메뉴 건너뛰기




Volumn , Issue , 2008, Pages 51-58

Biochemistry of Meat and Fat

Author keywords

Biochemistry of fat; Biochemistry of meat; Carboxypeptidase; Meat composition; Postmortem muscle metabolism

Indexed keywords


EID: 84889393298     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470376430.ch6     Document Type: Chapter
Times cited : (19)

References (53)
  • 1
    • 0034193858 scopus 로고    scopus 로고
    • Activities of phospholipase A and lysophospholipases in glycolytic and oxidative skeletal muscles in the rabbit
    • C Alasnier, G Gandemer. 2000. Activities of phospholipase A and lysophospholipases in glycolytic and oxidative skeletal muscles in the rabbit. J Sci Food Agric 80:698-704
    • (2000) J Sci Food Agric , vol.80 , pp. 698-704
    • Alasnier, C.1    Gandemer, G.2
  • 2
    • 0032219434 scopus 로고    scopus 로고
    • Concentration of free amino acids and dipeptides in porcine skeletal muscles with different oxidative patterns
    • MC Aristoy, F Toldrá. 1998. Concentration of free amino acids and dipeptides in porcine skeletal muscles with different oxidative patterns. Meat Sci 50:327-332
    • (1998) Meat Sci , vol.50 , pp. 327-332
    • Aristoy, M.C.1    Toldrá, F.2
  • 3
    • 0346639280 scopus 로고    scopus 로고
    • Histidine dipeptides HPLC-based test for the detection of mammalian origin proteins in feeds for ruminants
    • MC Aristoy, F Toldrá. 2004. Histidine dipeptides HPLC-based test for the detection of mammalian origin proteins in feeds for ruminants. Meat Sci 67:211-217
    • (2004) Meat Sci , vol.67 , pp. 211-217
    • Aristoy, M.C.1    Toldrá, F.2
  • 5
    • 0035076390 scopus 로고    scopus 로고
    • ATP metabolites during aging of exudative and nonexudative pork meats
    • N Batlle, MC Aristoy, F Toldrá. 2001. ATP metabolites during aging of exudative and nonexudative pork meats. J Food Sci 66:68-71
    • (2001) J Food Sci , vol.66 , pp. 68-71
    • Batlle, N.1    Aristoy, M.C.2    Toldrá, F.3
  • 8
    • 0034113376 scopus 로고    scopus 로고
    • Historical perspectives and current aspects of pork meat quality in the USA
    • RG Cassens. 2000. Historical perspectives and current aspects of pork meat quality in the USA. Food Chem 69:357-363
    • (2000) Food Chem , vol.69 , pp. 357-363
    • Cassens, R.G.1
  • 9
    • 0028185906 scopus 로고
    • Endogenous skeletal muscle antioxidants
    • KM Chan, EA Decker. 1994. Endogenous skeletal muscle antioxidants. Crit Rev Food Sci Nutri 34: 403-426
    • (1994) Crit Rev Food Sci Nutri , vol.34 , pp. 403-426
    • Chan, K.M.1    Decker, E.A.2
  • 10
    • 0030016595 scopus 로고
    • Structure and function of the 20S and 26S proteasomes
    • O Coux, K Tanaka, A Goldberg. 1995. Structure and function of the 20S and 26S proteasomes. Ann Rev Biochem 65:801-847
    • (1995) Ann Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.3
  • 11
    • 0035028998 scopus 로고    scopus 로고
    • Glutathione peroxidase activity, tissue and soluble selenium content in beef and pork in relation to meat aging and pig RN phenotype
    • C Daun, M Johansson, G Onning, B Akesson. 2001. Glutathione peroxidase activity, tissue and soluble selenium content in beef and pork in relation to meat aging and pig RN phenotype. Food Chem 73:313-319
    • (2001) Food Chem , vol.73 , pp. 313-319
    • Daun, C.1    Johansson, M.2    Onning, G.3    Akesson, B.4
  • 12
    • 0013086918 scopus 로고    scopus 로고
    • Le protéasome: une nouvelle protéase impliquée dans la maturation de la viande
    • D Dutaud, RG Taylor, B Picard, A Ouali. 1996. Le protéasome: une nouvelle protéase impliquée dans la maturation de la viande. Viandes Prod Carnés 17: 333-335
    • (1996) Viandes Prod Carnés , vol.17 , pp. 333-335
    • Dutaud, D.1    Taylor, R.G.2    Picard, B.3    Ouali, A.4
  • 13
    • 0001559155 scopus 로고
    • The contribution of proteolytic enzymes to postmortem changes in muscle
    • DJ Etherington. 1984. The contribution of proteolytic enzymes to postmortem changes in muscle. J An Sci 59:1644-1650
    • (1984) J An Sci , vol.59 , pp. 1644-1650
    • Etherington, D.J.1
  • 14
    • 0038164492 scopus 로고
    • Conditioning of meat factors influencing protease activity
    • A Romita, C Valin, AA Taylor, eds. London (UK): Elsevier Applied Sci
    • DJ Etherington. 1987. Conditioning of meat factors influencing protease activity. In: Accelerated Processing of Meat. A Romita, C Valin, AA Taylor, eds. London (UK): Elsevier Applied Sci, pp. 21-28
    • (1987) Accelerated Processing of Meat , pp. 21-28
    • Etherington, D.J.1
  • 15
    • 0019209405 scopus 로고
    • Characteristics of triacylglycerol and partial acylglycerol hydrolysis by human plasma lipoprotein lipase
    • CJ Fielding, PE Fielding. 1980. Characteristics of triacylglycerol and partial acylglycerol hydrolysis by human plasma lipoprotein lipase. Biochimica Biophysica Acta 620:440-446
    • (1980) Biochimica Biophysica Acta , vol.620 , pp. 440-446
    • Fielding, C.J.1    Fielding, P.E.2
  • 17
    • 0034340878 scopus 로고    scopus 로고
    • Effect of carnosine, anserine and other endogenous skeletal peptides on the activity of porcine muscle alanyl and arginyl aminopeptidases
    • MP Gianelli, M Flores, VJ Moya, MC Aristoy, F Toldrá. 2000. Effect of carnosine, anserine and other endogenous skeletal peptides on the activity of porcine muscle alanyl and arginyl aminopeptidases. J Food Biochem 24:69-78
    • (2000) J Food Biochem , vol.24 , pp. 69-78
    • Gianelli, M.P.1    Flores, M.2    Moya, V.J.3    Aristoy, M.C.4    Toldrá, F.5
  • 20
    • 0032219482 scopus 로고    scopus 로고
    • Lipid composition and lipolytic enzyme activities in porcine skeletal muscles with different oxidative pattern
    • P Hernández, JL Navarro, F Toldrá. 1998. Lipid composition and lipolytic enzyme activities in porcine skeletal muscles with different oxidative pattern. Meat Sci 49:1-10
    • (1998) Meat Sci , vol.49 , pp. 1-10
    • Hernández, P.1    Navarro, J.L.2    Toldrá, F.3
  • 21
    • 0022401715 scopus 로고
    • Positional specificity of lysosomal acide lipase purified from rabbit liver
    • T Imanaka, M Yamaguchi, S Ahkuma, S Takano. 1985. Positional specificity of lysosomal acide lipase purified from rabbit liver. J Biochem 98:927-931
    • (1985) J Biochem , vol.98 , pp. 927-931
    • Imanaka, T.1    Yamaguchi, M.2    Ahkuma, S.3    Takano, S.4
  • 22
    • 0026810591 scopus 로고
    • Fat characteristics of pigs fed fish oil containing eicosapentaenoic and docosahexanoic acids
    • M Irie, M Sakimoto. 1992. Fat characteristics of pigs fed fish oil containing eicosapentaenoic and docosahexanoic acids. J An Sci 70:470-477
    • (1992) J An Sci , vol.70 , pp. 470-477
    • Irie, M.1    Sakimoto, M.2
  • 24
    • 84889340978 scopus 로고    scopus 로고
    • Meat Science and Applications. YH Hui, WK Nip, RW Rogers, OA Young, eds. New York: Marcel Dekker Inc
    • RG Kauffman. 2001. Meat composition. In: Meat Science and Applications. YH Hui, WK Nip, RW Rogers, OA Young, eds. New York: Marcel Dekker Inc., pp. 1-19
    • (2001) Meat composition , pp. 1-19
    • Kauffman, R.G.1
  • 25
    • 0002514983 scopus 로고
    • Muscle proteinases and meat aging
    • M Koohmaraie. 1994. Muscle proteinases and meat aging. Meat Sci 36:93-104
    • (1994) Meat Sci , vol.36 , pp. 93-104
    • Koohmaraie, M.1
  • 26
    • 0000805516 scopus 로고
    • Effect of postmortem storage on Ca2_ dependent proteases, their inhibitor and myofibril fragmentation
    • M Koohmaraie, SC Seideman, JE Schollmeyer, TR Dutson, JD Grouse. 1987. Effect of postmortem storage on Ca2_ dependent proteases, their inhibitor and myofibril fragmentation. Meat Sci 19:187-196
    • (1987) Meat Sci , vol.19 , pp. 187-196
    • Koohmaraie, M.1    Seideman, S.C.2    Schollmeyer, J.E.3    Dutson, T.R.4    Grouse, J.D.5
  • 27
    • 33751155536 scopus 로고
    • Comparative study on the lipoxygenase activities of some soybean cultivars
    • JS Marczy, ML Simon, L Mozsik, B Szajani. 1995. Comparative study on the lipoxygenase activities of some soybean cultivars. J Agric Food Chem 43: 313-315
    • (1995) J Agric Food Chem , vol.43 , pp. 313-315
    • Marczy, J.S.1    Simon, M.L.2    Mozsik, L.3    Szajani, B.4
  • 28
    • 0019816949 scopus 로고
    • Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L
    • U Matsukura, A Okitani, T Nishimura, H Katoh. 1981. Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L. Biochim. Biophys Acta 662:41-47
    • (1981) Biochim. Biophys Acta , vol.662 , pp. 41-47
    • Matsukura, U.1    Okitani, A.2    Nishimura, T.3    Katoh, H.4
  • 29
    • 0004286047 scopus 로고
    • eds. A Glossary and Bibliography. Exopeptidases. London (UK): Academic Press
    • JK McDonald, AJ Barrett, eds. 1986. Mammalian Proteases. A Glossary and Bibliography. Vol 2. Exopeptidases. London (UK): Academic Press
    • (1986) Mammalian Proteases , vol.2
    • McDonald, J.K.1    Barrett, A.J.2
  • 30
    • 0025440289 scopus 로고
    • Determination of the alteration in fatty acid profiles, sensory characteristics and carcass traits of swine fed elevated levels of monounsaturated fats in the diet
    • MF Miller, SD Shackelford, KD Hayden, JO Reagan. 1990. Determination of the alteration in fatty acid profiles, sensory characteristics and carcass traits of swine fed elevated levels of monounsaturated fats in the diet. J An Sci 68:1624-1631
    • (1990) J An Sci , vol.68 , pp. 1624-1631
    • Miller, M.F.1    Shackelford, S.D.2    Hayden, K.D.3    Reagan, J.O.4
  • 31
    • 0030903775 scopus 로고    scopus 로고
    • The importance of meat enzymes in ripening and flavor generation in dry fermented sausages First results of a European project
    • K Molly, DI Demeyer, G Johansson, M Raemaekers, M Ghistelinck, I Geenen. 1997. The importance of meat enzymes in ripening and flavor generation in dry fermented sausages. First results of a European project. Food Chem 54:539-545
    • (1997) Food Chem , vol.54 , pp. 539-545
    • Molly, K.1    Demeyer, D.I.2    Johansson, G.3    Raemaekers, M.4    Ghistelinck, M.5    Geenen, I.6
  • 32
    • 84872887922 scopus 로고
    • Manipulation of the fatty acid composition of pig meat lipids by dietary means
    • CA Morgan, RC Noble, M Cocchi, R McCartney. 1992. Manipulation of the fatty acid composition of pig meat lipids by dietary means. J Sci Food and Agric 58:357-368
    • (1992) J Sci Food and Agric , vol.58 , pp. 357-368
    • Morgan, C.A.1    Noble, R.C.2    Cocchi, M.3    McCartney, R.4
  • 34
    • 0019555638 scopus 로고
    • Characterization of hydrolase H, a new muscle protease possessing aminoendopeptidase activity
    • A Okitani, T Nishimura, H Kato. 1981. Characterization of hydrolase H, a new muscle protease possessing aminoendopeptidase activity. Eur J Biochem 115:269-274
    • (1981) Eur J Biochem , vol.115 , pp. 269-274
    • Okitani, A.1    Nishimura, T.2    Kato, H.3
  • 35
    • 0002635128 scopus 로고
    • Sensory quality of meat as affected by muscle biochemistry and modern technologies
    • LO Fiems, BG Cottyn, DI Demeyer, eds. Amsterdam, The Netherlands: Elsevier Science Pub, BV
    • A Ouali. 1991. Sensory quality of meat as affected by muscle biochemistry and modern technologies. In: Animal Biotechnology and the Quality of Meat Production. LO Fiems, BG Cottyn, DI Demeyer, eds. Amsterdam, The Netherlands: Elsevier Science Pub, BV, pp. 85-105
    • (1991) Animal Biotechnology and the Quality of Meat Production , pp. 85-105
    • Ouali, A.1
  • 36
    • 84889471784 scopus 로고    scopus 로고
    • Overview of muscle peptidases and their potential role in meat texture development
    • F Toldrá, ed. Trivandrum, India: Research Signpost
    • A Ouali, MA Sentandreu. 2002. Overview of muscle peptidases and their potential role in meat texture development. In: Research Advances in the Quality of Meat and Meat Products. F Toldrá, ed. Trivandrum, India: Research Signpost, pp. 33-63
    • (2002) Research Advances in the Quality of Meat and Meat Products , pp. 33-63
    • Ouali, A.1    Sentandreu, M.A.2
  • 38
    • 0036986447 scopus 로고    scopus 로고
    • Role of muscle endopeptidases and their inhibitors in meat tenderness
    • MA Sentandreu, G Coulis, A Ouali. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci Technol 13:398-419
    • (2002) Trends Food Sci Technol , vol.13 , pp. 398-419
    • Sentandreu, M.A.1    Coulis, G.2    Ouali, A.3
  • 39
    • 0002663740 scopus 로고    scopus 로고
    • Dipeptidylpeptidase activities along the processing of Serrano dry-cured ham
    • MA Sentandreu, F Toldrá. 2002. Dipeptidylpeptidase activities along the processing of Serrano dry-cured ham. European Food Res Technol 213:83-87
    • (2002) European Food Res Technol , vol.213 , pp. 83-87
    • Sentandreu, M.A.1    Toldrá, F.2
  • 40
    • 0002752607 scopus 로고
    • Lipases. B. Borgström, HL Brockman, eds. Amsterdam, The Netherlands: Elsevier
    • LC Smith, HJ Pownall. 1984. Lipoprotein lipase. In: Lipases. B. Borgström, HL Brockman, eds. Amsterdam, The Netherlands: Elsevier, pp. 263-305
    • (1984) Lipoprotein lipase , pp. 263-305
    • Smith, L.C.1    Pownall, H.J.2
  • 41
    • 0002695830 scopus 로고
    • The enzymology of dry-curing of meat products
    • FJM Smulders, F Toldrá J Flores, M Prieto. Nijmegen, The Netherlands: Audet
    • F Toldrá. 1992. The enzymology of dry-curing of meat products. In: New Technologies for Meat and Meat Products. FJM Smulders, F Toldrá J Flores, M Prieto. Nijmegen, The Netherlands: Audet, pp. 209-231
    • (1992) New Technologies for Meat and Meat Products , pp. 209-231
    • Toldrá, F.1
  • 42
    • 0346706011 scopus 로고    scopus 로고
    • Proteolysis and lipolysis in flavour development of dry-cured meat products
    • F Toldrá 1998. Proteolysis and lipolysis in flavour development of dry-cured meat products. Meat Sci 49:s101-s110
    • (1998) Meat Sci , vol.49
    • Toldrá, F.1
  • 43
    • 0013385789 scopus 로고    scopus 로고
    • Trumbull, Connecticut: Food & Nutrition Press
    • F Toldrá. 2002. Dry-cured Meat Products. Trumbull, Connecticut: Food & Nutrition Press, pp. 1-238
    • (2002) Dry-cured Meat Products , pp. 1-238
    • Toldrá, F.1
  • 44
    • 70049087232 scopus 로고    scopus 로고
    • Meat: Chemistry and biochemistry
    • YH Hui, JD Culbertson, S Duncan, I Guerrero-Legarreta, ECY Li-Chan, CY Ma, CH Manley, TA McMeekin, WK Nip, LML Nollet, MS Rahman, F Toldrá, YL Xiong, eds Boca Raton, Florida: CRC Press, 28-1-28-18
    • F Toldrá. 2006a. Meat: Chemistry and biochemistry. In: Handbook of Food Science, Technology and Engineering. YH Hui, JD Culbertson, S Duncan, I Guerrero-Legarreta, ECY Li-Chan, CY Ma, CH Manley, TA McMeekin, WK Nip, LML Nollet, MS Rahman, F Toldrá, YL Xiong, eds. Volume 1. Boca Raton, Florida: CRC Press, pp. 28-1-28-18
    • (2006) Handbook of Food Science, Technology and Engineering , vol.1
    • Toldrá, F.1
  • 45
    • 84889621719 scopus 로고    scopus 로고
    • Biochemistry of processing meat and poultry
    • YH Hui, WK Nip, ML Nollet, G Paliyath & BK Simpson, eds. Ames, Iowa: Blackwell Publishing
    • F Toldrá. 2006b. Biochemistry of processing meat and poultry. In: Food Biochemistry and Food Processing. YH Hui, WK Nip, ML Nollet, G Paliyath & BK Simpson, eds. Ames, Iowa: Blackwell Publishing, pp. 315-335
    • (2006) Food Biochemistry and Food Processing , pp. 315-335
    • Toldrá, F.1
  • 46
    • 84890144846 scopus 로고    scopus 로고
    • Biochemical proteolysis basis for improved processing of dry-cured meats
    • LML Nollet, F Toldrá, eds. Boca Raton, Florida: CRC Press
    • F Toldrá. 2006c. Biochemical proteolysis basis for improved processing of dry-cured meats. In: Advanced Technologies for Meat Processing. LML Nollet, F Toldrá, eds. Boca Raton, Florida: CRC Press, pp. 329-351
    • (2006) Advanced Technologies for Meat Processing , pp. 329-351
    • Toldrá, F.1
  • 47
    • 0032064706 scopus 로고    scopus 로고
    • The role of muscle proteases and lipases in flavor development during the processing of dry-cured ham
    • F Toldrá, M Flores. 1998. The role of muscle proteases and lipases in flavor development during the processing of dry-cured ham. Crit Rev Food Sci Nutrit 38: 331-352
    • (1998) Crit Rev Food Sci Nutrit , vol.38 , pp. 331-352
    • Toldrá, F.1    Flores, M.2
  • 48
    • 0026579299 scopus 로고
    • Activities of pork muscle proteases in cured meats
    • F Toldrá, E Rico, J Flores. 1992. Activities of pork muscle proteases in cured meats. Biochimie 74:291-296
    • (1992) Biochimie , vol.74 , pp. 291-296
    • Toldrá, F.1    Rico, E.2    Flores, J.3
  • 49
    • 0018135686 scopus 로고
    • Enzymes catalyzing the hydrolysis of long-chain monoacylglycerols in rat adipose tissue
    • H Tornquist, P Nilsson-Ehle, P Belfrage. 1978. Enzymes catalyzing the hydrolysis of long-chain monoacylglycerols in rat adipose tissue. Biochimica Biophysica Acta 530:474-486
    • (1978) Biochimica Biophysica Acta , vol.530 , pp. 474-486
    • Tornquist, H.1    Nilsson-Ehle, P.2    Belfrage, P.3
  • 50
    • 84889346964 scopus 로고    scopus 로고
    • Muscle protein changes post mortem in relation to pork quality traits
    • RD Warner, RG Kauffman, RL Russell. 1997. Muscle protein changes post mortem in relation to pork quality traits. Meat Sci 33:359-372
    • (1997) Meat Sci , vol.33 , pp. 359-372
    • Warner, R.D.1    Kauffman, R.G.2    Russell, R.L.3
  • 51
    • 0026480564 scopus 로고
    • Mammalian lipoxygenases: molecular structures and functions
    • S Yamamoto. 1992. Mammalian lipoxygenases: molecular structures and functions. Biochimica Biophysica Acta 1128:117-131
    • (1992) Biochimica Biophysica Acta , vol.1128 , pp. 117-131
    • Yamamoto, S.1
  • 52
    • 0242331100 scopus 로고    scopus 로고
    • Significance of preslaughter stress and different tissue PUFA levels on the oxidative status and stability of porcine muscle and meat
    • JF Young, K Rosenvold, J Stagsted, CL Steffensen, JH Nielsen, HJ Andersen. 2003. Significance of preslaughter stress and different tissue PUFA levels on the oxidative status and stability of porcine muscle and meat. J Agric Food Chem 51:6877-6881
    • (2003) J Agric Food Chem , vol.51 , pp. 6877-6881
    • Young, J.F.1    Rosenvold, K.2    Stagsted, J.3    Steffensen, C.L.4    Nielsen, J.H.5    Andersen, H.J.6
  • 53
    • 84986519237 scopus 로고
    • Cathepsin D and its effects on myofibrillar proteins: a review
    • MG Zeece, K Katoh. 1989. Cathepsin D and its effects on myofibrillar proteins: a review. J Food Biochem 13:157-161
    • (1989) J Food Biochem , vol.13 , pp. 157-161
    • Zeece, M.G.1    Katoh, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.