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Volumn 54, Issue 8, 2014, Pages 1012-1031

Exogenous Proteases for Meat Tenderization

Author keywords

Meat; microbial; plant; proteases; tenderization

Indexed keywords

ENZYMES;

EID: 84893574486     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408398.2011.623247     Document Type: Article
Times cited : (181)

References (188)
  • 1
    • 0026215090 scopus 로고
    • Some properties of a cysteine proteinase inhibitor from corn endosperm
    • Abe, M. and Arai, S. 1991. Some properties of a cysteine proteinase inhibitor from corn endosperm. Agric. Biol. Chem., 55: 2417-2418.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2417-2418
    • Abe, M.1    Arai, S.2
  • 2
    • 23144431945 scopus 로고    scopus 로고
    • Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11
    • Adinarayana, K., Ellaiah, P. and Prasad, D. S. 2003. Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11. AAPS Pharm. Sci. Tech, 4 (4): 440-448.
    • (2003) AAPS Pharm. Sci. Tech , vol.4 , Issue.4 , pp. 440-448
    • Adinarayana, K.1    Ellaiah, P.2    Prasad, D.S.3
  • 3
    • 17644374563 scopus 로고    scopus 로고
    • Stabilization and partial purification of a protease from ginger rhizome (Zingiber offinale Roscoe)
    • Adulyatham, P. and Owusu-Apenten, R. 2005. Stabilization and partial purification of a protease from ginger rhizome (Zingiber offinale Roscoe). J. Food Sci., 70: C231-C234.
    • (2005) J. Food Sci. , vol.70
    • Adulyatham, P.1    Owusu-Apenten, R.2
  • 4
    • 34548572301 scopus 로고    scopus 로고
    • Effects of various treatments on the texture softening of post-breeding mature cows meat
    • Proceedings of the 52nd International Conference of Meat Science and Technology, pp
    • Ahmed, A. M., Matsumoto, N., Kawahara, S., Ohta, K., Kuroda, R., Okayama, T., Nakade, K., Numata, M., Nakamura, T. and Muguruma, M. 2006. Effects of various treatments on the texture softening of post-breeding mature cows meat.: 431-432. Proceedings of the 52nd International Conference of Meat Science and Technology, pp
    • (2006) , pp. 431-432
    • Ahmed, A.M.1    Matsumoto, N.2    Kawahara, S.3    Ohta, K.4    Kuroda, R.5    Okayama, T.6    Nakade, K.7    Numata, M.8    Nakamura, T.9    Muguruma, M.10
  • 5
    • 0020541585 scopus 로고
    • Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum
    • Anastasi, A., Brown, M. A., Kembhavi, A. A., Nicklin, M. J. H., Sayers, C. A., Sunter, D. C. and Barrett, A. J. 1983. Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. J. Biochem., 211: 129-138.
    • (1983) J. Biochem. , vol.211 , pp. 129-138
    • Anastasi, A.1    Brown, M.A.2    Kembhavi, A.A.3    Nicklin, M.J.H.4    Sayers, C.A.5    Sunter, D.C.6    Barrett, A.J.7
  • 6
    • 84892337543 scopus 로고    scopus 로고
    • Meat tenderization with a thermolabile protease
    • US Patent 6,849,284 B2
    • Ashie, I., Sorensen, T. and Nielsen, P. M. Meat tenderization with a thermolabile protease. 2005. US Patent 6,849,284 B2
    • Ashie, I.1    Sorensen, T.2    Nielsen, P.M.3
  • 7
    • 0036689388 scopus 로고    scopus 로고
    • Effects of papain and a microbial enzyme on meat proteins and beef tenderness
    • Ashie, I. N. A., Sorensen, T. L. and Nielsen, P. M. 2002. Effects of papain and a microbial enzyme on meat proteins and beef tenderness. J. Food Sci., 67: 2138-2142.
    • (2002) J. Food Sci. , vol.67 , pp. 2138-2142
    • Ashie, I.N.A.1    Sorensen, T.L.2    Nielsen, P.M.3
  • 8
    • 0030028342 scopus 로고    scopus 로고
    • Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B
    • Auerswald, E. A., Nägler, D. K., Gross, S., Assfalg-Machleidt, I., Stubbs, M. T., Eckerskorn, C., Machleidt, W. and Fritz, H. 1996. Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B. Eur. J. Biochem., 235: 534-42.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 534-542
    • Auerswald, E.A.1    Nägler, D.K.2    Gross, S.3    Assfalg-Machleidt, I.4    Stubbs, M.T.5    Eckerskorn, C.6    Machleidt, W.7    Fritz, H.8
  • 9
    • 52449146575 scopus 로고
    • Study of a papain activation factor present in the dialysable fraction of soyabean extract
    • Bahadur, K. and Saxena, I. 1964. Study of a papain activation factor present in the dialysable fraction of soyabean extract. Biol. Plantarum (Praiia)., 6: 165-170.
    • (1964) Biol. Plantarum (Praiia). , vol.6 , pp. 165-170
    • Bahadur, K.1    Saxena, I.2
  • 10
    • 0010091380 scopus 로고
    • Indigenous and exogenous enzymes in meat
    • In: Fox P. F., editors London, UK, London,: Elsevier Applied Science
    • Bailey, M. E. and Murdock, F. A. 1991. " Indigenous and exogenous enzymes in meat ". In Food Enzymology, Edited by: Fox, P. F. Vol. 2, 237-264. London, UK: Elsevier Applied Science.
    • (1991) Food Enzymology , vol.2 , pp. 237-264
    • Bailey, M.E.1    Murdock, F.A.2
  • 11
    • 0003932342 scopus 로고
    • Isolation and characterization of the four major cysteine-proteinase components of the latex of carica papaya
    • Baines, B. S. and Brocklehurst, K. 1982. Isolation and characterization of the four major cysteine-proteinase components of the latex of carica papaya. J. Protein Chem., 12: 119-139.
    • (1982) J. Protein Chem. , vol.12 , pp. 119-139
    • Baines, B.S.1    Brocklehurst, K.2
  • 12
    • 0019156319 scopus 로고
    • Structure of actinidin, after refinement at 1.7 A resolution
    • Baker, E. N. 1980. Structure of actinidin, after refinement at 1.7 A resolution. J. Mol. Biol., 141: 441-484.
    • (1980) J. Mol. Biol. , vol.141 , pp. 441-484
    • Baker, E.N.1
  • 13
    • 0005919263 scopus 로고
    • Bromelain: Properties and commercial production
    • Balls, A. K., Thompson, R. R. and Kies, M. W. 1941. Bromelain: Properties and commercial production. Ind. Eng. Chem. Res., 33: 950-953.
    • (1941) Ind. Eng. Chem. Res. , vol.33 , pp. 950-953
    • Balls, A.K.1    Thompson, R.R.2    Kies, M.W.3
  • 15
    • 75849133926 scopus 로고    scopus 로고
    • Rapid method for quantitative determination of proteolytic activity with cyclic voltammetry
    • Baş, D. and Boyaci, I. H. 2010. Rapid method for quantitative determination of proteolytic activity with cyclic voltammetry. Electroanalysis, 22: 265-267.
    • (2010) Electroanalysis , vol.22 , pp. 265-267
    • Baş, D.1    Boyaci, I.H.2
  • 16
    • 41049094962 scopus 로고    scopus 로고
    • Production and characterization of extracellular protease of mutant Aspergillus niger AB100 grown on fish scale
    • Basu, B. R., Banik, A. K. and Das, M. 2008. Production and characterization of extracellular protease of mutant Aspergillus niger AB100 grown on fish scale. World J. Microbiol. Biotechn., 24: 449-455.
    • (2008) World J. Microbiol. Biotechn. , vol.24 , pp. 449-455
    • Basu, B.R.1    Banik, A.K.2    Das, M.3
  • 17
    • 84893561349 scopus 로고    scopus 로고
    • Fermentation of Fish Roe
    • In: Heldman D. R., Hoover D. G., Wheeler M. B., editors USA,: Taylor & Francis Group
    • Bekhit, A. E. D. 2010. " Fermentation of Fish Roe ". In The Encyclopedia of Biotechnology in Agriculture and Food, Edited by: Heldman, D. R., Hoover, D. G. and Wheeler, M. B. Vol. 1, 251-256. USA: Taylor & Francis Group.
    • (2010) The Encyclopedia of Biotechnology in Agriculture and Food , vol.1 , pp. 251-256
    • Bekhit, A.E.D.1
  • 18
    • 33644497941 scopus 로고    scopus 로고
    • Towards unifying meat shear force measurement systems to determine meat tenderness
    • th International Conference of Meat Science and Technology
    • th International Conference of Meat Science and Technology
    • (2003) , pp. 221-222
    • Bekhit, A.E.D.1    Devine, C.E.2    Morton, J.D.3    Bickerstaffe, R.4
  • 19
    • 68949141019 scopus 로고    scopus 로고
    • Effect of kiwifruit juice and water pre-rigor infusion on lamb quality
    • rd International Conference of Meat Science and Technology
    • rd International Conference of Meat Science and Technology
    • (2007) , pp. 377-378
    • Bekhit, A.E.D.1    Han, J.2    Morton, J.3    Sedcole, R.4
  • 20
    • 0037208104 scopus 로고    scopus 로고
    • Warner-Bratzler shear evaluations of 40 bovine muscles
    • Belew, J. B., Brooks, J. C., McKenna, D. R. and Savell, J. W. 2003. Warner-Bratzler shear evaluations of 40 bovine muscles. Meat Sci., 64: 507-512.
    • (2003) Meat Sci. , vol.64 , pp. 507-512
    • Belew, J.B.1    Brooks, J.C.2    McKenna, D.R.3    Savell, J.W.4
  • 21
    • 0038266965 scopus 로고    scopus 로고
    • Effect of the fungal extracellular protease EPg222 on texture of whole pieces of pork loin
    • Benito, M. J., Rodríguez, M., Acosta, R. and Córdoba, J. J. 2003. Effect of the fungal extracellular protease EPg222 on texture of whole pieces of pork loin. Meat Sci., 65: 877-884.
    • (2003) Meat Sci. , vol.65 , pp. 877-884
    • Benito, M.J.1    Rodríguez, M.2    Acosta, R.3    Córdoba, J.J.4
  • 22
    • 0034097961 scopus 로고    scopus 로고
    • Pig plasma protein: Potential use as proteinase inhibitor for surimi manufacture; inhibitory activity and the active components
    • Benjakul, S. and Visessanguan, W. 2000. Pig plasma protein: Potential use as proteinase inhibitor for surimi manufacture; inhibitory activity and the active components. J. Sci. Food Agr., 80: 1351-1356.
    • (2000) J. Sci. Food Agr. , vol.80 , pp. 1351-1356
    • Benjakul, S.1    Visessanguan, W.2
  • 23
    • 0014942114 scopus 로고
    • Mapping the active site of papain with the aid of peptide substrates and inhibitors
    • Berger, A. and Schechter, I. 1970. Mapping the active site of papain with the aid of peptide substrates and inhibitors. Phil. Trans. R. Soc. B. Biol. Sci., 257: 249-264.
    • (1970) Phil. Trans. R. Soc. B. Biol. Sci. , vol.257 , pp. 249-264
    • Berger, A.1    Schechter, I.2
  • 24
    • 84893576500 scopus 로고
    • The proteolytic enzymes of Aspergillus oryzae. IV. On the inhibition of the enzymes by serum
    • Bergkvist, R. 1963. The proteolytic enzymes of Aspergillus oryzae. IV. On the inhibition of the enzymes by serum. Acta Chem. Scand., 17: 2239-2249.
    • (1963) Acta Chem. Scand. , vol.17 , pp. 2239-2249
    • Bergkvist, R.1
  • 25
    • 84986483792 scopus 로고
    • Processing systems for hot- and cold-boned primal from mature cow carcasses
    • Berry, B. W. and Cross, H. R. 1982. Processing systems for hot- and cold-boned primal from mature cow carcasses. J. Food Sci., 47: 875-879.
    • (1982) J. Food Sci. , vol.47 , pp. 875-879
    • Berry, B.W.1    Cross, H.R.2
  • 26
    • 33644917143 scopus 로고    scopus 로고
    • Preparation of proteolytic activity rich ginger powder and evaluation of its tenderizing effect on spent-hen muscles
    • Bhaskar, N., Sachindra, N. M., Modi, V. K., Sakhare, P. Z. and Mahendrakar, N. S. 2006. Preparation of proteolytic activity rich ginger powder and evaluation of its tenderizing effect on spent-hen muscles. J. Muscle Foods., 17: 174-184.
    • (2006) J. Muscle Foods. , vol.17 , pp. 174-184
    • Bhaskar, N.1    Sachindra, N.M.2    Modi, V.K.3    Sakhare, P.Z.4    Mahendrakar, N.S.5
  • 28
    • 0001049937 scopus 로고
    • A new protease activity assay using fluorescence polarization
    • Bolger, R. and Checovich, W. 1994. A new protease activity assay using fluorescence polarization. Biotechniques., 17: 585-589.
    • (1994) Biotechniques. , vol.17 , pp. 585-589
    • Bolger, R.1    Checovich, W.2
  • 29
    • 0031161111 scopus 로고    scopus 로고
    • Actinidin levels in fruit of Actinidia species and some Actinidia arguta Rootstock-Scion combinations
    • Boyes, S., Strübi, P. and Marsh, H. 1997. Actinidin levels in fruit of Actinidia species and some Actinidia arguta Rootstock-Scion combinations. LWT, 30: 379-389.
    • (1997) LWT , vol.30 , pp. 379-389
    • Boyes, S.1    Strübi, P.2    Marsh, H.3
  • 30
    • 45949128116 scopus 로고
    • Clinical biochemistry and pathology of mature beef cattle following ante-mortem intravenous administration of a commercial papain preparation
    • Bradley, R., O'Toole, D. T., Wells, D. E, Anderson, P. H., Hartley, P., Berrett, S., Morris, J. E., Insch, C. G. and Hayward, E. A. 1987. Clinical biochemistry and pathology of mature beef cattle following ante-mortem intravenous administration of a commercial papain preparation. Meat Sci., 19: 139-151.
    • (1987) Meat Sci. , vol.19 , pp. 139-151
    • Bradley, R.1    O'Toole, D.T.2    Wells, D.E.3    Anderson, P.H.4    Hartley, P.5    Berrett, S.6    Morris, J.E.7    Insch, C.G.8    Hayward, E.A.9
  • 31
  • 32
    • 55449094462 scopus 로고    scopus 로고
    • Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d1, actinidin, and Act d2, a thaumation-like protein
    • Bublin, M., Radauer, C., Knulst, A., Wagner, S., Scheiner, O., Mackie, A. R., Mills, E. N. and Breiteneder, H. 2008. Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d1, actinidin, and Act d2, a thaumation-like protein. Mol. Nut. Food Res., 52: 1130-1139.
    • (2008) Mol. Nut. Food Res. , vol.52 , pp. 1130-1139
    • Bublin, M.1    Radauer, C.2    Knulst, A.3    Wagner, S.4    Scheiner, O.5    Mackie, A.R.6    Mills, E.N.7    Breiteneder, H.8
  • 33
    • 9644254396 scopus 로고
    • Proteolytic activity of Pseudomonas perolens and effects on porcine muscle
    • Buckley, D. J., Gann, G. L., Price, J. F. and Spink, G. C. 1974. Proteolytic activity of Pseudomonas perolens and effects on porcine muscle. J. Food Sci., 39: 825-828.
    • (1974) J. Food Sci. , vol.39 , pp. 825-828
    • Buckley, D.J.1    Gann, G.L.2    Price, J.F.3    Spink, G.C.4
  • 34
    • 79956105212 scopus 로고    scopus 로고
    • Ginger and its health claims: Molecular aspects
    • Butt, M. S. and Sultan, M. T. 2011. Ginger and its health claims: Molecular aspects. Crit. Rev. Food Sci. Nutr., 51: 383-393.
    • (2011) Crit. Rev. Food Sci. Nutr. , vol.51 , pp. 383-393
    • Butt, M.S.1    Sultan, M.T.2
  • 35
    • 85013021231 scopus 로고    scopus 로고
    • Adding enzymes to improve meat tenderness (Beef Facts: Product Enhancement series). National Cattlemen's Beef Association
    • Retrieved 12/11/2009, from
    • Calkins, C. R. and Sullivan, G. 2007. " Adding enzymes to improve meat tenderness (Beef Facts: Product Enhancement series). National Cattlemen's Beef Association ". Retrieved 12/11/2009, from http://www.beefresearch.org/CMDocs/BeefResearch/Adding%20Enzymes%20to%20Improve%20Beef%20Tenderness.pdf
    • (2007)
    • Calkins, C.R.1    Sullivan, G.2
  • 37
    • 33750231900 scopus 로고    scopus 로고
    • Le comportement du consommateur décodé par l'anthropologie. Le cas des crises de la vache folle
    • Cazes-Valette, G. 2001. Le comportement du consommateur décodé par l'anthropologie. Le cas des crises de la vache folle. Rev. Fr. Market., 183/184: 99-113.
    • (2001) Rev. Fr. Market. , vol.183-184 , pp. 99-113
    • Cazes-Valette, G.1
  • 38
    • 0019743640 scopus 로고
    • Amino acid analysis at the picomole level
    • Chang, J. Y., Knecht, R. and Braun, D. G. 1981. Amino acid analysis at the picomole level. Biochem. J., 199: 547-555.
    • (1981) Biochem. J. , vol.199 , pp. 547-555
    • Chang, J.Y.1    Knecht, R.2    Braun, D.G.3
  • 40
    • 0033533253 scopus 로고    scopus 로고
    • The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale
    • Choi, K. H., Laursen, R. A. and Allen, K. N. 1999. The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale. Biochem., 38: 11624-11633.
    • (1999) Biochem. , vol.38 , pp. 11624-11633
    • Choi, K.H.1    Laursen, R.A.2    Allen, K.N.3
  • 41
    • 68949091769 scopus 로고    scopus 로고
    • Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue
    • Christensen, M., Tørngren, M. A., Gunvig, A., Rozlosnik, N., Lametsch, R., Karlsson, A. H. and Ertbjerg, P. 2009. Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue. J. Sci. Food Agr., 89: 1607-1614.
    • (2009) J. Sci. Food Agr. , vol.89 , pp. 1607-1614
    • Christensen, M.1    Tørngren, M.A.2    Gunvig, A.3    Rozlosnik, N.4    Lametsch, R.5    Karlsson, A.H.6    Ertbjerg, P.7
  • 43
    • 84893586946 scopus 로고
    • The legislative aspects of the use of industrial enzymes
    • In: Godfrey T., Reichelt J., editors New York, New York,: Nature Press
    • Denner, W. H. B. 1983. " The legislative aspects of the use of industrial enzymes ". In Industrial Enzymology, Edited by: Godfrey, T. and Reichelt, J. 111-137. New York: Nature Press.
    • (1983) Industrial Enzymology , pp. 111-137
    • Denner, W.H.B.1
  • 44
    • 84865536159 scopus 로고    scopus 로고
    • Purification, characterization of alkaline protease enzyme from native isolate Aspergillus niger and its compatibility with commercial detergents
    • Devi, M. K., Banu, A. R., Gnanaprabhal, G. R., Pradeep, B. V. and Palaniswamy, M. 2008. Purification, characterization of alkaline protease enzyme from native isolate Aspergillus niger and its compatibility with commercial detergents. Indian J. Sci. Tech., 1: 1-6.
    • (2008) Indian J. Sci. Tech. , vol.1 , pp. 1-6
    • Devi, M.K.1    Banu, A.R.2    Gnanaprabhal, G.R.3    Pradeep, B.V.4    Palaniswamy, M.5
  • 45
    • 77956524061 scopus 로고    scopus 로고
    • Variation of meat shear force measurements- A characteristic of meat
    • Proceedings of the 52nd International Conference of Meat Science and Technology
    • Devine, C. E., Wells, R. W. and North, M. 2006. Variation of meat shear force measurements- A characteristic of meat.: 575-576. Proceedings of the 52nd International Conference of Meat Science and Technology
    • (2006) , pp. 575-576
    • Devine, C.E.1    Wells, R.W.2    North, M.3
  • 46
    • 2642661481 scopus 로고    scopus 로고
    • Asthma caused by Ficus benjamina latex: Evidence of cross-reactivity with fig fruit and papain
    • Díez Gömez, M. L., Quirce, S. and Aragoneses, E. 1998. Asthma caused by Ficus benjamina latex: Evidence of cross-reactivity with fig fruit and papain. Ann. Allergy Asthma Immunol., 80: 24-30.
    • (1998) Ann. Allergy Asthma Immunol. , vol.80 , pp. 24-30
    • Díez Gömez, M.L.1    Quirce, S.2    Aragoneses, E.3
  • 47
    • 0010284704 scopus 로고
    • Enzymes in the tenderization of Meat
    • In: Birch G. G., Blakebrough N., Parker K. J., editors London, UK, London,: Applied Science Publishers LTD
    • Dransfield, E. and Etherington, D. 1981. " Enzymes in the tenderization of Meat ". In Enzymes and Food Processing, Edited by: Birch, G. G., Blakebrough, N. and Parker, K. J. 177-194. London, UK: Applied Science Publishers LTD.
    • (1981) Enzymes and Food Processing , pp. 177-194
    • Dransfield, E.1    Etherington, D.2
  • 48
    • 33746331364 scopus 로고    scopus 로고
    • Bovine muscle 20S proteasome. II: Contribution of the 20S proteasome to meat tenderization as revealed by an ultrastructural approach
    • Dutaud, D., Aubry, L., Guignot, F., Vignon, X., Monin, G. and Ouali, A. 2006. Bovine muscle 20S proteasome. II: Contribution of the 20S proteasome to meat tenderization as revealed by an ultrastructural approach. Meat Sci., 74: 337-344.
    • (2006) Meat Sci. , vol.74 , pp. 337-344
    • Dutaud, D.1    Aubry, L.2    Guignot, F.3    Vignon, X.4    Monin, G.5    Ouali, A.6
  • 49
    • 84893534384 scopus 로고    scopus 로고
    • Codex Alimentarius Commission, Codex Ad Hoc Report of the 3rd Session of the Intergovernmental Task Force on Foods Derived from Biotechnology, Yokohama, Japan, 4-8 March 2002
    • FAO/WHO, Joint FAO/WHO Food Standard Programme, Twenty-Fifth Session, Rome, Italy 30 June- 5 July 2003
    • FAO/WHO. 2003. " Codex Alimentarius Commission, Codex Ad Hoc Report of the 3rd Session of the Intergovernmental Task Force on Foods Derived from Biotechnology, Yokohama, Japan, 4-8 March 2002 ". Joint FAO/WHO Food Standard Programme, Twenty-Fifth Session, Rome, Italy 30 June- 5 July 2003
    • (2003)
  • 50
    • 0025823806 scopus 로고
    • A continuous fluorescent assay for measuring protease activity sing natural protein substrate
    • Farmer, W. H. and Yuan, Z. 1991. A continuous fluorescent assay for measuring protease activity sing natural protein substrate. Anal. Biochem., 197: 347-352.
    • (1991) Anal. Biochem. , vol.197 , pp. 347-352
    • Farmer, W.H.1    Yuan, Z.2
  • 51
    • 27744551916 scopus 로고    scopus 로고
    • Determining consumer valuation of differentiated beef steak quality attributes
    • Feldkamp, T. J., Schroeder, T. C. and Lusk, J. L. 2005. Determining consumer valuation of differentiated beef steak quality attributes. J. Muscle Foods, 16: 1-15.
    • (2005) J. Muscle Foods , vol.16 , pp. 1-15
    • Feldkamp, T.J.1    Schroeder, T.C.2    Lusk, J.L.3
  • 52
    • 0038162199 scopus 로고    scopus 로고
    • Cross-reactivity between Ficus benjamina latex and fig fruit in patients with clinical fig allergy
    • Focke, M., Hemmer, W., Wöhrl, S., Götz, M. and Jarisch, R. 2003. Cross-reactivity between Ficus benjamina latex and fig fruit in patients with clinical fig allergy. Clin. Exp. Allergy, 33: 971-977.
    • (2003) Clin. Exp. Allergy , vol.33 , pp. 971-977
    • Focke, M.1    Hemmer, W.2    Wöhrl, S.3    Götz, M.4    Jarisch, R.5
  • 53
    • 0000051107 scopus 로고
    • Tenderization of beef with bacterial collagenase
    • Foegeding, E. A. and Larick, D. K. 1986. Tenderization of beef with bacterial collagenase. Meat Sci., 19: 201-214.
    • (1986) Meat Sci. , vol.19 , pp. 201-214
    • Foegeding, E.A.1    Larick, D.K.2
  • 54
    • 84986533217 scopus 로고
    • Tenderization of beef: Effect of enzyme, enzyme level, and cooking method
    • Fogle, D. R., Plimpton, R. F., Ockerman, H. W., Jarenback, L. and Presson, T. 1982. Tenderization of beef: Effect of enzyme, enzyme level, and cooking method. J. Food Sci., 47: 1113-1118.
    • (1982) J. Food Sci. , vol.47 , pp. 1113-1118
    • Fogle, D.R.1    Plimpton, R.F.2    Ockerman, H.W.3    Jarenback, L.4    Presson, T.5
  • 55
    • 84893526529 scopus 로고
    • Enzyme Preparations From Animal and Plant Sources; Affirmation of Gras Status as Direct Food Ingredients 60 Fed
    • Food and Drug Administration, Reg. 32904-32912 (21 CFR PART 184, [Docket No. 84G-0257])
    • Food and Drug Administration. 1995, June 26. " Enzyme Preparations From Animal and Plant Sources; Affirmation of Gras Status as Direct Food Ingredients 60 Fed ". Reg. 32904-32912 (21 CFR PART 184, [Docket No. 84G-0257])
    • (1995)
  • 56
    • 84893602092 scopus 로고    scopus 로고
    • Secondary Direct Food Additives Permitted in Food for Human Consumption; Milk-Clotting Enzymes
    • Food and Drug Administration, 62 Fed. Reg. 59281-59284 (21 CFR Part 173, [Docket No. 93F-0461])
    • Food and Drug Administration. 1997, November 3. " Secondary Direct Food Additives Permitted in Food for Human Consumption; Milk-Clotting Enzymes ". 62 Fed. Reg. 59281-59284 (21 CFR Part 173, [Docket No. 93F-0461])
    • (1997)
  • 57
    • 84892321647 scopus 로고    scopus 로고
    • Carbohydrase and protease enzyme preparations derived from Bacillus subtilis or Bacillus amyloliquefaciens: Affirmation of GRAS Status as direct food ingredients
    • Food and Drug Administration, 64 Fed. Reg. 19887-19895 (21 CFR Part 184, [Docket No. 84G-0257])
    • Food and Drug Administration. 1999, April 23. " Carbohydrase and protease enzyme preparations derived from Bacillus subtilis or Bacillus amyloliquefaciens: Affirmation of GRAS Status as direct food ingredients ". 64 Fed. Reg. 19887-19895 (21 CFR Part 184, [Docket No. 84G-0257])
    • (1999)
  • 58
    • 84893575477 scopus 로고    scopus 로고
    • Database of select committee on GRAS substances (SCOGS) reviews
    • Food and Drug Administration, CFR184.1585, Available from. Accessed on October 12, 2009
    • Food and Drug Administration. 2009. " Database of select committee on GRAS substances (SCOGS) reviews ". CFR184.1585, Available from http://www.accessdata.fda.gov/scripts/fcn/fcnNavigation.cfm?rpt=scogsListing&displayAll=true. Accessed on October 12, 2009
    • (2009)
  • 59
    • 0014278378 scopus 로고
    • Ficin and papain inhibitor from chicken egg white
    • Fossum, K. and Whitaker, J. R. 1968. Ficin and papain inhibitor from chicken egg white. Arch. Biochem. Biophys., 126: 367-375.
    • (1968) Arch. Biochem. Biophys. , vol.126 , pp. 367-375
    • Fossum, K.1    Whitaker, J.R.2
  • 60
    • 85006550164 scopus 로고
    • The activation of papain
    • Fruton, J. S. and Bergmann, M. 1940. The activation of papain. J. Biol. Chem., 133: 153-156.
    • (1940) J. Biol. Chem. , vol.133 , pp. 153-156
    • Fruton, J.S.1    Bergmann, M.2
  • 62
    • 84986525859 scopus 로고
    • Modulating the conditioning of meat by the use of oryzacyctatin, a cysteine proteinase inhibitor of rice seed origin
    • Funaki, J., Abe, K., Hayabuchi, H. and Arai, S. 1991. Modulating the conditioning of meat by the use of oryzacyctatin, a cysteine proteinase inhibitor of rice seed origin. J. Food Biochem., 15: 253-262.
    • (1991) J. Food Biochem. , vol.15 , pp. 253-262
    • Funaki, J.1    Abe, K.2    Hayabuchi, H.3    Arai, S.4
  • 64
  • 67
    • 0034332241 scopus 로고    scopus 로고
    • Rigor temperature and meat quality characteristics of lamb longissimus muscle
    • Geesink, G. H., Bekhit, A. D. and Bickerstaffe, R. 2000. Rigor temperature and meat quality characteristics of lamb longissimus muscle. J. Anim. Sci., 78: 2842-2848.
    • (2000) J. Anim. Sci. , vol.78 , pp. 2842-2848
    • Geesink, G.H.1    Bekhit, A.D.2    Bickerstaffe, R.3
  • 68
    • 33749402662 scopus 로고    scopus 로고
    • μ-Calpain is essential for postmortem proteolysis of muscle proteins
    • Geesink, G. H., Kuchay, S., Chishti, A. H. and Koohmaraie, M. 2006. μ-Calpain is essential for postmortem proteolysis of muscle proteins. J. Anim. Sci., 84: 2834-2840.
    • (2006) J. Anim. Sci. , vol.84 , pp. 2834-2840
    • Geesink, G.H.1    Kuchay, S.2    Chishti, A.H.3    Koohmaraie, M.4
  • 69
    • 85079996733 scopus 로고    scopus 로고
    • Muscle enzymes: Proteinases
    • In: Nollet L., Toldra F., editors USA,: Taylor & Francis Group
    • Geesink, G. H. and Veiseth, E. 2009. " Muscle enzymes: Proteinases ". In Handbook of Muscle Food Analysis, Edited by: Nollet, L. and Toldra, F. 91-110. USA: Taylor & Francis Group.
    • (2009) Handbook of Muscle Food Analysis , pp. 91-110
    • Geesink, G.H.1    Veiseth, E.2
  • 70
    • 0034373990 scopus 로고    scopus 로고
    • Meat tenderization by proteolytic enzymes after osmotic dehydration
    • Gerelt, B., Ikeuchi, Y. and Suzuki, A. 2000. Meat tenderization by proteolytic enzymes after osmotic dehydration. Meat Sci., 56: 311-318.
    • (2000) Meat Sci. , vol.56 , pp. 311-318
    • Gerelt, B.1    Ikeuchi, Y.2    Suzuki, A.3
  • 71
    • 0030845998 scopus 로고    scopus 로고
    • Effects of high pressure on Papain activity and structure
    • Gomes, M. R. A., Sumner, I. G. and Ledward, D. A. 1997. Effects of high pressure on Papain activity and structure. J. Sci. Food Agr., 75: 67-72.
    • (1997) J. Sci. Food Agr. , vol.75 , pp. 67-72
    • Gomes, M.R.A.1    Sumner, I.G.2    Ledward, D.A.3
  • 72
    • 38349025923 scopus 로고    scopus 로고
    • Cysteine proteases
    • In: Polaina J., MacCabe A. P., editors NY, USA, NY,: Springer
    • Grzonka, Z., Kasprzykowski, F. and Wiczk, W. 2007. " Cysteine proteases ". In Industrial Enzymes, Edited by: Polaina, J. and MacCabe, A. P. 181-195. NY, USA: Springer.
    • (2007) Industrial Enzymes , pp. 181-195
    • Grzonka, Z.1    Kasprzykowski, F.2    Wiczk, W.3
  • 73
    • 33947197428 scopus 로고    scopus 로고
    • Thermal destabilization of stem bromelain by Trehalose
    • Habib, S., Khan, M. A. and Younus, H. 2007. Thermal destabilization of stem bromelain by Trehalose. Protein J., 26: 117-124.
    • (2007) Protein J. , vol.26 , pp. 117-124
    • Habib, S.1    Khan, M.A.2    Younus, H.3
  • 74
    • 13844289324 scopus 로고    scopus 로고
    • Proteinase activity and stability of natural bromelain preparations
    • Hale, L. P., Greer, P. K., Trinh, C. T. and James, C. L. 2005. Proteinase activity and stability of natural bromelain preparations. Int. Immunopharmacol., 5: 783-793.
    • (2005) Int. Immunopharmacol. , vol.5 , pp. 783-793
    • Hale, L.P.1    Greer, P.K.2    Trinh, C.T.3    James, C.L.4
  • 75
    • 0029910233 scopus 로고    scopus 로고
    • Vitamin C: Antioxidant or pro-oxidant in vivo?
    • Halliwell, B. 1996. Vitamin C: Antioxidant or pro-oxidant in vivo?. Free Radic. Res., 25: 439-454.
    • (1996) Free Radic. Res. , vol.25 , pp. 439-454
    • Halliwell, B.1
  • 76
    • 64049117743 scopus 로고    scopus 로고
    • Pre-rigor infusion with kiwifruit juice improves lamb tenderness
    • Han, J., Morton, J. D., Bekhit, A. E. D. and Sedcole, J. R. 2009. Pre-rigor infusion with kiwifruit juice improves lamb tenderness. Meat Sci., 82: 324-330.
    • (2009) Meat Sci. , vol.82 , pp. 324-330
    • Han, J.1    Morton, J.D.2    Bekhit, A.E.D.3    Sedcole, J.R.4
  • 77
    • 0000173363 scopus 로고    scopus 로고
    • Isolation and partial characterization of a soybean cystatin cysteine proteinase inhibitor of Coleopteran digestive proteolytic activity
    • (1991)
    • Hines, M. E., Osuala, C. I. and Nielsen, S. S. Isolation and partial characterization of a soybean cystatin cysteine proteinase inhibitor of Coleopteran digestive proteolytic activity. J. Agric. Food Chem., 31 1515-1520. (1991)
    • J. Agric. Food Chem. , vol.31 , pp. 1515-1520
    • Hines, M.E.1    Osuala, C.I.2    Nielsen, S.S.3
  • 79
    • 84355163741 scopus 로고    scopus 로고
    • Tendering mechanisms: Mechanical
    • In: Jensen W. K., Devine C., Dikeman M., editors Oxford, UK, Oxford,: Elsevier Academic Press
    • Hopkins, D. L. 2004. " Tendering mechanisms: Mechanical ". In Encyclopedia of Meat Sciences, Edited by: Jensen, W. K., Devine, C. and Dikeman, M. 1355-1363. Oxford, UK: Elsevier Academic Press.
    • (2004) Encyclopedia of Meat Sciences , pp. 1355-1363
    • Hopkins, D.L.1
  • 80
    • 84959538627 scopus 로고    scopus 로고
    • Protein degradation post mortem and tenderisation
    • In: Du M., McCormick R., editors USA,: CRC Press, Taylor & Francis Group
    • Hopkins, D. L. and Geesink, G. H. 2009. " Protein degradation post mortem and tenderisation. In: Applied Muscle Biology and Meat Science ". Edited by: Du, M. and McCormick, R. 149-173. USA: CRC Press, Taylor & Francis Group.
    • (2009) Applied Muscle Biology and Meat Science , pp. 149-173
    • Hopkins, D.L.1    Geesink, G.H.2
  • 81
    • 84355163741 scopus 로고    scopus 로고
    • Tenderizing mechanisms: Chemical and enzymatic
    • In: Jensen W. K., Devine C., Dikeman M., editors Oxford, UK, Oxford,: Elsevier Academic Press
    • Hopkins, D. L. and Huff-Lonergan, E. 2004. " Tenderizing mechanisms: Chemical and enzymatic. In: Encyclopedia of Meat Sciences ". Edited by: Jensen, W. K., Devine, C. and Dikeman, M. 11363-1369. Oxford, UK: Elsevier Academic Press.
    • (2004) Encyclopedia of Meat Sciences , pp. 11363-11369
    • Hopkins, D.L.1    Huff-Lonergan, E.2
  • 82
    • 0036198178 scopus 로고    scopus 로고
    • Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat
    • Hopkins, D. L. and Thompson, J. M. 2002. Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat. Aust. J. Agr. Res., 53: 149-166.
    • (2002) Aust. J. Agr. Res. , vol.53 , pp. 149-166
    • Hopkins, D.L.1    Thompson, J.M.2
  • 83
    • 1242310089 scopus 로고    scopus 로고
    • Up- and down-regulation of longissimus tenderness parallels changes in the myofibril-bound calpain 3 protein
    • Ilian, M. A., Bekhit, A. E. D., Stevenson, B., Morton, J. D., Isherwood, P. and Bickerstaffe, R. 2004. Up- and down-regulation of longissimus tenderness parallels changes in the myofibril-bound calpain 3 protein. Meat Sci., 67: 433-445.
    • (2004) Meat Sci. , vol.67 , pp. 433-445
    • Ilian, M.A.1    Bekhit, A.E.D.2    Stevenson, B.3    Morton, J.D.4    Isherwood, P.5    Bickerstaffe, R.6
  • 84
    • 0343223471 scopus 로고
    • Kinetic studies of bromelain catalysis
    • Inagami, T. and Murachi, T. 1963. Kinetic studies of bromelain catalysis. Biochem., 2: 1439-1444.
    • (1963) Biochem. , vol.2 , pp. 1439-1444
    • Inagami, T.1    Murachi, T.2
  • 85
    • 0347373594 scopus 로고    scopus 로고
    • Purification and characterization of extracellular cysteine protease inhibitor from Chlorella sp
    • Ishihara, M., Morine, N., Taira, T. and Toya, S. 2000. Purification and characterization of extracellular cysteine protease inhibitor from Chlorella sp. Food Sci. Techol. Res., 6: 161-165.
    • (2000) Food Sci. Techol. Res. , vol.6 , pp. 161-165
    • Ishihara, M.1    Morine, N.2    Taira, T.3    Toya, S.4
  • 86
    • 84893625383 scopus 로고
    • The activation of Papain and related plant enzymes with sodium thiosulfate
    • Jaffé, W. G. 1945. The activation of Papain and related plant enzymes with sodium thiosulfate. Arch. Biochem., 8: 385-393.
    • (1945) Arch. Biochem. , vol.8 , pp. 385-393
    • Jaffé, W.G.1
  • 87
  • 88
    • 84893590992 scopus 로고    scopus 로고
    • Tenderization of meat by natural enzyme control
    • US Patent 4,336,271
    • Kang, C. K., Jodlowski, R. F., Donnelly, T. H. and Warner, W. D. Tenderization of meat by natural enzyme control. 1982a. US Patent 4,336,271
    • Kang, C.K.1    Jodlowski, R.F.2    Donnelly, T.H.3    Warner, W.D.4
  • 89
    • 29744461973 scopus 로고    scopus 로고
    • Inhibition of protease in intact fish fillets by soaking in or injection of recombinant soy cystatin or bovine plasma
    • Kang, I. and Lanier, T. C. 2005. Inhibition of protease in intact fish fillets by soaking in or injection of recombinant soy cystatin or bovine plasma. J. Agric. Food Chem., 53: 9795-9799.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 9795-9799
    • Kang, I.1    Lanier, T.C.2
  • 90
    • 84986466174 scopus 로고
    • Degradation of various meat fractions by tenderizing enzymes
    • Kang, C. K. and Rice, E. E. 1970. Degradation of various meat fractions by tenderizing enzymes. J. Food Sci., 35: 563-565.
    • (1970) J. Food Sci. , vol.35 , pp. 563-565
    • Kang, C.K.1    Rice, E.E.2
  • 91
    • 84987332280 scopus 로고
    • Tenderization of meat with papaya latex proteases
    • Kang, C. K. and Warner, W. D. 1974. Tenderization of meat with papaya latex proteases. J. Food Sci., 39: 812-818.
    • (1974) J. Food Sci. , vol.39 , pp. 812-818
    • Kang, C.K.1    Warner, W.D.2
  • 93
    • 84893551321 scopus 로고    scopus 로고
    • Tenderization of meat by with proteolytic enzymes
    • US Patent 3,818,106
    • Kang, C. K., Warner, W. D. and Rice, E. E. Tenderization of meat by with proteolytic enzymes. 1982b. US Patent 3,818,106
    • Kang, C.K.1    Warner, W.D.2    Rice, E.E.3
  • 94
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer, K. M., Peiffer, S. L. and DiTomas, M. E. 1993. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. USA., 90: 3063-3067.
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 97
    • 0026096833 scopus 로고
    • Specific degradation of myosin in meat by Bromelain research note
    • Kim, H.-J. and Taub, I. A. 1991. Specific degradation of myosin in meat by Bromelain research note. Food Chem., 40: 337-343.
    • (1991) Food Chem. , vol.40 , pp. 337-343
    • Kim, H.-J.1    Taub, I.A.2
  • 98
    • 1042290220 scopus 로고    scopus 로고
    • Papain protects papaya trees from herbivorous insects: Role of cysteine proteases in latex
    • Konno, K., Hirayama, C., Nakamura, M., Tateishi, K., Tamura, Y., Hattori, M. and Kohno, K. 2004. Papain protects papaya trees from herbivorous insects: Role of cysteine proteases in latex. Plant J., 37: 370-378.
    • (2004) Plant J. , vol.37 , pp. 370-378
    • Konno, K.1    Hirayama, C.2    Nakamura, M.3    Tateishi, K.4    Tamura, Y.5    Hattori, M.6    Kohno, K.7
  • 99
    • 33745648075 scopus 로고    scopus 로고
    • Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system
    • Koohmaraie, M. and Geesink, G. H. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci., 74: 34-43.
    • (2006) Meat Sci. , vol.74 , pp. 34-43
    • Koohmaraie, M.1    Geesink, G.H.2
  • 100
    • 0000391619 scopus 로고
    • Ficus Enzymes: II. Properties of the proteolytic enzymes from the latex of Ficus carica variety Kadota
    • Kramer, D. E. and Whitaker, J. R. 1964. Ficus Enzymes: II. Properties of the proteolytic enzymes from the latex of Ficus carica variety Kadota. J. Biol. Chem., 239: 2178-2183.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2178-2183
    • Kramer, D.E.1    Whitaker, J.R.2
  • 101
    • 0027310980 scopus 로고
    • Reagents for the preparation of chromphorically labeled polyethylene glycol-protein conjugates
    • Ladd, D. L. and Snow, R. A. 1993. Reagents for the preparation of chromphorically labeled polyethylene glycol-protein conjugates. Anal. Biochem., 210: 258-261.
    • (1993) Anal. Biochem. , vol.210 , pp. 258-261
    • Ladd, D.L.1    Snow, R.A.2
  • 102
    • 0030681334 scopus 로고    scopus 로고
    • Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases
    • Lee, K. L., Albee, K. L., Bernasconi, R. J. and Edmunds, T. 1997. Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases. Biochem. J., 327: 199-202.
    • (1997) Biochem. J. , vol.327 , pp. 199-202
    • Lee, K.L.1    Albee, K.L.2    Bernasconi, R.J.3    Edmunds, T.4
  • 103
    • 0013637393 scopus 로고
    • Tenderization of meat with ginger rhizome protease
    • Lee, Y. B., Sehnert, D. J. and Ashmore, C. R. 1986. Tenderization of meat with ginger rhizome protease. J. Food Sci., 51: 1558-1559.
    • (1986) J. Food Sci. , vol.51 , pp. 1558-1559
    • Lee, Y.B.1    Sehnert, D.J.2    Ashmore, C.R.3
  • 104
    • 70449698635 scopus 로고    scopus 로고
    • A second look into fibre typing-Relation to meat quality
    • Lefaucheur, L. 2010. A second look into fibre typing-Relation to meat quality. Meat Sci., 84: 257-270.
    • (2010) Meat Sci. , vol.84 , pp. 257-270
    • Lefaucheur, L.1
  • 105
    • 52249084763 scopus 로고    scopus 로고
    • Collagen contribution to meat toughness: Theoretical aspects
    • Lepetit, J. 2008. Collagen contribution to meat toughness: Theoretical aspects. Meat Sci., 80: 960-967.
    • (2008) Meat Sci. , vol.80 , pp. 960-967
    • Lepetit, J.1
  • 106
    • 84986516462 scopus 로고
    • Application of actinidin from kiwifruit to meat tenderization and characterization of beef muscle protein hydrolysis
    • Lewis, D. A. and Luh, B. S. 1988. Application of actinidin from kiwifruit to meat tenderization and characterization of beef muscle protein hydrolysis. J. Food Biochem., 12: 147-158.
    • (1988) J. Food Biochem. , vol.12 , pp. 147-158
    • Lewis, D.A.1    Luh, B.S.2
  • 107
    • 0023801371 scopus 로고
    • Interaction of the cysteine Proteinase inhibitor chicken cystatin with papain
    • Lindahl, P., Alriksson, E., Jornvall, H. and Bjork, I. 1988. Interaction of the cysteine Proteinase inhibitor chicken cystatin with papain. Biochem., 27: 5074-5082.
    • (1988) Biochem. , vol.27 , pp. 5074-5082
    • Lindahl, P.1    Alriksson, E.2    Jornvall, H.3    Bjork, I.4
  • 108
    • 84982339558 scopus 로고
    • A cold shortening effect in beef muscles
    • Locker, R. H. and Hagyard, C. J. 1963. A cold shortening effect in beef muscles. J. Sci. Food Agr., 14: 787-793.
    • (1963) J. Sci. Food Agr. , vol.14 , pp. 787-793
    • Locker, R.H.1    Hagyard, C.J.2
  • 110
    • 22144493345 scopus 로고    scopus 로고
    • Current research in meat color: Review
    • Mancini, R. A. and Hunt, M. C. 2005. Current research in meat color: Review. Meat Sci., 71: 100-121.
    • (2005) Meat Sci. , vol.71 , pp. 100-121
    • Mancini, R.A.1    Hunt, M.C.2
  • 111
    • 85012961861 scopus 로고
    • Effects of enzyme applications on sensory, chemical and process characteristics of beef steaks and roasts
    • McKeith, F. K., Brewer, S. M. and Bruggen, K. A. 1994. Effects of enzyme applications on sensory, chemical and process characteristics of beef steaks and roasts. J. Muscle Foods, 5: 149-164.
    • (1994) J. Muscle Foods , vol.5 , pp. 149-164
    • McKeith, F.K.1    Brewer, S.M.2    Bruggen, K.A.3
  • 113
  • 114
    • 84985204568 scopus 로고
    • Improved tenderness of restructured beef steaks by microbial collagenase derived from Vibrio B-30
    • Miller, A. J., Strange, E. D. and Whiting, R. C. 1989. Improved tenderness of restructured beef steaks by microbial collagenase derived from Vibrio B-30. J. Food Sci., 54: 855-857.
    • (1989) J. Food Sci. , vol.54 , pp. 855-857
    • Miller, A.J.1    Strange, E.D.2    Whiting, R.C.3
  • 115
    • 84981848867 scopus 로고
    • The hydrolysis of beef proteins by various proteolytic enzymes
    • Miyada, D. S. and Tappel, A. L. 1956. The hydrolysis of beef proteins by various proteolytic enzymes. J. Food Sci., 21: 217-225.
    • (1956) J. Food Sci. , vol.21 , pp. 217-225
    • Miyada, D.S.1    Tappel, A.L.2
  • 116
    • 19944371762 scopus 로고    scopus 로고
    • Isolation of natural inhibitors of papain obtained from Carica papaya Latex
    • Monti, R., Contiero, J. and José Goulart, A. 2004. Isolation of natural inhibitors of papain obtained from Carica papaya Latex. Braz. Arch. Biol. Technol., 47: 747-754.
    • (2004) Braz. Arch. Biol. Technol. , vol.47 , pp. 747-754
    • Monti, R.1    Contiero, J.2    José Goulart, A.3
  • 117
    • 33746887051 scopus 로고    scopus 로고
    • Effects of high concentration of salts on the esterase activity and structure of a kiwifruit peptidase, actinidain
    • Morimoto, K., Furuta, E., Hashimoto, H. and Inouye, K. 2006. Effects of high concentration of salts on the esterase activity and structure of a kiwifruit peptidase, actinidain. J. Biochem., 139: 1065-1071.
    • (2006) J. Biochem. , vol.139 , pp. 1065-1071
    • Morimoto, K.1    Furuta, E.2    Hashimoto, H.3    Inouye, K.4
  • 118
    • 1242290715 scopus 로고
    • Purification and physical characterization of stem Bromelain
    • Murachi, T., Yasui, M. and Yasuda, Y. 1964. Purification and physical characterization of stem Bromelain. Biochem., 3: 48-55.
    • (1964) Biochem. , vol.3 , pp. 48-55
    • Murachi, T.1    Yasui, M.2    Yasuda, Y.3
  • 120
    • 9644275379 scopus 로고    scopus 로고
    • Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome)
    • Naveena, B. M., Mendiratta, S. K. and Anjaneyulu, A. S. R. 2004. Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Meat Sci., 68: 363-369.
    • (2004) Meat Sci. , vol.68 , pp. 363-369
    • Naveena, B.M.1    Mendiratta, S.K.2    Anjaneyulu, A.S.R.3
  • 121
    • 0014084188 scopus 로고
    • The activation of Papain and Ficin by phosphorothioate
    • Neumann, H., Shinitzky, M. and Smith, R. A. 1967. The activation of Papain and Ficin by phosphorothioate. Biochem., 6: 1421-1428.
    • (1967) Biochem. , vol.6 , pp. 1421-1428
    • Neumann, H.1    Shinitzky, M.2    Smith, R.A.3
  • 123
    • 34047130232 scopus 로고    scopus 로고
    • Fruits of the actinidia genus
    • Nishiyama, I. 2007. Fruits of the actinidia genus. Adv. Food and Nutr. Res., 52: 293-324.
    • (2007) Adv. Food and Nutr. Res. , vol.52 , pp. 293-324
    • Nishiyama, I.1
  • 124
    • 0001453229 scopus 로고
    • Inhibition of papain in meat by potato protein or ascorbic acid
    • Ockerman, H. W., Harnsawas, S. and Yetim, H. 1993. Inhibition of papain in meat by potato protein or ascorbic acid. J. Food Sci., 58: 1265-1268.
    • (1993) J. Food Sci. , vol.58 , pp. 1265-1268
    • Ockerman, H.W.1    Harnsawas, S.2    Yetim, H.3
  • 125
    • 0028896997 scopus 로고
    • Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing
    • Ohtsuki, K., Taguchi, K., Sato, K. and Kawabata, M. 1995. Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing. Biochim. Biophys. Acta., 1243: 181-184.
    • (1995) Biochim. Biophys. Acta. , vol.1243 , pp. 181-184
    • Ohtsuki, K.1    Taguchi, K.2    Sato, K.3    Kawabata, M.4
  • 126
    • 0343290176 scopus 로고
    • Studies on Bromelain. II. Its activation and fractionation
    • Ota, S., Fu, T. H. and Hirohata, R. 1961. Studies on Bromelain. II. Its activation and fractionation. J. Biochem., 49: 532-537.
    • (1961) J. Biochem. , vol.49 , pp. 532-537
    • Ota, S.1    Fu, T.H.2    Hirohata, R.3
  • 129
    • 0015850539 scopus 로고
    • Isolation and characterization of a protease inhibitor from commercial stem bromelain acetone powder
    • Perlstein, S. H. and Kezdy, F. J. 1972. Isolation and characterization of a protease inhibitor from commercial stem bromelain acetone powder. J. Supramol. Struct., 1: 249-254.
    • (1972) J. Supramol. Struct. , vol.1 , pp. 249-254
    • Perlstein, S.H.1    Kezdy, F.J.2
  • 130
    • 0034223094 scopus 로고    scopus 로고
    • Bovine placental protease specificity towards muscle connective tissue proteins
    • Phillips, A. L., Means, W. J., Kalchayanand, N., McCormick, R. J. and Miller, K. W. 2000. Bovine placental protease specificity towards muscle connective tissue proteins. J. Anim. Sci., 78: 1861-1866.
    • (2000) J. Anim. Sci. , vol.78 , pp. 1861-1866
    • Phillips, A.L.1    Means, W.J.2    Kalchayanand, N.3    McCormick, R.J.4    Miller, K.W.5
  • 131
    • 73449085453 scopus 로고    scopus 로고
    • Influence of blade tenderization, moisture enhancement and pancreatin enzyme treatment on the processing characteristics and tenderness of beef semitendinosus muscle
    • Pietrasik, Z., Aalhus, J. L., Gibson, L. L. and Shand, P. J. 2010. Influence of blade tenderization, moisture enhancement and pancreatin enzyme treatment on the processing characteristics and tenderness of beef semitendinosus muscle. Meat Sci., 84: 512-517.
    • (2010) Meat Sci. , vol.84 , pp. 512-517
    • Pietrasik, Z.1    Aalhus, J.L.2    Gibson, L.L.3    Shand, P.J.4
  • 132
    • 77949568912 scopus 로고    scopus 로고
    • Effect of aspartic protease from Aspergillus oryzae on the tenderness of beef
    • nd International Conference of Meat Science and Technology
    • nd International Conference of Meat Science and Technology
    • (2006) , pp. 475-476
    • Pietrasik, Z.1    Shand, P.J.2
  • 133
    • 0015923982 scopus 로고
    • On the mode of activation of the catalytically essential sulfhydryl group of papain
    • Polgar, L. 1973. On the mode of activation of the catalytically essential sulfhydryl group of papain. Eur. J. Biochem., 33: 104-109.
    • (1973) Eur. J. Biochem. , vol.33 , pp. 104-109
    • Polgar, L.1
  • 134
    • 54049113036 scopus 로고    scopus 로고
    • Development of a commercial system to apply the Meat Standards Australia grading model to optimise the return on eating quality in a beef supply chain
    • Polkinghorne, R., Philpott, D. J., Gee, A., Doljanin, A. and Innes, J. 2008. Development of a commercial system to apply the Meat Standards Australia grading model to optimise the return on eating quality in a beef supply chain. Aust. J. Exp. Agr., 48: 1451-1458.
    • (2008) Aust. J. Exp. Agr. , vol.48 , pp. 1451-1458
    • Polkinghorne, R.1    Philpott, D.J.2    Gee, A.3    Doljanin, A.4    Innes, J.5
  • 135
    • 33645766998 scopus 로고    scopus 로고
    • Effects of elastase from a Bacillus strain on the tenderization of beef meat
    • Qihe, C., Guoqing, H., Yingchun, J. and Hui, N. 2006. Effects of elastase from a Bacillus strain on the tenderization of beef meat. Food Chem., 98: 624-629.
    • (2006) Food Chem. , vol.98 , pp. 624-629
    • Qihe, C.1    Guoqing, H.2    Yingchun, J.3    Hui, N.4
  • 136
    • 33947302375 scopus 로고    scopus 로고
    • Cysteine proteinase inhibitor from chicken plasma: Fractionation, characterization and autolysis inhibition of fish myofibrillar proteins
    • Rawdkuen, S., Benjakul, S., Visessanguan, W. and Lanier, T. C. 2007. Cysteine proteinase inhibitor from chicken plasma: Fractionation, characterization and autolysis inhibition of fish myofibrillar proteins. Food Chem., 101: 1647-1657.
    • (2007) Food Chem. , vol.101 , pp. 1647-1657
    • Rawdkuen, S.1    Benjakul, S.2    Visessanguan, W.3    Lanier, T.C.4
  • 138
    • 2342586055 scopus 로고    scopus 로고
    • Variation in palatability and biochemical traits within and among eleven beef muscles
    • Rhee, M. S., Wheeler, T. L., Shackelford, S. D. and Koohmaraie, M. 2004. Variation in palatability and biochemical traits within and among eleven beef muscles. J. Anim. Sci., 82: 534-550.
    • (2004) J. Anim. Sci. , vol.82 , pp. 534-550
    • Rhee, M.S.1    Wheeler, T.L.2    Shackelford, S.D.3    Koohmaraie, M.4
  • 139
    • 0015886561 scopus 로고
    • Effect of pre-slaughter injections of papain on toughness in lamb muscles induced by rapid chilling
    • Rhodes, D. N. and Dransfield, E. 1973. Effect of pre-slaughter injections of papain on toughness in lamb muscles induced by rapid chilling. J. Sci. Food Agri., 24: 1583-1588.
    • (1973) J. Sci. Food Agri. , vol.24 , pp. 1583-1588
    • Rhodes, D.N.1    Dransfield, E.2
  • 140
    • 84893589054 scopus 로고    scopus 로고
    • Meat tenderization with a proteolytic enzyme from Trichoderma reessei
    • US Patent 4,600,589
    • Robbins, F. M., Allen, A. L., Walker, J. E. and Cohen, S. H. Meat tenderization with a proteolytic enzyme from Trichoderma reessei. 1986. US Patent 4,600,589
    • Robbins, F.M.1    Allen, A.L.2    Walker, J.E.3    Cohen, S.H.4
  • 141
    • 0000395931 scopus 로고
    • Naturally occurring protein crystals in the potato. Inhibitor of Papain, Chymopapain and Ficin
    • Rodis, P. and Hoff, J. E. 1984. Naturally occurring protein crystals in the potato. Inhibitor of Papain, Chymopapain and Ficin. Plant Physiol., 74: 907-911.
    • (1984) Plant Physiol. , vol.74 , pp. 907-911
    • Rodis, P.1    Hoff, J.E.2
  • 142
    • 0024289238 scopus 로고
    • Ananain: A novel cysteine proteinase found in pineapple stem
    • Rowan, A. D., Buttle, D. J. and Barrett, A. J. 1988. Ananain: A novel cysteine proteinase found in pineapple stem. Arch. Biochem. Biophys., 267: 262-270.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 262-270
    • Rowan, A.D.1    Buttle, D.J.2    Barrett, A.J.3
  • 143
    • 0025268799 scopus 로고
    • The cysteine proteinases of the pineapple plant
    • Rowan, A. D., Buttle, D. J. and Barrett, A. J. 1990. The cysteine proteinases of the pineapple plant. Biochem. J., 266: 869-875.
    • (1990) Biochem. J. , vol.266 , pp. 869-875
    • Rowan, A.D.1    Buttle, D.J.2    Barrett, A.J.3
  • 144
    • 0013903416 scopus 로고
    • Chymotrypsin inhibitor I from potatoes: Reactivity with mammalian, plant, bacterial, and fungal proteinases
    • Ryan, C. A. 1966. Chymotrypsin inhibitor I from potatoes: Reactivity with mammalian, plant, bacterial, and fungal proteinases. Biochem., 5: 1592-1596.
    • (1966) Biochem. , vol.5 , pp. 1592-1596
    • Ryan, C.A.1
  • 146
    • 16244409236 scopus 로고    scopus 로고
    • A novel cysteine protease inhibitor with lectin activity from the epidermis of the Japanese eel Anguilla japonica
    • Saitoh, E., Isemura, S., Chiba, A., Oka, S. and Odani, S. 2005. A novel cysteine protease inhibitor with lectin activity from the epidermis of the Japanese eel Anguilla japonica. Comp. Biochem. Physiol. B., 141: 103-109.
    • (2005) Comp. Biochem. Physiol. B. , vol.141 , pp. 103-109
    • Saitoh, E.1    Isemura, S.2    Chiba, A.3    Oka, S.4    Odani, S.5
  • 149
    • 84893523627 scopus 로고
    • Applied enzymology of meat texture optimization
    • Westport, Connecticut, USA, Westport, Connecticut,: The AVI Publishing Company, Inc
    • Schwimmer, S. 1981. " Applied enzymology of meat texture optimization ". In Source Book of Food Enzymology, 481-496. Westport, Connecticut, USA: The AVI Publishing Company, Inc.
    • (1981) Source Book of Food Enzymology , pp. 481-496
    • Schwimmer, S.1
  • 150
    • 0036986447 scopus 로고    scopus 로고
    • Role of muscle endopeptidases and their inhibitors in meat tenderness
    • Sentandreu, M. A., Coulis, G. and Ouali, A. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci. Technol., 13: 400-421.
    • (2002) Trends Food Sci. Technol. , vol.13 , pp. 400-421
    • Sentandreu, M.A.1    Coulis, G.2    Ouali, A.3
  • 151
    • 0029399183 scopus 로고
    • Relationship between shear force and trained sensory panel tenderness ratings of 10 major muscles from Bos indicus and Bos taurus cattle
    • Shackelford, S. D., Wheeler, T. L. and Koohmaraie, M. 1995. Relationship between shear force and trained sensory panel tenderness ratings of 10 major muscles from Bos indicus and Bos taurus cattle. J. Anim. Sci., 73: 3333-3340.
    • (1995) J. Anim. Sci. , vol.73 , pp. 3333-3340
    • Shackelford, S.D.1    Wheeler, T.L.2    Koohmaraie, M.3
  • 152
    • 0014200129 scopus 로고
    • The activation reaction of papain
    • Sluyterman, L. A. 1967. The activation reaction of papain. Biochim. Biophys. Acta, 139: 430-438.
    • (1967) Biochim. Biophys. Acta , vol.139 , pp. 430-438
    • Sluyterman, L.A.1
  • 153
    • 84892322813 scopus 로고    scopus 로고
    • Enzymes
    • Oxford, UK, Oxford,: Blackwell Science
    • Smith, J. and Hong-Shum, L. 2003. " Enzymes ". In Food Additives Data Book, 389-462. Oxford, UK: Blackwell Science.
    • (2003) Food Additives Data Book , pp. 389-462
    • Smith, J.1    Hong-Shum, L.2
  • 154
    • 33748522739 scopus 로고    scopus 로고
    • Modified-atmosphere storage under subatmospheric pressure and beef quality: II. Color, drip, cooking loss, sarcomere length, and tenderness
    • Smulders, F. J. M., Hiesberger, J., Hofbauer, P., Dögl, B. and Dransfield, E. 2006. Modified-atmosphere storage under subatmospheric pressure and beef quality: II. Color, drip, cooking loss, sarcomere length, and tenderness. J. Anim. Sci., 84: 2456-2462.
    • (2006) J. Anim. Sci. , vol.84 , pp. 2456-2462
    • Smulders, F.J.M.1    Hiesberger, J.2    Hofbauer, P.3    Dögl, B.4    Dransfield, E.5
  • 155
    • 0015968138 scopus 로고
    • Properties of Clostridium perfringens (Welchii) type A α-toxin (phospolipase C) purified by electrofocusing
    • Smyth, C. J. and Arbuthnott, J. P. 1974. Properties of Clostridium perfringens (Welchii) type A α-toxin (phospolipase C) purified by electrofocusing. J. Med. Microbiol., 7: 41-66.
    • (1974) J. Med. Microbiol. , vol.7 , pp. 41-66
    • Smyth, C.J.1    Arbuthnott, J.P.2
  • 156
    • 78650250761 scopus 로고    scopus 로고
    • Effects of Enzymes on Beef Tenderness and Palatability Traits
    • Accessed October 11, 2009
    • Stefanek, J. L., Scanga, J. A., Belk, K. E. and Smith, G. C. 2002. " Effects of Enzymes on Beef Tenderness and Palatability Traits ". http://ansci.colostate.edu/content/view/10./ Accessed October 11, 2009
    • (2002)
    • Stefanek, J.L.1    Scanga, J.A.2    Belk, K.E.3    Smith, G.C.4
  • 157
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A. C. and Ménard, R. 1994. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol., 244: 486-500.
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Ménard, R.2
  • 158
    • 65649105394 scopus 로고    scopus 로고
    • Characterization of ginger proteases and their potential as a rennin replacement
    • Su, H.-P., Huanga, M.-J. and Wang, H.-T. 2009. Characterization of ginger proteases and their potential as a rennin replacement. J. Sci. Food Agri., 89: 1178-1185.
    • (2009) J. Sci. Food Agri. , vol.89 , pp. 1178-1185
    • Su, H.-P.1    Huanga, M.-J.2    Wang, H.-T.3
  • 159
    • 0030438338 scopus 로고    scopus 로고
    • Purification and characterization of six kiwifruit proteases isolated with two ion-exchange resins, Toyopearl-Super Q and Bakerbond WP-PEI
    • Sugiyama, S., Ohtsuki, K., Sato, K. and Kawabata, M. 1996. Purification and characterization of six kiwifruit proteases isolated with two ion-exchange resins, Toyopearl-Super Q and Bakerbond WP-PEI. Biosci. Biotechnol. Biochem., 60: 1994-2000.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1994-2000
    • Sugiyama, S.1    Ohtsuki, K.2    Sato, K.3    Kawabata, M.4
  • 160
    • 77956833621 scopus 로고    scopus 로고
    • Utilization of restructuring technology in the production of meat products: A review
    • Sun, X. D. 2009. Utilization of restructuring technology in the production of meat products: A review. CyTA- J. Food, 7: 153-162.
    • (2009) CyTA- J. Food , vol.7 , pp. 153-162
    • Sun, X.D.1
  • 161
    • 84893552283 scopus 로고    scopus 로고
    • Protease variants
    • US Patent 2007/0281332 A1
    • Svendsen, A. and Minning, S. Protease variants. 2007. US Patent 2007/0281332 A1
    • Svendsen, A.1    Minning, S.2
  • 163
    • 0001646115 scopus 로고
    • Effects of an alkaline elastase from an alkalophilic Bacillus sytrain on the tenderization of beef meat
    • Takagi, H., Kondou, M., Hisatsuka, T., Nakamori, S., Tsai, Y. C. and Yamasaki, M. 1992. Effects of an alkaline elastase from an alkalophilic Bacillus sytrain on the tenderization of beef meat. J. Agric. Food Chem., 40: 577-583.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 577-583
    • Takagi, H.1    Kondou, M.2    Hisatsuka, T.3    Nakamori, S.4    Tsai, Y.C.5    Yamasaki, M.6
  • 164
    • 84981879512 scopus 로고
    • Meat tenerization.II. Factors affecting the tenderization of beef by Papain
    • Tappel, A. L., Miyada, D. S., Sterling, C. and Maier, V. P. 1956. Meat tenerization.II. Factors affecting the tenderization of beef by Papain. J. Food Sci., 21: 375-383.
    • (1956) J. Food Sci. , vol.21 , pp. 375-383
    • Tappel, A.L.1    Miyada, D.S.2    Sterling, C.3    Maier, V.P.4
  • 165
    • 84990480579 scopus 로고
    • Papain induced allergic reactions
    • Tarlo, S. M., Shaikh, W. and Bell, B. 1978. Papain induced allergic reactions. Clin. Allergy., 8: 207-215.
    • (1978) Clin. Allergy. , vol.8 , pp. 207-215
    • Tarlo, S.M.1    Shaikh, W.2    Bell, B.3
  • 166
    • 0034966117 scopus 로고    scopus 로고
    • Ingredient and labeling issues associated with allergenic foods
    • Taylor, S. L. and Hefle, S. L. 2001. Ingredient and labeling issues associated with allergenic foods. Allergy., 56: 64-69.
    • (2001) Allergy. , vol.56 , pp. 64-69
    • Taylor, S.L.1    Hefle, S.L.2
  • 168
    • 84893526340 scopus 로고    scopus 로고
    • Method for tenderizing raw beef
    • US Patent 6,537, 598 B1
    • Teran, J. F. Method for tenderizing raw beef. 2003. US Patent 6,537, 598 B1
    • Teran, J.F.1
  • 169
    • 84987368845 scopus 로고
    • Ginger rhizome: A new source of proteolytic enzyme
    • Thompson, E. H., Wolf, I. D. and Allen, C. E. 1973. Ginger rhizome: A new source of proteolytic enzyme. J. Food Sci., 38: 652-655.
    • (1973) J. Food Sci. , vol.38 , pp. 652-655
    • Thompson, E.H.1    Wolf, I.D.2    Allen, C.E.3
  • 170
    • 79952815691 scopus 로고    scopus 로고
    • The effect of a kiwi fruit based solution on meat traits in beef m. semimembranous
    • Toohey, E. S., Kerr, M. J., van de Ven, R. and Hopkins, D. L. 2011. The effect of a kiwi fruit based solution on meat traits in beef m. semimembranous. Meat Sci., 88: 468-471.
    • (2011) Meat Sci. , vol.88 , pp. 468-471
    • Toohey, E.S.1    Kerr, M.J.2    van de Ven, R.3    Hopkins, D.L.4
  • 171
    • 84891475600 scopus 로고    scopus 로고
    • Composition ad method for tenderizing meat
    • US Patent 7,250,184 B2
    • Toren, J. F. 2007. Composition ad method for tenderizing meat. US Patent 7,250,184 B2
    • (2007)
    • Toren, J.F.1
  • 172
    • 0037207836 scopus 로고    scopus 로고
    • Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics
    • Torrescano, G., Sánchez-Escalante, A., Giménez, B., Roncalés, P. and Beltrán, J. A. 2003. Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics. Meat Sci., 64: 85-91.
    • (2003) Meat Sci. , vol.64 , pp. 85-91
    • Torrescano, G.1    Sánchez-Escalante, A.2    Giménez, B.3    Roncalés, P.4    Beltrán, J.A.5
  • 173
    • 84982339053 scopus 로고
    • Meat tenderization. III. Hydrolysis of actomyosin, actin and collagen by papain
    • Tsen, C. C. and Tappel, A. L. 1959. Meat tenderization. III. Hydrolysis of actomyosin, actin and collagen by papain. J. Food Sci., 24: 362-364.
    • (1959) J. Food Sci. , vol.24 , pp. 362-364
    • Tsen, C.C.1    Tappel, A.L.2
  • 174
    • 4043126640 scopus 로고    scopus 로고
    • Factors regulating lamb longissimus tenderness are affected by age at slaughter
    • Veiseth, E., Shackelford, S. D., Wheeler, T. L. and Koohmaraie, M. 2004. Factors regulating lamb longissimus tenderness are affected by age at slaughter. Meat Sci., 68: 635-640.
    • (2004) Meat Sci. , vol.68 , pp. 635-640
    • Veiseth, E.1    Shackelford, S.D.2    Wheeler, T.L.3    Koohmaraie, M.4
  • 175
    • 0036323161 scopus 로고    scopus 로고
    • The effects of pressure treatments with kiwi fruit protease on adult cattle semitendinosus muscle
    • Wada, M., Suzuki, T., Yaguti, Y. and Hasegawa, T. 2002. The effects of pressure treatments with kiwi fruit protease on adult cattle semitendinosus muscle. Food Chem., 78: 167-171.
    • (2002) Food Chem. , vol.78 , pp. 167-171
    • Wada, M.1    Suzuki, T.2    Yaguti, Y.3    Hasegawa, T.4
  • 176
    • 0020687944 scopus 로고
    • A Thiol Inhibitor Produced by Aspergillus niger
    • Walker, J. M. and Chaplin, S. C. 1983. A Thiol Inhibitor Produced by Aspergillus niger. J. Gene. Microbiol., 129: 735-738.
    • (1983) J. Gene. Microbiol. , vol.129 , pp. 735-738
    • Walker, J.M.1    Chaplin, S.C.2
  • 177
    • 0000118723 scopus 로고    scopus 로고
    • Characterization of active components in food-grade proteinase inhibitors for surimi manufacture
    • Weerasinghe, V. C., Morrissey, M. T. and An, H. 1996a. Characterization of active components in food-grade proteinase inhibitors for surimi manufacture. J. Agric. Food Chem., 44: 2584-2590.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 2584-2590
    • Weerasinghe, V.C.1    Morrissey, M.T.2    An, H.3
  • 178
    • 0001064289 scopus 로고    scopus 로고
    • Whey protein concentrate as a proteinase inhibitor in Pacific Whiting surimi
    • Weerasinghe, V. C., Morrissey, M. T. and An, H. 1996b. Whey protein concentrate as a proteinase inhibitor in Pacific Whiting surimi. J. Food Sci., 61: 367-371.
    • (1996) J. Food Sci. , vol.61 , pp. 367-371
    • Weerasinghe, V.C.1    Morrissey, M.T.2    An, H.3
  • 179
    • 84982338327 scopus 로고
    • Properties of the proteolytic enzymes of commercial ficin
    • Whitaker, J. R. 1957. Properties of the proteolytic enzymes of commercial ficin. J. Food Sci., 22: 483-493.
    • (1957) J. Food Sci. , vol.22 , pp. 483-493
    • Whitaker, J.R.1
  • 180
    • 2442610018 scopus 로고    scopus 로고
    • Structure-function relationships in class CA1 cysteine peptidase propeptides
    • Wiederanders, B. 2003. Structure-function relationships in class CA1 cysteine peptidase propeptides. Acta Biochim. Pol., 50: 691-713.
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 691-713
    • Wiederanders, B.1
  • 181
    • 44049124203 scopus 로고
    • The use of proteases from extreme Thermophiles for meat tenderisation
    • Wilson, S. A., Young, O. A., Coolbear, T. and Daniel, R. M. 1992. The use of proteases from extreme Thermophiles for meat tenderisation. Meat Sci., 32: 93-103.
    • (1992) Meat Sci. , vol.32 , pp. 93-103
    • Wilson, S.A.1    Young, O.A.2    Coolbear, T.3    Daniel, R.M.4
  • 182
    • 0017567237 scopus 로고
    • Purification and properties of a protease with elastase activity from Pseudomonas aeruginosa
    • Wretlind, B. and Wadström, T. 1977. Purification and properties of a protease with elastase activity from Pseudomonas aeruginosa. J. Gene. Microbiol., 103: 319-327.
    • (1977) J. Gene. Microbiol. , vol.103 , pp. 319-327
    • Wretlind, B.1    Wadström, T.2
  • 183
    • 0034617146 scopus 로고    scopus 로고
    • Inhibition of Papain by S-Nitrosothiols
    • Xian, M., Chen, X., Liu, Z., Wang, K. and Wang, P. G. 2000. Inhibition of Papain by S-Nitrosothiols. J. Biol. Chem., 275: 20467-20473.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20467-20473
    • Xian, M.1    Chen, X.2    Liu, Z.3    Wang, K.4    Wang, P.G.5
  • 185
    • 0010914990 scopus 로고
    • Proteolytic enzymes in green asparagus, kiwifruit and miut: Occurrence and partial characterisation
    • Yamaguchi, Y., Yamashita, Y., Takeda, I. and Kiso, H. 1982. Proteolytic enzymes in green asparagus, kiwifruit and miut: Occurrence and partial characterisation. Agric. Biol. Chem., 46: 1983-1986.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 1983-1986
    • Yamaguchi, Y.1    Yamashita, Y.2    Takeda, I.3    Kiso, H.4
  • 186
    • 0037048734 scopus 로고    scopus 로고
    • Application potency of engineered G159 mutants on P1 substrate pocket of Subtilisin YaB as improved meat tenderizers
    • Yeh, C.-M., Yang, M.-C. and Tsai, Y.-C. 2002. Application potency of engineered G159 mutants on P1 substrate pocket of Subtilisin YaB as improved meat tenderizers. J. Agric. Food Chem., 50: 6199-6204.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6199-6204
    • Yeh, C.-M.1    Yang, M.-C.2    Tsai, Y.-C.3
  • 187
    • 0033045451 scopus 로고    scopus 로고
    • Inactivation of papain by pulsed electric fields in a continuous system
    • Yeom, H. W., Zhang, Q. H. and Dunne, C. P. 1999. Inactivation of papain by pulsed electric fields in a continuous system. Food Chem., 67: 53-59.
    • (1999) Food Chem. , vol.67 , pp. 53-59
    • Yeom, H.W.1    Zhang, Q.H.2    Dunne, C.P.3
  • 188
    • 0542393202 scopus 로고    scopus 로고
    • Thermal activation of immobilized papain
    • Zhuo, R., He, F., Liu, L. and Xu, M. 1998. Thermal activation of immobilized papain. Chin. J. Polym. Sci., 16: 142-146.
    • (1998) Chin. J. Polym. Sci. , vol.16 , pp. 142-146
    • Zhuo, R.1    He, F.2    Liu, L.3    Xu, M.4


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