30
    • 0037175436 scopus 로고    scopus 로고
    • Isolation of alpha-1-antitrypsin from human plasma by partitioning in aqueous biphasis systems of polyethyleneglycol phosphate
    • G. Reh, B. Nerli, and G. Pico Isolation of alpha-1-antitrypsin from human plasma by partitioning in aqueous biphasis systems of polyethyleneglycol phosphate J Chromatogr B 780 2002 389 396
    • (2002) J Chromatogr B , vol.780 , pp. 389-396
    • Reh, G.1    Nerli, B.2    Pico, G.3
  • 31
    • 0037281333 scopus 로고    scopus 로고
    • Effect of chemically modified soy proteins and ficin-tenderized meat on the quality attributes of sausage
    • R. Remezani, M. Aminlari, and H. Fallahi Effect of chemically modified soy proteins and ficin-tenderized meat on the quality attributes of sausage J Food Sci 68 2003 85 88
    • (2003) J Food Sci , vol.68 , pp. 85-88
    • Remezani, R.1    Aminlari, M.2    Fallahi, H.3
  • 33
    • 20344378937 scopus 로고    scopus 로고
    • Features of the acid protease partition in aqueous two-phase systems of polyethylene glycol-phosphate: Chymosin and pepsin
    • D. Spelzini, B. Farruggia, and G. Pico Features of the acid protease partition in aqueous two-phase systems of polyethylene glycol-phosphate: chymosin and pepsin J Chromatogr B 821 2005 60 66
    • (2005) J Chromatogr B , vol.821 , pp. 60-66
    • Spelzini, D.1    Farruggia, B.2    Pico, G.3
  • 34
  • 35
    • 34249752702 scopus 로고    scopus 로고
    • Partitioning features of bovine trypsin and a-chymotrypsin in polyethyleneglycol-sodium citrate aqueous two-phase systems
    • G. Tubio, B. Nerli, and G. Pico Partitioning features of bovine trypsin and a-chymotrypsin in polyethyleneglycol-sodium citrate aqueous two-phase systems J Chromatogr B 852 2007 244 249
    • (2007) J Chromatogr B , vol.852 , pp. 244-249
    • Tubio, G.1    Nerli, B.2    Pico, G.3
  • 36
    • 58149279258 scopus 로고    scopus 로고
    • Extraction of trypsin from bovine pancreas by applying polyethyleneglycol/sodium citrate aqueous two-phase systems
    • G. Tubio, G.A. Pico, and B.B. Nerli Extraction of trypsin from bovine pancreas by applying polyethyleneglycol/sodium citrate aqueous two-phase systems J Chromatogr B 877 2009 115 120
    • (2009) J Chromatogr B , vol.877 , pp. 115-120
    • Tubio, G.1    Pico, G.A.2    Nerli, B.B.3
  • 37
    • 33846263350 scopus 로고    scopus 로고
    • Characterization of news proteolytic enzymes from ripe fruits of bromelia antiacantha bertol (Bromeliaceae)
    • D. Vallés, S. Furtado, and A.M.B. Cantera Characterization of news proteolytic enzymes from ripe fruits of bromelia antiacantha bertol (Bromeliaceae) Enzyme Microb Technol 40 2007 409 413
    • (2007) Enzyme Microb Technol , vol.40 , pp. 409-413
    • Vallés, D.1    Furtado, S.2    Cantera, A.M.B.3
  • 39
    • 22144495399 scopus 로고    scopus 로고
    • Purification and stabilization of ricin B from tobacco hairy root culture medium by aqueous two-phase extraction
    • C. Zhang, F. Medina-Bolivar, S. Buswell, and C.L. Cramer Purification and stabilization of ricin B from tobacco hairy root culture medium by aqueous two-phase extraction J Biotechnol 117 2005 39 48
    • (2005) J Biotechnol , vol.117 , pp. 39-48
    • Zhang, C.1    Medina-Bolivar, F.2    Buswell, S.3    Cramer, C.L.4


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