메뉴 건너뛰기




Volumn 35, Issue 4, 2005, Pages 291-299

Identification of protease from Euphorbia amygdaloides latex and its use in cheese production

Author keywords

Cheese production; Euphorbia amygdaloides; Protease

Indexed keywords

CASEIN; LATEX; PEPTIDE HYDROLASE;

EID: 27844568194     PISSN: 10826068     EISSN: 15322297     Source Type: Journal    
DOI: 10.1080/10826060500218107     Document Type: Article
Times cited : (14)

References (21)
  • 1
    • 0037376207 scopus 로고    scopus 로고
    • Porocerain, a stable cysteine protease from the latex of Calotropis Procera
    • Dubey, V.K.; Jagannadham, M.V. Porocerain, a stable cysteine protease from the latex of Calotropis Procera. Phytochemistry 2003, 62 (7), 1057-1071.
    • (2003) Phytochemistry , vol.62 , Issue.7 , pp. 1057-1071
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 2
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interaction of plant and other organisms
    • Dalling, M.J., Ed.; Boca Raton, FL
    • Boller, T. Roles of proteolytic enzymes in interaction of plant and other organisms. In Plant Proteolytic Enzymes; Dalling, M.J., Ed.; Boca Raton, FL, 1986; 67-96.
    • (1986) Plant Proteolytic Enzymes , pp. 67-96
    • Boller, T.1
  • 4
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assay
    • Kembhavi, A.A.; Buttle, D.J.; Knight, C.G.; Barrett, A.J. The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assay. Arch. Biochem. Biophys. 1993, 303, 208-213.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 6
    • 0014690242 scopus 로고    scopus 로고
    • Papaya lysozyme: Terminal sequences and enzymatic properties
    • Howard, J.B.; Glazer, A.N. Papaya lysozyme: Terminal sequences and enzymatic properties. J. Biol. Chem. 1996, 2446, 1399-1409.
    • (1996) J. Biol. Chem. , vol.2446 , pp. 1399-1409
    • Howard, J.B.1    Glazer, A.N.2
  • 7
    • 0012388036 scopus 로고
    • Studies of bacteriolytic enzyme from latex of Ervatamia coronaria
    • Kidwai, A.M.; Murti, C.R.K. Studies of bacteriolytic enzyme from latex of Ervatamia coronaria. Indian J. Chem. 1994, 1, 41-45.
    • (1994) Indian J. Chem. , vol.1 , pp. 41-45
    • Kidwai, A.M.1    Murti, C.R.K.2
  • 8
    • 0018786627 scopus 로고
    • Studies on proteinases from Calotropis gigantea latex. Purification and some properties of two proteinases containing carbohydrates
    • Abraham, I.; Joshi, P.N. Studies on proteinases from Calotropis gigantea latex. Purification and some properties of two proteinases containing carbohydrates. Biochim. Biophys. Acta 1979, 568, 111-119.
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 111-119
    • Abraham, I.1    Joshi, P.N.2
  • 9
    • 0015911270 scopus 로고
    • Multiple molecular forms of stem bromelain. Isolation and characterization of two closely related components, SB1 and SB2
    • Takahasi, N.; Yasuda, Y.; Goto, K.; Miyake, T.; Murachi, T. Multiple molecular forms of stem bromelain. Isolation and characterization of two closely related components, SB1 and SB2. J. Biochem. 1973, 74, 355-373.
    • (1973) J. Biochem. , vol.74 , pp. 355-373
    • Takahasi, N.1    Yasuda, Y.2    Goto, K.3    Miyake, T.4    Murachi, T.5
  • 10
    • 77049169880 scopus 로고
    • Crystalline Papain. I. Preparation, Specificity and activation
    • Kimmel, J.R.; Smith, E.L. Crystalline Papain. I. Preparation, Specificity and activation. J. Biol. Chem. 1954, 207, 515-531.
    • (1954) J. Biol. Chem. , vol.207 , pp. 515-531
    • Kimmel, J.R.1    Smith, E.L.2
  • 11
    • 0033517819 scopus 로고    scopus 로고
    • Structural characterization of highly stable cysteine protease Ervatamin C
    • Kundu, M.; Jagannadham, M.V. Structural characterization of highly stable cysteine protease Ervatamin C. Biochem. Biophys. Res. Comm. 1999, 264, 635-642.
    • (1999) Biochem. Biophys. Res. Comm. , vol.264 , pp. 635-642
    • Kundu, M.1    Jagannadham, M.V.2
  • 12
    • 3142519772 scopus 로고    scopus 로고
    • Proteolytic properties of Funastrum clausum latex
    • Morcelle, S.R.; Caffini, N.O.; Priolo, N. Proteolytic properties of Funastrum clausum latex. Fitoterapia 2004, 75, 480-493.
    • (2004) Fitoterapia , vol.75 , pp. 480-493
    • Morcelle, S.R.1    Caffini, N.O.2    Priolo, N.3
  • 14
    • 0036664583 scopus 로고    scopus 로고
    • Isolation and characterization of proteolytic enzymes from the lateks of Synadenium granthii Hook (F)
    • Menon, M.; Vithayathil, P.J.; Raju, S.M.; Ramadoss, C.S. Isolation and characterization of proteolytic enzymes from the lateks of Synadenium granthii Hook (F). Plant Sci. 2002, 163 (1), 131-139.
    • (2002) Plant Sci. , vol.163 , Issue.1 , pp. 131-139
    • Menon, M.1    Vithayathil, P.J.2    Raju, S.M.3    Ramadoss, C.S.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 17744405761 scopus 로고    scopus 로고
    • Immmobilization and characterization of ficin
    • Fadiloǧlu, S. Immmobilization and characterization of ficin. Nahrung/Food 2001, 45 (2), 143-146.
    • (2001) Nahrung/Food , vol.45 , Issue.2 , pp. 143-146
    • Fadiloǧlu, S.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 33947484782 scopus 로고
    • Determination of molecular weight of proteins by gel filtration on Sephadex
    • Whitaker, J.R. Determination of molecular weight of proteins by gel filtration on Sephadex. Anal. Chem. 1963, 35, 1950-1953.
    • (1963) Anal. Chem. , vol.35 , pp. 1950-1953
    • Whitaker, J.R.1
  • 19
    • 27844483352 scopus 로고    scopus 로고
    • Isolation and characterization of euphorbain 1,a proteinase from the latex of Euphorbia lathyris
    • Lynn, K.R.; Clevette-Radford, N.A. Isolation and characterization of euphorbain 1,a proteinase from the latex of Euphorbia lathyris. Phytochemistry 2003, 6 (7), 1057-1071.
    • (2003) Phytochemistry , vol.6 , Issue.7 , pp. 1057-1071
    • Lynn, K.R.1    Clevette-Radford, N.A.2
  • 20
    • 0037376207 scopus 로고    scopus 로고
    • Procerain, a stable cysteine protease from the latex of Calotropis procera
    • Dubey, V.K.; Jagannadham, M.V. Procerain, a stable cysteine protease from the latex of Calotropis procera.. Phytochemistry 2003, 62 (7), 1057-1071.
    • (2003) Phytochemistry , vol.62 , Issue.7 , pp. 1057-1071
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 21
    • 0842266152 scopus 로고    scopus 로고
    • Purification and some properties of a cysteine proteinase from soghum malt variety SK5912
    • Ogbonna, A.C.; Obi, S.K.C.; Okolo, B.N.; Odibo, F.J.C. Purification and some properties of a cysteine proteinase from soghum malt variety SK5912. J. Sci. Food Agric. 2004, 84 (2), 113-120.
    • (2004) J. Sci. Food Agric. , vol.84 , Issue.2 , pp. 113-120
    • Ogbonna, A.C.1    Obi, S.K.C.2    Okolo, B.N.3    Odibo, F.J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.