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Volumn 46, Issue 1, 2011, Pages 335-343

Comparative study on the effect of acid- and alkaline-aided extractions on mechanically separated turkey meat (MSTM): Chemical characteristics of recovered proteins

Author keywords

Acid and alkaline extractions; Mechanically separated turkey meat; Protein

Indexed keywords

ALKALINE EXTRACTION; ALKALINE TREATMENT; AMINO ACID ANALYSIS; CHEMICAL CHARACTERISTIC; COMPARATIVE STUDIES; EXTRACTABILITY; GLUTAMIC ACID; MYOFIBRILLAR PROTEINS; MYOSIN HEAVY CHAIN; PH VALUE; PHYSICOCHEMICAL PROPERTY; POLAR LIPIDS; PROTEIN ISOLATES; PROTEIN YIELD; PROTEOGLYCANS; SDS-PAGE ANALYSIS; SEDIMENT FRACTION; STATISTICAL DIFFERENCES; TOTAL PROTEIN; TURKEY MEAT; URONIC ACIDS; VARIOUS PH;

EID: 78650252283     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.09.006     Document Type: Article
Times cited : (58)

References (52)
  • 1
    • 78650245612 scopus 로고    scopus 로고
    • Farm animal statistics: Meat consumption
    • USDA/ERS (accessedJan.2010)
    • USDA/ERS. Farm animal statistics: meat consumption. Factory farming. http://www.hsus.org/farm/resources/pubs/stats-meat-consumption.html (accessed Jan. 2010); 2007.
    • (2007) Factory Farming
  • 2
    • 61849087086 scopus 로고    scopus 로고
    • CFC (Chicken Farmers of Canada) (accessedJan.2010)
    • CFC (Chicken Farmers of Canada). Annual report 2008. Chicken Farmers of Canada. http://www.chicken.ca/app/wa/mediaEntrymediaEntryId=5230 (accessed Jan. 2010); 2008.
    • (2008) Annual Report 2008. Chicken Farmers of Canada
  • 3
    • 0041142944 scopus 로고
    • Changes in myofibrillar protein and collagen content of mechanically deboned chicken meat due to washing and screening
    • T.S. Yang, and G.W. Froning Changes in myofibrillar protein and collagen content of mechanically deboned chicken meat due to washing and screening Poult Sci 71 7 1992 1221 1227
    • (1992) Poult Sci , vol.71 , Issue.7 , pp. 1221-1227
    • Yang, T.S.1    Froning, G.W.2
  • 5
    • 0002454157 scopus 로고    scopus 로고
    • Surimi processing from dark muscle fish
    • H.O. Hultin, and S.D. Kelleher Surimi processing from dark muscle fish J.W. Park, Surimi and surimi seafood 2000 Marcel Dekker Inc. New York 59 77
    • (2000) Surimi and Surimi Seafood , pp. 59-77
    • Hultin, H.O.1    Kelleher, S.D.2
  • 7
    • 70349917891 scopus 로고    scopus 로고
    • Capacity of reductants and chelators to prevent lipid oxidation catalyzed by fish haemoglobin
    • R. Maestre, M. Pazos, J. Iglesias, and I. Medina Capacity of reductants and chelators to prevent lipid oxidation catalyzed by fish haemoglobin J Agric Food Chem 57 19 2009 9190 9196
    • (2009) J Agric Food Chem , vol.57 , Issue.19 , pp. 9190-9196
    • Maestre, R.1    Pazos, M.2    Iglesias, J.3    Medina, I.4
  • 8
    • 33646384252 scopus 로고    scopus 로고
    • Functional fish protein ingredients from fish species of warm and temperate waters: Comparison of acid- and alkali-aided processing vs. conventional surimi processing
    • H.G. Kristinsson, and N. Demir Functional fish protein ingredients from fish species of warm and temperate waters: comparison of acid- and alkali-aided processing vs. conventional surimi processing P.J. Bechtel, Advances in seafood byproducts 2003 Univ. of Alaska Press Fairbanks, AK 277 298
    • (2003) Advances in Seafood Byproducts , pp. 277-298
    • Kristinsson, H.G.1    Demir, N.2
  • 9
    • 19444381148 scopus 로고    scopus 로고
    • A comparative study between acid- and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle
    • H.G. Kristinsson, A.E. Theodore, N. Demir, and B. Ingadottir A comparative study between acid- and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle J Food Sci 70 4 2005 298 306
    • (2005) J Food Sci , vol.70 , Issue.4 , pp. 298-306
    • Kristinsson, H.G.1    Theodore, A.E.2    Demir, N.3    Ingadottir, B.4
  • 10
    • 65149095227 scopus 로고    scopus 로고
    • The acid and alkaline solubilization process for the isolation of muscle proteins: State of the art
    • H. Nolsoe, and I. Undeland The acid and alkaline solubilization process for the isolation of muscle proteins: state of the art Food Bioproc Technol 2 2009 1 27
    • (2009) Food Bioproc Technol , vol.2 , pp. 1-27
    • Nolsoe, H.1    Undeland, I.2
  • 11
    • 73549124985 scopus 로고    scopus 로고
    • The clinical effectiveness of glucosamine and chondroitin supplements in slowing or arresting progression of osteoarthritis of the knee: A systematic review and economic evaluation
    • C. Black, C. Clar, R. Henderson, C. MacEachern, P. McNamee, and Z. Quayyum The clinical effectiveness of glucosamine and chondroitin supplements in slowing or arresting progression of osteoarthritis of the knee: a systematic review and economic evaluation Health Technol Assess 13 52 2009 1 148
    • (2009) Health Technol Assess , vol.13 , Issue.52 , pp. 1-148
    • Black, C.1    Clar, C.2    Henderson, R.3    MacEachern, C.4    McNamee, P.5    Quayyum, Z.6
  • 12
    • 0028906513 scopus 로고
    • The effect of osteoarthritis on disability and health care in Canada
    • E.M. Badley The effect of osteoarthritis on disability and health care in Canada J Rheumatol Suppl. 43 1995 19 22
    • (1995) J Rheumatol , vol.43 , pp. 19-22
    • Badley, E.M.1
  • 13
    • 0347694884 scopus 로고    scopus 로고
    • New approaches for the effective recovery of fish proteins and their physicochemical characteristics
    • Y.S. Kim, J.W. Park, and Y.J. Choi New approaches for the effective recovery of fish proteins and their physicochemical characteristics Fish Sci 69 6 2003 1231 1239
    • (2003) Fish Sci , vol.69 , Issue.6 , pp. 1231-1239
    • Kim, Y.S.1    Park, J.W.2    Choi, Y.J.3
  • 14
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of biuret reaction
    • A.C. Gornall, C.J. Bradwill, and M.M. David Determination of serum proteins by means of biuret reaction J Biol Chem 177 2 1949 755 766
    • (1949) J Biol Chem , vol.177 , Issue.2 , pp. 755-766
    • Gornall, A.C.1    Bradwill, C.J.2    David, M.M.3
  • 15
    • 0142063536 scopus 로고    scopus 로고
    • Functional protein isolates from mechanically deboned turkey by alkaline solubilization with isoelectric precipitation
    • Y. Liang, and H.O. Hultin Functional protein isolates from mechanically deboned turkey by alkaline solubilization with isoelectric precipitation J Muscle Food 14 3 2003 195 205
    • (2003) J Muscle Food , vol.14 , Issue.3 , pp. 195-205
    • Liang, Y.1    Hultin, H.O.2
  • 16
    • 25444446815 scopus 로고    scopus 로고
    • The influence of extraction and precipitation pH on the dry matter yield of broiler dark meat
    • M. Betti, and D.L. Fletcher The influence of extraction and precipitation pH on the dry matter yield of broiler dark meat Poult Sci 84 8 2005 1303 1307
    • (2005) Poult Sci , vol.84 , Issue.8 , pp. 1303-1307
    • Betti, M.1    Fletcher, D.L.2
  • 17
    • 84981865736 scopus 로고
    • Evaluation of the Biuret and dye-binding methods for protein determination in meats
    • J. Torten, and J.R. Whitaker Evaluation of the Biuret and dye-binding methods for protein determination in meats J Food Sci 29 2 1964 168 174
    • (1964) J Food Sci , vol.29 , Issue.2 , pp. 168-174
    • Torten, J.1    Whitaker, J.R.2
  • 18
    • 74549114157 scopus 로고    scopus 로고
    • Alkali aided protein extraction from chicken dark meat: Chemical and functional properties of recovered proteins
    • D. Omana, Y. Xu, V. Moayedi, and M. Betti Alkali aided protein extraction from chicken dark meat: chemical and functional properties of recovered proteins Process Biochem 45 3 2010 375 381
    • (2010) Process Biochem , vol.45 , Issue.3 , pp. 375-381
    • Omana, D.1    Xu, Y.2    Moayedi, V.3    Betti, M.4
  • 19
    • 0036812288 scopus 로고    scopus 로고
    • Acid-aided protein recovery from enzyme-rich Pacific whiting
    • Y.J. Choi, and J.W. Park Acid-aided protein recovery from enzyme-rich Pacific whiting J Food Sci 67 8 2002 2962 2967
    • (2002) J Food Sci , vol.67 , Issue.8 , pp. 2962-2967
    • Choi, Y.J.1    Park, J.W.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural protein during the assembly of the head of bacteriophage T4 Nature 277 1970 680 685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • J. Folch, M. Lees, and G.H.S. Stanley A simple method for the isolation and purification of total lipids from animal tissues J Biol Chem 226 1 1957 467 509
    • (1957) J Biol Chem , vol.226 , Issue.1 , pp. 467-509
    • Folch, J.1    Lees, M.2    Stanley, G.H.S.3
  • 22
    • 0345328242 scopus 로고    scopus 로고
    • Determination of the lipid classes and fatty acid profile of Niger (Guizotia abyssinica Cass.) seed oil
    • M.F. Ramadan, and J.T. Morsel Determination of the lipid classes and fatty acid profile of Niger (Guizotia abyssinica Cass.) seed oil Phytochem Anal 14 6 2003 366 370
    • (2003) Phytochem Anal , vol.14 , Issue.6 , pp. 366-370
    • Ramadan, M.F.1    Morsel, J.T.2
  • 23
    • 0018973750 scopus 로고
    • Relative susceptibility of microsomes from lung, heart, liver, kidney, brain and testes to lipid peroxidation: Correction with vitamin e content
    • D.J. Kornburst, and R.D. Mavis Relative susceptibility of microsomes from lung, heart, liver, kidney, brain and testes to lipid peroxidation: correction with vitamin E content Lipids 15 1980 315 322
    • (1980) Lipids , vol.15 , pp. 315-322
    • Kornburst, D.J.1    Mavis, R.D.2
  • 24
    • 0014154751 scopus 로고
    • Determination of hydroxyproline
    • H. Stegemann, and K. Stalder Determination of hydroxyproline Clin Chim Acta 18 1967 267 273
    • (1967) Clin Chim Acta , vol.18 , pp. 267-273
    • Stegemann, H.1    Stalder, K.2
  • 25
    • 50549161624 scopus 로고
    • A modified uronic acid carbazole reaction
    • T. Bitter, and H.M. Muir A modified uronic acid carbazole reaction Anal Biochem 4 1962 330 334
    • (1962) Anal Biochem , vol.4 , pp. 330-334
    • Bitter, T.1    Muir, H.M.2
  • 26
    • 0018394892 scopus 로고
    • A partial modification of the carbazole method of Bitter and Muir for quantitation of hexuronic acids
    • M. Kosakai, and Z. Yosizawa A partial modification of the carbazole method of Bitter and Muir for quantitation of hexuronic acids Anal Biochem 93 1979 295 298
    • (1979) Anal Biochem , vol.93 , pp. 295-298
    • Kosakai, M.1    Yosizawa, Z.2
  • 27
    • 42149110472 scopus 로고    scopus 로고
    • SAS user's guide Version 9.0, SAS Institute. Inc., Cary, NC. USA
    • SAS user's guide. Statistics, Version 9.0, SAS Institute. Inc., Cary, NC. USA; 2006.
    • (2006) Statistics
  • 28
    • 77955655072 scopus 로고    scopus 로고
    • Structure-function relationship of muscle proteins
    • Y.L. Xiong Structure-function relationship of muscle proteins S. Damodaran, A. Paraf, Food proteins and their applications 1997 Marcel Dekker Inc. New York 341 342
    • (1997) Food Proteins and Their Applications , pp. 341-342
    • Xiong, Y.L.1
  • 29
    • 0021663774 scopus 로고
    • Milk proteins: Physicochemical and functional properties
    • J.E. Kinsella Milk proteins: physicochemical and functional properties CRC Crit Rev Food Sci Nutr 21 1984 197 262
    • (1984) CRC Crit Rev Food Sci Nutr , vol.21 , pp. 197-262
    • Kinsella, J.E.1
  • 30
    • 0011916364 scopus 로고
    • The influence of pH on the protein net charge in the myofibrillar system
    • R. Hamm The influence of pH on the protein net charge in the myofibrillar system Rec Meat Conf Proc 47 1994 5 9
    • (1994) Rec Meat Conf Proc , vol.47 , pp. 5-9
    • Hamm, R.1
  • 31
    • 0037021586 scopus 로고    scopus 로고
    • Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process
    • I. Undeland, S.D. Kelleher, and H.O. Hultin Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process J Agric Food Chem 50 2002 7371 7379
    • (2002) J Agric Food Chem , vol.50 , pp. 7371-7379
    • Undeland, I.1    Kelleher, S.D.2    Hultin, H.O.3
  • 33
    • 2542461592 scopus 로고    scopus 로고
    • Changes in trout hemoglobin conformations and solubility after exposure to acid and alkali pH
    • H.G. Kristinsson, and H.O. Hultin Changes in trout hemoglobin conformations and solubility after exposure to acid and alkali pH J Agric Food Chem 52 11 2004 3633 3643
    • (2004) J Agric Food Chem , vol.52 , Issue.11 , pp. 3633-3643
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 35
    • 33746753269 scopus 로고    scopus 로고
    • Functional properties of Rohu (Labeo rohita) proteins during iced storage
    • M. Mohan, D. Ramachandran, and T.V. Sankar Functional properties of Rohu (Labeo rohita) proteins during iced storage Food Res Int 39 8 2006 847 854
    • (2006) Food Res Int , vol.39 , Issue.8 , pp. 847-854
    • Mohan, M.1    Ramachandran, D.2    Sankar, T.V.3
  • 36
    • 0002207547 scopus 로고
    • Relationships between structure and functional properties of food proteins
    • J.E. Kinsella Relationships between structure and functional properties of food proteins P.F. Fox, J.J. Condon, Food proteins 1982 Applied Science Publishers London 51 103
    • (1982) Food Proteins , pp. 51-103
    • Kinsella, J.E.1
  • 37
    • 0031901189 scopus 로고    scopus 로고
    • Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH
    • T.M. Lin, and J.W. Park Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH J Food Sci 63 2 1998 215 218
    • (1998) J Food Sci , vol.63 , Issue.2 , pp. 215-218
    • Lin, T.M.1    Park, J.W.2
  • 38
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins
    • F.J. Monahan, J.B. German, and J.E. Kinsella Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins J Agric Food Chem 43 1 1995 46 52
    • (1995) J Agric Food Chem , vol.43 , Issue.1 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 39
    • 67650433165 scopus 로고    scopus 로고
    • Functional and biochemical characterization of proteins remaining in solution after isoelectric precipitation
    • C. Pires, I. Batista, V. Godinho, and M.L. Nunes Functional and biochemical characterization of proteins remaining in solution after isoelectric precipitation J Aquat Food Prod Technol 17 1 2008 60 72
    • (2008) J Aquat Food Prod Technol , vol.17 , Issue.1 , pp. 60-72
    • Pires, C.1    Batista, I.2    Godinho, V.3    Nunes, M.L.4
  • 40
    • 77957156941 scopus 로고    scopus 로고
    • Effect of acid- and alkaline-aided extractions on functional and rheological properties of proteins recovered from mechanically separated turkey meat (MSTM)
    • Y. Hrynets, D.A. Omana, Y. Xu, and M. Betti Effect of acid- and alkaline-aided extractions on functional and rheological properties of proteins recovered from mechanically separated turkey meat (MSTM) J Food Sci 75 7 2010 E477 E486
    • (2010) J Food Sci , vol.75 , Issue.7
    • Hrynets, Y.1    Omana, D.A.2    Xu, Y.3    Betti, M.4
  • 41
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • E.R. Stadtman Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions Annu Rev Biochem 62 1993 797 821
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 42
    • 50649095897 scopus 로고    scopus 로고
    • Determination of sulphur amino acids in foods as related to biovalidity
    • S.M. Rutherfurd, and P.J. Moughan Determination of sulphur amino acids in foods as related to biovalidity J AOAC Int 91 4 2008 907 913
    • (2008) J AOAC Int , vol.91 , Issue.4 , pp. 907-913
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 43
    • 0037077378 scopus 로고    scopus 로고
    • Isolation, purification, and biochemical characterization of a novel water soluble protein from Inca Peanut (Plukenetia volubilis L.)
    • S.K. Sathe, B.R. Hamaker, K.W.C. Sze-Tao, and M. Venkatachalam Isolation, purification, and biochemical characterization of a novel water soluble protein from Inca Peanut (Plukenetia volubilis L.) J Agric Food Chem 50 17 2002 4906 4908
    • (2002) J Agric Food Chem , vol.50 , Issue.17 , pp. 4906-4908
    • Sathe, S.K.1    Hamaker, B.R.2    Sze-Tao, K.W.C.3    Venkatachalam, M.4
  • 46
    • 0024447382 scopus 로고
    • Histidine and proline are important sites of free radical damage to proteins
    • R.T. Dean, S.P. Wolff, and M.A. McElligott Histidine and proline are important sites of free radical damage to proteins Free Rad Res Commun 7 2 1989 97 103
    • (1989) Free Rad Res Commun , vol.7 , Issue.2 , pp. 97-103
    • Dean, R.T.1    Wolff, S.P.2    McElligott, M.A.3
  • 47
    • 0028363342 scopus 로고
    • Activation of hydrogen peroxide copper (II) complexes with some histidine-containing peptides and their SOD-like activities
    • J.I. Ueda, T. Ozawa, M. Miyazaki, and Y. Fujiwara Activation of hydrogen peroxide copper (II) complexes with some histidine-containing peptides and their SOD-like activities J Inorg Biochem 55 2 1994 123 130
    • (1994) J Inorg Biochem , vol.55 , Issue.2 , pp. 123-130
    • Ueda, J.I.1    Ozawa, T.2    Miyazaki, M.3    Fujiwara, Y.4
  • 48
    • 0030273308 scopus 로고    scopus 로고
    • Alkali-assisted extraction of proteins from meat and bone residue of harp seal (Phoca groenlandica)
    • F. Shahidi, and J. Synowiecki Alkali-assisted extraction of proteins from meat and bone residue of harp seal (Phoca groenlandica) Food Chem 57 2 1996 317 321
    • (1996) Food Chem , vol.57 , Issue.2 , pp. 317-321
    • Shahidi, F.1    Synowiecki, J.2
  • 50
    • 47949083218 scopus 로고    scopus 로고
    • Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process
    • S. Rawdkuen, S. Sai-Ut, S. Khamsorn, M. Chaijan, and S. Benjakul Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process Food Chem 112 1 2009 112 119
    • (2009) Food Chem , vol.112 , Issue.1 , pp. 112-119
    • Rawdkuen, S.1    Sai-Ut, S.2    Khamsorn, S.3    Chaijan, M.4    Benjakul, S.5
  • 51
    • 1942518232 scopus 로고    scopus 로고
    • Chemical composition of the infrapatellar fat pad of swine
    • T. Nakano, Y.W. Wang, L. Ozimek, and J.S. Sim Chemical composition of the infrapatellar fat pad of swine J Anat 204 4 2004 301 306
    • (2004) J Anat , vol.204 , Issue.4 , pp. 301-306
    • Nakano, T.1    Wang, Y.W.2    Ozimek, L.3    Sim, J.S.4
  • 52
    • 84956899820 scopus 로고
    • Studies on the formation of collagen: I. Properties and fractionation of neutral salt extracts of normal guinea pig connective tissue
    • J. Gross Studies on the formation of collagen: I. Properties and fractionation of neutral salt extracts of normal guinea pig connective tissue J Exp Med 107 2 1958 247 263
    • (1958) J Exp Med , vol.107 , Issue.2 , pp. 247-263
    • Gross, J.1


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