메뉴 건너뛰기




Volumn 134, Issue 3, 2012, Pages 1267-1278

Protein and mineral characterisation of rendered meat and bone meal

Author keywords

Collagen; MALDI; MBM; Osteocalcin; Species identification

Indexed keywords

AMINO ACID COMPOSITIONS; MALDI; MAMMALIAN TISSUES; MBM; MEAT AND BONE MEAL; OSTEOCALCIN; PROTEIN DAMAGE; SMALL ANGLE X-RAY DIFFRACTIONS; SPECIES COMPOSITION; SPECIES IDENTIFICATION; SPECTROMETRIC METHODS; STRUCTURAL PROTEINS; TREATMENT TEMPERATURE; TYPE I COLLAGEN;

EID: 84861100344     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2012.02.167     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 79954967870 scopus 로고    scopus 로고
    • Determination of osteocalcin in meat and bone meal of bovine and porcine origin using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry and high-resolution hybrid mass spectrometry
    • G. Balizs, C. Weise, C. Rozycki, T. Opialla, S. Sawada, and J. Zagon Determination of osteocalcin in meat and bone meal of bovine and porcine origin using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry and high-resolution hybrid mass spectrometry Analytica Chimica Acta 693 2011 89 99
    • (2011) Analytica Chimica Acta , vol.693 , pp. 89-99
    • Balizs, G.1    Weise, C.2    Rozycki, C.3    Opialla, T.4    Sawada, S.5    Zagon, J.6
  • 2
    • 71949102106 scopus 로고    scopus 로고
    • Species identification by analysis of bone collagen using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry
    • M. Buckley, M. Collins, J. Thomas-Oates, and J.C. Wilson Species identification by analysis of bone collagen using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry Rapid Communications in Mass Spectrometry 23 2009 3843 3854
    • (2009) Rapid Communications in Mass Spectrometry , vol.23 , pp. 3843-3854
    • Buckley, M.1    Collins, M.2    Thomas-Oates, J.3    Wilson, J.C.4
  • 5
    • 0001756579 scopus 로고    scopus 로고
    • Towards an optimal method of archaeological collagen extraction; The influence of pH and grinding
    • M.J. Collins, and P. Galley Towards an optimal method of archaeological collagen extraction; the influence of pH and grinding Ancient Biomolecules 2 1998 209 222
    • (1998) Ancient Biomolecules , vol.2 , pp. 209-222
    • Collins, M.J.1    Galley, P.2
  • 7
    • 0010381849 scopus 로고
    • Amino acids and proteins from fossils
    • Broadhead, T.W. (ed.) The Palaeontology Society, Knoxville, Tennessee, USA
    • Curry, G. B. (1988). Amino acids and proteins from fossils. In: Broadhead, T.W. (ed.) Molecular Evolution and the Fossil Record. Short Courses in Palaeontology (1). The Palaeontology Society, Knoxville, Tennessee, USA, pp. 20-33.
    • (1988) Molecular Evolution and the Fossil Record. Short Courses in Palaeontology , Issue.1 , pp. 20-33
    • Curry, G.B.1
  • 10
    • 0030033534 scopus 로고    scopus 로고
    • Bone mineralization in an osteogenesis imperfecta mouse model studied by small angle x-ray scattering
    • P. Fratzl, O. Paris, K. Klaushofer, and W.J. Landis Bone mineralization in an osteogenesis imperfecta mouse model studied by small angle x-ray scattering Journal of Clinical Investigation 97 1996 396 402
    • (1996) Journal of Clinical Investigation , vol.97 , pp. 396-402
    • Fratzl, P.1    Paris, O.2    Klaushofer, K.3    Landis, W.J.4
  • 12
  • 14
    • 4544329562 scopus 로고    scopus 로고
    • Small-angle X-ray scattering: A high-throughput technique for investigating archaeological bone preservation
    • J.C. Hiller, M.J. Collins, A.T. Chamberlain, and T.J. Wess Small-angle X-ray scattering: a high-throughput technique for investigating archaeological bone preservation Journal of Archaeological Science 31 2004 1349 1359
    • (2004) Journal of Archaeological Science , vol.31 , pp. 1349-1359
    • Hiller, J.C.1    Collins, M.J.2    Chamberlain, A.T.3    Wess, T.J.4
  • 15
    • 0031878633 scopus 로고    scopus 로고
    • Monoclonal antibodies to porcine thermal-stable muscle protein for detection of pork in raw and cooked meats
    • F.C. Chen, Y.H.P. Hsieh, and R.C. Bridgman Monoclonal antibodies to porcine thermal-stable muscle protein for detection of pork in raw and cooked meats Journal of Food Sciences 63 1998 201 205
    • (1998) Journal of Food Sciences , vol.63 , pp. 201-205
    • Chen, F.C.1    Hsieh, Y.H.P.2    Bridgman, R.C.3
  • 16
    • 0031735136 scopus 로고    scopus 로고
    • A new procedure for determining enantiomeric DL amino acid ratios in fossils using reverse phase liquid chromatography
    • D.S. Kaufman, and W.F. Manley A new procedure for determining enantiomeric DL amino acid ratios in fossils using reverse phase liquid chromatography Quaternary Science Reviews 17 11 1998 987 1000
    • (1998) Quaternary Science Reviews , vol.17 , Issue.11 , pp. 987-1000
    • Kaufman, D.S.1    Manley, W.F.2
  • 17
    • 10644291255 scopus 로고    scopus 로고
    • Identification of a biomarker for the detection of prohibited meat and bone meal residues in animal feed
    • S.H. Kim, T.S. Huang, T.A. Seymour, C.I. Wei, S.C. Kempf, and C.R. Bridgman Identification of a biomarker for the detection of prohibited meat and bone meal residues in animal feed Journal of Food Science 69 2004 C739 C745
    • (2004) Journal of Food Science , vol.69
    • Kim, S.H.1    Huang, T.S.2    Seymour, T.A.3    Wei, C.I.4    Kempf, S.C.5    Bridgman, C.R.6
  • 19
    • 0030046726 scopus 로고    scopus 로고
    • Thermal stabilization of collagen fibers by calcification
    • P.L. Kronick, and P. Cooke Thermal stabilization of collagen fibers by calcification Connective Tissue Research 33 1996 275 282
    • (1996) Connective Tissue Research , vol.33 , pp. 275-282
    • Kronick, P.L.1    Cooke, P.2
  • 20
    • 0042769113 scopus 로고    scopus 로고
    • Age dependence of in situ termostability of collagen in human bone
    • X. Li, C.M. Agrawal, and X. Wang Age dependence of in situ termostability of collagen in human bone Calcified Tissue International 72 2003 513 518
    • (2003) Calcified Tissue International , vol.72 , pp. 513-518
    • Li, X.1    Agrawal, C.M.2    Wang, X.3
  • 21
    • 0001217622 scopus 로고
    • Amino acid racemization in heated and alkali-treated proteins
    • R. Liardon, and R.F. Hurrel Amino acid racemization in heated and alkali-treated proteins Journal of Agricultural Food Chemistry 31 1983 432 437
    • (1983) Journal of Agricultural Food Chemistry , vol.31 , pp. 432-437
    • Liardon, R.1    Hurrel, R.F.2
  • 23
    • 0007885440 scopus 로고
    • Effects of carcass maturity on collagen solubility and palatability of beef from grain-finished steers
    • R.K. Miller, J.D. Tatum, H.R. Cross, R.A. Bowling, and R.P. Clayton Effects of carcass maturity on collagen solubility and palatability of beef from grain-finished steers Journal of Food Science 48 1983 484 486
    • (1983) Journal of Food Science , vol.48 , pp. 484-486
    • Miller, R.K.1    Tatum, J.D.2    Cross, H.R.3    Bowling, R.A.4    Clayton, R.P.5
  • 25
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data the protein inference problem
    • A.I. Nesvizhskii, and R. Aebersold Interpretation of shotgun proteomic data the protein inference problem Molecular & Cellular Proteomics 4 2005 1419 1440
    • (2005) Molecular & Cellular Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 26
    • 33646206403 scopus 로고    scopus 로고
    • Biomolecules in fossil remains
    • Nielsen-Marsh, C. M. (2002). Biomolecules in fossil remains. The Biochemist, 12-14.
    • (2002) The Biochemist , pp. 12-14
    • Nielsen-Marsh, C.M.1
  • 28
    • 78649390387 scopus 로고    scopus 로고
    • The role of collagen in bone apatite formation in the presence of hydroxyapatite nucleation inhibitors
    • F. Nudelman, K. Pieterse, A. George, P.H.H. Bomans, H. Friedrich, and L.J. Brylka The role of collagen in bone apatite formation in the presence of hydroxyapatite nucleation inhibitors Nature Materials 9 2010 1004 1008
    • (2010) Nature Materials , vol.9 , pp. 1004-1008
    • Nudelman, F.1    Pieterse, K.2    George, A.3    Bomans, P.H.H.4    Friedrich, H.5    Brylka, L.J.6
  • 29
    • 1342280431 scopus 로고    scopus 로고
    • BSE Control: Detection of gelatine-derived peptides in animal feed by mass spectrometry
    • M.F. Ocaña, H. Neubert, A. Przyborowska, R. Parker, P. Bramley, and J. Halket BSE Control: Detection of gelatine-derived peptides in animal feed by mass spectrometry Analyst 129 2004 111 115
    • (2004) Analyst , vol.129 , pp. 111-115
    • Ocaña, M.F.1    Neubert, H.2    Przyborowska, A.3    Parker, R.4    Bramley, P.5    Halket, J.6
  • 31
    • 0034010048 scopus 로고    scopus 로고
    • New strategies for characterizing ancient proteins using matrix-assisted laser desorption ionization mass spectrometry
    • P. Ostrom, M. Schall, H. Gandhi, T. Shen, P. Hauschka, and J. Strahler New strategies for characterizing ancient proteins using matrix-assisted laser desorption ionization mass spectrometry Geochimica et Cosmochimica Acta 64 2000 1043 1050
    • (2000) Geochimica et Cosmochimica Acta , vol.64 , pp. 1043-1050
    • Ostrom, P.1    Schall, M.2    Gandhi, H.3    Shen, T.4    Hauschka, P.5    Strahler, J.6
  • 32
    • 0029663543 scopus 로고    scopus 로고
    • Amino acid racemization and the preservation of ancient DNA
    • H.N. Poinar, M. Hoss, J.L. Bada, and S. Paabo Amino acid racemization and the preservation of ancient DNA Science 272 1996 864 866
    • (1996) Science , vol.272 , pp. 864-866
    • Poinar, H.N.1    Hoss, M.2    Bada, J.L.3    Paabo, S.4
  • 34
    • 0031572274 scopus 로고    scopus 로고
    • Characterization of the complex between bovine osteocalcin and type i collagen
    • R.V. Prigodich, and M.R. Vesely Characterization of the complex between bovine osteocalcin and type I collagen Archives of Biochemistry and Biophysics 345 1997 339 341
    • (1997) Archives of Biochemistry and Biophysics , vol.345 , pp. 339-341
    • Prigodich, R.V.1    Vesely, M.R.2
  • 37
    • 0032215135 scopus 로고    scopus 로고
    • The effects of conformational constraints on aspartic acid racemization
    • A.C.T. Van Duin, and M.J. Collins The effects of conformational constraints on aspartic acid racemization Organic Geochemistry 29 1998 1227 1232
    • (1998) Organic Geochemistry , vol.29 , pp. 1227-1232
    • Van Duin, A.C.T.1    Collins, M.J.2
  • 38
    • 0001378397 scopus 로고
    • Dead Sea scrolls parchments: Unfolding of the collagen molecules and racemization of aspartic acid
    • S. Weiner, Z. Kustanovich, E. Gil-Av, and W. Traub Dead Sea scrolls parchments: unfolding of the collagen molecules and racemization of aspartic acid Nature 287 1980 820 823
    • (1980) Nature , vol.287 , pp. 820-823
    • Weiner, S.1    Kustanovich, Z.2    Gil-Av, E.3    Traub, W.4
  • 39
    • 0036479472 scopus 로고    scopus 로고
    • Microfocus small angle X-ray scattering reveals structural features in archaeological bone samples: Detection of changes in bone mineral habit and size
    • T. Wess, I. Alberts, J. Hiller, M. Drakopoulos, A.T. Chamberlain, and M. Collins Microfocus small angle X-ray scattering reveals structural features in archaeological bone samples: Detection of changes in bone mineral habit and size Calcified Tissue International 70 2002 103 110
    • (2002) Calcified Tissue International , vol.70 , pp. 103-110
    • Wess, T.1    Alberts, I.2    Hiller, J.3    Drakopoulos, M.4    Chamberlain, A.T.5    Collins, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.