메뉴 건너뛰기




Volumn 89, Issue 9, 2009, Pages 1607-1614

Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue

Author keywords

Actinidin; Atomic force microscope; Collagen solubility; Desmin; Pork; Tenderness

Indexed keywords

ACTINIDIA DELICIOSA; SUS;

EID: 68949091769     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3633     Document Type: Article
Times cited : (52)

References (32)
  • 2
    • 0026096833 scopus 로고
    • Specific degradation of myosin in meat by bromelain
    • Kim H-J and Taub IA, Specific degradation of myosin in meat by bromelain. Food Chem 40:337-343 (1991).
    • (1991) Food Chem , vol.40 , pp. 337-343
    • Kim, H.-J.1    Taub, I.A.2
  • 3
    • 0034373990 scopus 로고    scopus 로고
    • Meat tenderization by proteolytic enzymes after osmotic dehydration
    • Gerelt B, Ikeuchi Y and Suzuki A, Meat tenderization by proteolytic enzymes after osmotic dehydration. Meat Sci 56:311-318 (2000).
    • (2000) Meat Sci , vol.56 , pp. 311-318
    • Gerelt, B.1    Ikeuchi, Y.2    Suzuki, A.3
  • 4
    • 0036689388 scopus 로고    scopus 로고
    • Effects of papain and a microbial enzyme on meat proteins and beef tenderness
    • Ashie INA, Sorensen TL and Nielsen PM, Effects of papain and a microbial enzyme on meat proteins and beef tenderness. J Food Sci 67:2138-2142 (2002).
    • (2002) J Food Sci , vol.67 , pp. 2138-2142
    • Ashie, I.N.A.1    Sorensen, T.L.2    Nielsen, P.M.3
  • 5
    • 0014807078 scopus 로고
    • Anionic proteinase from Actinidia chinensis
    • McDowall MA, Anionic proteinase from Actinidia chinensis. Eur J Biochem 14:214-221 (1970).
    • (1970) Eur J Biochem , vol.14 , pp. 214-221
    • McDowall, M.A.1
  • 6
    • 0022429212 scopus 로고
    • Thiol proteases: Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H and stem Bromelain
    • Kamphuis IG, Drenth J and Baker EN, Thiol proteases: comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H and stem Bromelain. J Mol Biol 182:317-329 (1985).
    • (1985) J Mol Biol , vol.182 , pp. 317-329
    • Kamphuis, I.G.1    Drenth, J.2    Baker, E.N.3
  • 7
    • 84986516462 scopus 로고
    • Application of actinidin from kiwifruit to meat tenderization and characterization of beef muscle protein hydrolysis
    • Lewis DA and Luh BS, Application of actinidin from kiwifruit to meat tenderization and characterization of beef muscle protein hydrolysis. J Food Biochem 12:147-158 (1988).
    • (1988) J Food Biochem , vol.12 , pp. 147-158
    • Lewis, D.A.1    Luh, B.S.2
  • 8
    • 2342631166 scopus 로고    scopus 로고
    • The solubilization of unheated cattle Achilles tendon with actinidin under neutral and acidic conditions
    • Wada M, Hosaka M, Nakazawa R, Kobayashi Y and Hasegawa T, The solubilization of unheated cattle Achilles tendon with actinidin under neutral and acidic conditions. Food Sci Technol Res 10:35-37 (2004).
    • (2004) Food Sci Technol Res , vol.10 , pp. 35-37
    • Wada, M.1    Hosaka, M.2    Nakazawa, R.3    Kobayashi, Y.4    Hasegawa, T.5
  • 13
    • 0347622365 scopus 로고    scopus 로고
    • Effect of muscle type on the rate of post-mortem proteolysis in pigs
    • Christensen M, Henckel P and Purslow PP, Effect of muscle type on the rate of post-mortem proteolysis in pigs. Meat Sci 66:595-601 (2004).
    • (2004) Meat Sci , vol.66 , pp. 595-601
    • Christensen, M.1    Henckel, P.2    Purslow, P.P.3
  • 14
    • 33646513293 scopus 로고    scopus 로고
    • Mechanical properties of type I and type IIB single porcine muscle fibres
    • Christensen M, Kok C and Ertbjerg P, Mechanical properties of type I and type IIB single porcine muscle fibres. Meat Sci 73:422-425 (2006).
    • (2006) Meat Sci , vol.73 , pp. 422-425
    • Christensen, M.1    Kok, C.2    Ertbjerg, P.3
  • 15
    • 0036834247 scopus 로고    scopus 로고
    • Dietary-induced changes of muscle growth rate in pigs: Effects on in vivo and post-mortem muscle proteolysis and meat quality
    • Kristensen L, Therkildsen M, Riis B, Sørensen MT, Oksbjerg N, Purslow PP, et al, Dietary-induced changes of muscle growth rate in pigs: effects on in vivo and post-mortem muscle proteolysis and meat quality. J Anim Sci 80:2862-2871 (2002).
    • (2002) J Anim Sci , vol.80 , pp. 2862-2871
    • Kristensen, L.1    Therkildsen, M.2    Riis, B.3    Sørensen, M.T.4    Oksbjerg, N.5    Purslow, P.P.6
  • 16
    • 0025078028 scopus 로고
    • Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat products: NMKL collaborative study
    • Kolar K, Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat products: NMKL collaborative study. J Assoc Off Anal Chem 73:54-57 (1990).
    • (1990) J Assoc Off Anal Chem , vol.73 , pp. 54-57
    • Kolar, K.1
  • 17
    • 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, The effects of pressure treatments with kiwi fruit protease on adult cattle semitendinosus muscle. Food Chem 78:167-171 (2002).
    • (2002) Food Chem , vol.78 , pp. 167-171
    • Wada, M.1    Suzuki, T.2    Yaguti, Y.3    Hasegawa, T.4
  • 18
    • 0032917629 scopus 로고    scopus 로고
    • Relationship between proteolytic changes and tenderness in prerigor lactic acid marinated beef
    • Ertbjerg P, Mielche MM, Larsen LM and Møller AJ, Relationship between proteolytic changes and tenderness in prerigor lactic acid marinated beef. J Sci Food Agric 79:970-978 (1999).
    • (1999) J Sci Food Agric , vol.79 , pp. 970-978
    • Ertbjerg, P.1    Mielche, M.M.2    Larsen, L.M.3    Møller, A.J.4
  • 19
    • 0035606987 scopus 로고    scopus 로고
    • Tenderization of beef by lactic acid injected at different times post mortem
    • Berge P, Ertbjerg P, Larsen LM, Astruc T, Vignon X and Møller AJ, Tenderization of beef by lactic acid injected at different times post mortem. Meat Sci 57:347-357 (2001).
    • (2001) Meat Sci , vol.57 , pp. 347-357
    • Berge, P.1    Ertbjerg, P.2    Larsen, L.M.3    Astruc, T.4    Vignon, X.5    Møller, A.J.6
  • 20
    • 0000505192 scopus 로고
    • Analysis of Warner-Bratzler shear pattern with regard to myofibrillar and connective tissue components of tenderness
    • Møller AJ, Analysis of Warner-Bratzler shear pattern with regard to myofibrillar and connective tissue components of tenderness. Meat Sci 5:247-260 (1981).
    • (1981) Meat Sci , vol.5 , pp. 247-260
    • Møller, A.J.1
  • 21
    • 0029958160 scopus 로고    scopus 로고
    • Influence of temperature, fibre diameter and conditioning on the mechanical properties of single muscle fibres extended to fracture
    • Mutungi G, Purslow P and Warkup C, Influence of temperature, fibre diameter and conditioning on the mechanical properties of single muscle fibres extended to fracture. J Sci Food Agric 72:359-366 (1996).
    • (1996) J Sci Food Agric , vol.72 , pp. 359-366
    • Mutungi, G.1    Purslow, P.2    Warkup, C.3
  • 22
    • 0034375314 scopus 로고    scopus 로고
    • The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue
    • Christensen M, Purslow PP and Larsen LM, The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue. Meat Sci 55:301-307(2000).
    • (2000) Meat Sci , vol.55 , pp. 301-307
    • Christensen, M.1    Purslow, P.P.2    Larsen, L.M.3
  • 23
    • 0026539218 scopus 로고
    • Proteolytic and physicochemical mechanisms involved in meat texture development
    • Ouali A, Proteolytic and physicochemical mechanisms involved in meat texture development. Biochemistry 74:251-265 (1992).
    • (1992) Biochemistry , vol.74 , pp. 251-265
    • Ouali, A.1
  • 24
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in post-mortem bovine muscle
    • Huff-Lonergan E, Mitsuhahi T, Beekman DD, Parrish FC Jr, Olson DG and Robson RM, Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in post-mortem bovine muscle. J Anim Sci 74:993-1008 (1996).
    • (1996) J Anim Sci , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhahi, T.2    Beekman, D.D.3    Parrish Jr., F.C.4    Olson, D.G.5    Robson, R.M.6
  • 25
    • 84985057777 scopus 로고
    • Myofibril fragmentation and shear resistance of three bovine muscles during post-mortem storage
    • Olson DG, Parrish FC Jr and Stromer MH, Myofibril fragmentation and shear resistance of three bovine muscles during post-mortem storage. J Food Sci 41:1036-1041 (1976).
    • (1976) J Food Sci , vol.41 , pp. 1036-1041
    • Olson, D.G.1    Parrish Jr., F.C.2    Stromer, M.H.3
  • 26
    • 0036899914 scopus 로고    scopus 로고
    • Compensatory growth response in pigs, muscle protein turn-over and meat texture: Effects of restriction an/realimentation period
    • Therkildsen M, Riis B, Karlsson A, Kristensen L, Ertbjerg P, Purslow PP, et al, Compensatory growth response in pigs, muscle protein turn-over and meat texture: effects of restriction an/realimentation period. Anim Sci 75:367-377 (2002).
    • (2002) Anim Sci , vol.75 , pp. 367-377
    • Therkildsen, M.1    Riis, B.2    Karlsson, A.3    Kristensen, L.4    Ertbjerg, P.5    Purslow, P.P.6
  • 27
    • 22944451801 scopus 로고    scopus 로고
    • Effects of thawing temperature on the physicochemical properties of pre-rigor frozen chicken breast and leg muscles
    • Yu LH, Lee ES, Jeong JY, Paik HD, Choi JH and Kim CJ, Effects of thawing temperature on the physicochemical properties of pre-rigor frozen chicken breast and leg muscles. Meat Sci 71:375-382 (2005).
    • (2005) Meat Sci , vol.71 , pp. 375-382
    • Yu, L.H.1    Lee, E.S.2    Jeong, J.Y.3    Paik, H.D.4    Choi, J.H.5    Kim, C.J.6
  • 28
    • 43849099823 scopus 로고    scopus 로고
    • Tenderization and fragmentation of myofibrillar proteins in bovine longissimus dorsi muscle using proteolytic extract from Sarcodon aspratus
    • Shin H-G, Choi Y-M, Kim H-K, Ryu Y-U, Lee S-H and Kim B-C, Tenderization and fragmentation of myofibrillar proteins in bovine longissimus dorsi muscle using proteolytic extract from Sarcodon aspratus. Lebensm Wissen Technol 41:1389-1395 (2008).
    • (2008) Lebensm Wissen Technol , vol.41 , pp. 1389-1395
    • Shin, H.-G.1    Choi, Y.-M.2    Kim, H.-K.3    Ryu, Y.-U.4    Lee, S.-H.5    Kim, B.-C.6
  • 29
    • 6344260556 scopus 로고    scopus 로고
    • Desmin: A major intermediate filament protein essential for the structural integrity and function of muscle
    • Paulin D and Li Z, Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Exp Cell Res 301:1-7 (2004).
    • (2004) Exp Cell Res , vol.301 , pp. 1-7
    • Paulin, D.1    Li, Z.2
  • 31
    • 55449094462 scopus 로고    scopus 로고
    • Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein
    • Bublin M, Radauer C, Knulst A, Wagner S, Scheiner O, Mackie AR, et al, Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein. Mol Nutr Food Res 52:1130-1139 (2008).
    • (2008) Mol Nutr 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.