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Volumn 61, Issue 23, 2013, Pages 5449-5458

Application potential of ATR-FT/IR molecular spectroscopy in animal nutrition: Revelation of protein molecular structures of canola meal and presscake, as affected by heat-processing methods, in relationship with their protein digestive behavior and utilization for dairy cattle

Author keywords

helix; ATR FT IR molecular spectroscopy; canola; heat processing condition; protein nutritive value; protein secondary structure

Indexed keywords

CANOLA; HEAT-PROCESSING CONDITION; MICROBIAL PROTEINS; MOLECULAR STRUCTURAL; NUTRIENT UTILIZATION; NUTRITIVE VALUES; PROTEIN MOLECULAR STRUCTURES; PROTEIN SECONDARY STRUCTURE;

EID: 84879023651     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf400301y     Document Type: Article
Times cited : (68)

References (40)
  • 1
    • 0037199931 scopus 로고    scopus 로고
    • An analysis of the nutritive value of heat processed legume seeds for animal production using the DVE/OEB model: A review
    • DOI 10.1016/S0377-8401(02)00114-1, PII S0377840102001141
    • Yu, P.; Goelema, J. O.; Leury, B. J.; Tamminga, S.; Egan, A. R. An analysis of the nutritive value of heat processed legume seeds for animal production using the DVE/OEB model: a review Anim. Feed Sci. Technol. 2002, 99, 141-176 (Pubitemid 34961429)
    • (2002) Animal Feed Science and Technology , vol.99 , Issue.1-4 , pp. 141-176
    • Yu, P.1    Goelema, J.O.2    Leury, B.J.3    Tamminga, S.4    Egan, A.R.5
  • 2
    • 84986870266 scopus 로고
    • Thermal inactivation of lectins and trypsin inhibitor activity during steam processing of dry beans (Phaseolus vulgaris) and effects on protein quality
    • Van der Poel, A. F. B.; Blonk, J.; Van Zuilichem, D. J.; Van Ort, M. G. Thermal inactivation of lectins and trypsin inhibitor activity during steam processing of dry beans (Phaseolus vulgaris) and effects on protein quality J. Sci. Food Agric. 1990, 53, 215-228
    • (1990) J. Sci. Food Agric. , vol.53 , pp. 215-228
    • Van Der Poel, A.F.B.1    Blonk, J.2    Van Zuilichem, D.J.3    Van Ort, M.G.4
  • 3
    • 33646490012 scopus 로고    scopus 로고
    • Use of synchrotron-based FT/IR microspectroscopy to determine protein secondary structures of raw and heat treated brown and golden flaxseeds: A novel approach
    • Yu, P.; McKinnon, J. J.; Soita, H. W.; Christensen, C. R.; Christensen, D. A. Use of synchrotron-based FT/IR microspectroscopy to determine protein secondary structures of raw and heat treated brown and golden flaxseeds: a novel approach Can. J. Anim. Sci. 2005, 85, 437-448
    • (2005) Can. J. Anim. Sci. , vol.85 , pp. 437-448
    • Yu, P.1    McKinnon, J.J.2    Soita, H.W.3    Christensen, C.R.4    Christensen, D.A.5
  • 4
    • 0027354723 scopus 로고
    • Effect of the protein matrix on the digestion of cereal grains by ruminal microorganisms
    • McAllister, T. A.; Phillippe, R. C.; Rode, L. M.; Cheng, K. J. Effect of the protein matrix on the digestion of cereal grains by ruminal microorganisms J. Anim. Sci. 1993, 71, 205-212
    • (1993) J. Anim. Sci. , vol.71 , pp. 205-212
    • McAllister, T.A.1    Phillippe, R.C.2    Rode, L.M.3    Cheng, K.J.4
  • 5
    • 0027461064 scopus 로고
    • Peptide conformation and protein folding
    • DOI 10.1016/0959-440X(93)90203-W
    • Dyson, H. J.; Wright, P. E. Peptide conformation and protein folding Curr. Opin. Struct. Biol. 1990, 3, 60-65 (Pubitemid 23058384)
    • (1993) Current Opinion in Structural Biology , vol.3 , Issue.1 , pp. 60-65
    • Dyson, H.J.1    Wright, P.E.2
  • 6
    • 0003954817 scopus 로고    scopus 로고
    • 3 rd ed. McGraw-Hill: New York.
    • Carey, F. A. Organic Chemistry, 3 rd ed.; McGraw-Hill: New York, 1996.
    • (1996) Organic Chemistry
    • Carey, F.A.1
  • 7
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M.; Mantsch, H. H. The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 1995, 30, 95-120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 8
    • 25444455001 scopus 로고    scopus 로고
    • Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: A new approach
    • DOI 10.1079/BJN20051532
    • Yu, P. Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach Br. J. Nutr. 2005, 94, 655-665 (Pubitemid 41672368)
    • (2005) British Journal of Nutrition , vol.94 , Issue.5 , pp. 655-665
    • Yu, P.1
  • 9
    • 78349267213 scopus 로고    scopus 로고
    • Plant-based food and feed protein structure changes induced by gene-transformation, heating and bio-ethanol processing: A synchrotron-based molecular structure and nutrition research program
    • Yu, P. Plant-based food and feed protein structure changes induced by gene-transformation, heating and bio-ethanol processing: a synchrotron-based molecular structure and nutrition research program Mol. Nutr. Food Res. 2010, 54, 1535-1545
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 1535-1545
    • Yu, P.1
  • 10
    • 84879008336 scopus 로고    scopus 로고
    • New approach in protein research
    • In; Columbus, F. Nova Science: New York.
    • Yu, P. New approach in protein research. In Trends in Dietary Protein Research; Columbus, F., Ed.; Nova Science: New York, 2006.
    • (2006) Trends in Dietary Protein Research
    • Yu, P.1
  • 11
    • 84859528395 scopus 로고    scopus 로고
    • Molecular basis of protein structure in combined feeds (hulless barley with bioethanol coproduct of wheat dried distillers grains with solubles) in relation to protein rumen degradation kinetics and intestinal availability in dairy cattle
    • Zhang, X.; Yu, P. Molecular basis of protein structure in combined feeds (hulless barley with bioethanol coproduct of wheat dried distillers grains with solubles) in relation to protein rumen degradation kinetics and intestinal availability in dairy cattle J. Dairy Sci. 2012, 95, 3363-3379
    • (2012) J. Dairy Sci. , vol.95 , pp. 3363-3379
    • Zhang, X.1    Yu, P.2
  • 12
    • 4344582046 scopus 로고    scopus 로고
    • Probing equivocal effects of heat processing of legume seeds on performance of ruminants - A review
    • Yu, P.; Tamminga, S.; Egan, A. R.; Christensen, D. A. Probing equivocal effects of heat processing of legume seeds on performance of ruminants-a review Asian-Aust. J. Anim. Sci. 2004, 17, 869-876 (Pubitemid 39151530)
    • (2004) Asian-Australasian Journal of Animal Sciences , vol.17 , Issue.6 , pp. 869-876
    • Yu, P.1    Tamminga, S.2    Egan, A.R.3    Christensen, D.A.4
  • 13
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • DOI 10.1111/j.1745-7270.2007.00320.x
    • Kong, J.; Yu, S. Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochem. Biophys. Sin. 2007, 39, 549-559 (Pubitemid 47293710)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 14
    • 82155171336 scopus 로고    scopus 로고
    • Dry and moist heating-induced changes in protein molecular structure, protein subfraction, and nutrient profiles in soybeans
    • Samadi, T.; Yu, P. Dry and moist heating-induced changes in protein molecular structure, protein subfraction, and nutrient profiles in soybeans J. Dairy Sci. 2011, 94, 6092-6102
    • (2011) J. Dairy Sci. , vol.94 , pp. 6092-6102
    • Samadi, T.1    Yu, P.2
  • 15
    • 84877615510 scopus 로고    scopus 로고
    • Effect of processing conditions on the nutritive value of canola meal and canola presscake. Comparison of the yellow-seeded (Brassica juncea) and the brown-seeded (Brassica napus) canola meal with the brown-seeded (Brassica napus) canola presscake
    • Theodoridou, K.; Yu, P. Effect of processing conditions on the nutritive value of canola meal and canola presscake. Comparison of the yellow-seeded (Brassica juncea) and the brown-seeded (Brassica napus) canola meal with the brown-seeded (Brassica napus) canola presscake J. Sci. Food Agric. 2013, 93, 1986-1995
    • (2013) J. Sci. Food Agric. , vol.93 , pp. 1986-1995
    • Theodoridou, K.1    Yu, P.2
  • 16
    • 84875425297 scopus 로고    scopus 로고
    • Metabolic characteristics of the proteins in yellow-seeded and brown-seeded canola meal and presscake in dairy cattle: Comparison of three systems (PDI, DVE, and NRC) in nutrient supply and feed milk value (FMV)
    • Theodoridou, K.; Yu, P. Metabolic characteristics of the proteins in yellow-seeded and brown-seeded canola meal and presscake in dairy cattle: comparison of three systems (PDI, DVE, and NRC) in nutrient supply and feed milk value (FMV) J. Agric. Food Chem. 2013, 61, 2820-2830
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 2820-2830
    • Theodoridou, K.1    Yu, P.2
  • 17
    • 33646320949 scopus 로고
    • The estimation of protein degradability in the rumen from incubation measurements weighted according to rate of passage
    • Ørskov, E. R.; McDonald, I. The estimation of protein degradability in the rumen from incubation measurements weighted according to rate of passage J. Agric. Sci. 1979, 92, 499-503
    • (1979) J. Agric. Sci. , vol.92 , pp. 499-503
    • Ørskov, E.R.1    McDonald, I.2
  • 18
    • 38249043990 scopus 로고
    • Evaluation of mathematical models to describe neutral detergent residue in terms of its susceptibility to degradation in the rumen
    • Robinson, P. H.; Fadel, J. G.; Tamminga, S. Evaluation of mathematical models to describe neutral detergent residue in terms of its susceptibility to degradation in the rumen Anim. Feed Sci. Technol. 1986, 15, 249-271
    • (1986) Anim. Feed Sci. Technol. , vol.15 , pp. 249-271
    • Robinson, P.H.1    Fadel, J.G.2    Tamminga, S.3
  • 19
    • 84984499932 scopus 로고
    • On the analysis of dacron bag data for low degradability feeds
    • Dhanoa, M. On the analysis of dacron bag data for low degradability feeds Grass Forage Sci. 1988, 43, 441-444
    • (1988) Grass Forage Sci. , vol.43 , pp. 441-444
    • Dhanoa, M.1
  • 22
    • 0031993533 scopus 로고    scopus 로고
    • FT-IR microspectroscopic imaging of flax (Linum usitatissimum L.) stems
    • Himmelsbach, D. S.; Khalili, S.; Akin, D. E. FT-IR microspectroscopic imaging of flax (Linum usitatissimum L.) stems Cell. Mol. Biol. 1998, 44, 99-108
    • (1998) Cell. Mol. Biol. , vol.44 , pp. 99-108
    • Himmelsbach, D.S.1    Khalili, S.2    Akin, D.E.3
  • 24
    • 0037437320 scopus 로고    scopus 로고
    • Revealing protein infrared spectral detail in a heterogeneous matrix dominated by starch
    • Wetzel, D. L.; Srivarin, P.; Finney, J. R. Revealing protein infrared spectral detail in a heterogeneous matrix dominated by starch Vib. Spectrosc. 2003, 31, 109-114
    • (2003) Vib. Spectrosc. , vol.31 , pp. 109-114
    • Wetzel, D.L.1    Srivarin, P.2    Finney, J.R.3
  • 25
    • 84879011449 scopus 로고    scopus 로고
    • Infrared microspectroscopy and imaging [online], National Synchrotron Light Source, Brookhaven National Laboratory; available at (accessed Aug 15).
    • Miller, L. M. Infrared microspectroscopy and imaging [online], National Synchrotron Light Source, Brookhaven National Laboratory; available at http://www.nsls.bnl.gov/newsroom/publications/otherpubs/imaging/ workshopmillerhighres.pdf (accessed Aug 15, 2011).
    • (2011)
    • Miller, L.M.1
  • 26
    • 11144309346 scopus 로고    scopus 로고
    • Applications of vibrational spectroscopy in life, pharmaceutical and natural sciences
    • In; Chalmers, J. M. Griffiths, P. R. Wiley: New York, Vol. 5
    • Budevska, B. O. Applications of vibrational spectroscopy in life, pharmaceutical and natural sciences. In Handbook of Vibrational Spectroscopy; Chalmers, J. M.; Griffiths, P. R., Eds.; Wiley: New York, 2002; Vol. 5, pp 3720-3732.
    • (2002) Handbook of Vibrational Spectroscopy , pp. 3720-3732
    • Budevska, B.O.1
  • 27
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • DOI 10.1016/j.bbabio.2007.06.004, PII S0005272807001375
    • Barth, A. Infrared spectroscopy of proteins Biochim. Biophys. Acta-Bioenergetics 2007, 1767, 1073-1101 (Pubitemid 47313388)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.9 , pp. 1073-1101
    • Barth, A.1
  • 28
    • 0038349442 scopus 로고    scopus 로고
    • Ex vivo tissue analysis by infrared spectroscopy
    • In; Meyers, R. A. Wiley: Chichester, UK, Vol. 1
    • Jackson, M.; Mantsch, H. H. Ex vivo tissue analysis by infrared spectroscopy. In Encyclopedia of Analytical Chemistry; Meyers, R. A., Ed.; Wiley: Chichester, UK, 2000; Vol. 1, pp 131-156.
    • (2000) Encyclopedia of Analytical Chemistry , pp. 131-156
    • Jackson, M.1    Mantsch, H.H.2
  • 29
    • 0003419256 scopus 로고    scopus 로고
    • SAS. version 9.3; SAS Institute, Inc. Cary, NC
    • SAS. User's Guide: Statistics, version 9.3; SAS Institute, Inc.: Cary, NC, 2003
    • (2003) User's Guide: Statistics
  • 30
    • 0003067652 scopus 로고    scopus 로고
    • A macro for converting mean separation output to letter groupings
    • In; SAS Institute: Cary, NC.
    • Saxton, A. M. A macro for converting mean separation output to letter groupings. In PROC MIXED 1243-1246 in 23rd SAS User Group Intl; SAS Institute: Cary, NC, 1998.
    • (1998) PROC MIXED 1243-1246 in 23rd SAS User Group Intl
    • Saxton, A.M.1
  • 32
    • 84875579006 scopus 로고    scopus 로고
    • In-depth study of the protein molecular structures of different types of dried distillers grains with solubles and their relationship to digestive characteristics
    • 10.1002/jsfa.5912
    • Liu, B.; Thacker, P.; Yu, P. In-depth study of the protein molecular structures of different types of dried distillers grains with solubles and their relationship to digestive characteristics J. Sci. Food Agric. 2012, 10.1002/jsfa.5912
    • (2012) J. Sci. Food Agric.
    • Liu, B.1    Thacker, P.2    Yu, P.3
  • 33
    • 77049116075 scopus 로고    scopus 로고
    • Detecting molecular changes in Vimy flaxseed protein structure using synchrotron FTIRM and DRIFT spectroscopic techniques: Structural and biochemical characterization
    • Doiron, K. J.; Yu, P.; Christensen, C. R.; Christensen, D. A.; McKinnon, J. J. Detecting molecular changes in Vimy flaxseed protein structure using synchrotron FTIRM and DRIFT spectroscopic techniques: Structural and biochemical characterization Spectroscopy 2009, 23, 307-322
    • (2009) Spectroscopy , vol.23 , pp. 307-322
    • Doiron, K.J.1    Yu, P.2    Christensen, C.R.3    Christensen, D.A.4    McKinnon, J.J.5
  • 34
    • 84872146329 scopus 로고    scopus 로고
    • Detect the sensitivity and response of protein molecular structure of whole canola seed (yellow and brown) to different heat processing methods and relation to protein utilization and availability using ATR-FT/IR molecular spectroscopy with chemometrics
    • Samadi, T.; Theodoridou, K.; Yu, P. Detect the sensitivity and response of protein molecular structure of whole canola seed (yellow and brown) to different heat processing methods and relation to protein utilization and availability using ATR-FT/IR molecular spectroscopy with chemometrics Spectrochim. Acta A 2013, 105, 304-313
    • (2013) Spectrochim. Acta A , vol.105 , pp. 304-313
    • Samadi, T.1    Theodoridou, K.2    Yu, P.3
  • 35
    • 84857988790 scopus 로고    scopus 로고
    • Response of lipid related molecular structure to wet and dry heating in canola tissue
    • Saman Abeysekara, S.; Yu, P. Response of lipid related molecular structure to wet and dry heating in canola tissue Spectrochim. Acta A 2012, 90, 63-71
    • (2012) Spectrochim. Acta A , vol.90 , pp. 63-71
    • Saman Abeysekara, S.1    Yu, P.2
  • 36
    • 9344233308 scopus 로고    scopus 로고
    • Using synchrotron-based FTIR microspectroscopy to reveal chemical features of feather protein secondary structure: Comparison with other feed protein sources
    • Yu, P.; McKinnon, J. J.; Christensen, C. R.; Christensen, D. A. Using synchrotron-based FTIR microspectroscopy to reveal chemical features of feather protein secondary structure: comparison with other feed protein sources J. Agric. Food Chem. 2004, 52, 7353-7361
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 7353-7361
    • Yu, P.1    McKinnon, J.J.2    Christensen, C.R.3    Christensen, D.A.4
  • 37
    • 68149139296 scopus 로고    scopus 로고
    • Heat-induced protein structure and subfractions in relation to protein degradation kinetics and intestinal availability in dairy cattle
    • Doiron, K.; Yu, P.; McKinnon, J. J.; Christensen, D. A. Heat-induced protein structure and subfractions in relation to protein degradation kinetics and intestinal availability in dairy cattle J. Dairy Sci. 2009, 92, 3319-3330
    • (2009) J. Dairy Sci. , vol.92 , pp. 3319-3330
    • Doiron, K.1    Yu, P.2    McKinnon, J.J.3    Christensen, D.A.4
  • 38
    • 77952596945 scopus 로고    scopus 로고
    • Using DRIFT molecular spectroscopy with uni- and multivariate spectral techniques to detect protein molecular structure differences among different genotypes of barley
    • Liu, B.; Yu, P. Using DRIFT molecular spectroscopy with uni- and multivariate spectral techniques to detect protein molecular structure differences among different genotypes of barley J. Agric. Food Chem. 2010, 58, 6264-6269
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 6264-6269
    • Liu, B.1    Yu, P.2
  • 39
    • 0034611366 scopus 로고    scopus 로고
    • Chemical characterization and in situ nutrient degradability of wet distillers' grains derived from barley-based ethanol production
    • DOI 10.1016/S0377-8401(99)00133-9, PII S0377840199001339
    • Mustafa, A. F.; McKinnon, J. J.; Christensen, D. A. Chemical characterization and in situ nutrient degradability of wet distillers' grains derived from barley-based ethanol production Anim. Feed. Sci. Technol. 2000, 83, 301-311 (Pubitemid 30152732)
    • (2000) Animal Feed Science and Technology , vol.83 , Issue.3-4 , pp. 301-311
    • Mustafa, A.F.1    McKinnon, J.J.2    Christensen, D.A.3
  • 40
    • 77955022194 scopus 로고    scopus 로고
    • Effects of bioethanol plant and coproduct type on the metabolic characteristics of the proteins in dairy cattle
    • Nuez-Ortin, W. G.; Yu, P. Effects of bioethanol plant and coproduct type on the metabolic characteristics of the proteins in dairy cattle J. Dairy Sci. 2010, 93, 3775-3783
    • (2010) J. Dairy Sci. , vol.93 , pp. 3775
    • Nuez-Ortin, W.G.1    Yu, P.2


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