메뉴 건너뛰기




Volumn 77, Issue 10, 2012, Pages

Trypsin Inhibitory Activity and Gel-Enhancing Effect of Sarcoplasmic Proteins from Common Carp

Author keywords

Fish protein; Inhibitor; Proteinase; Sarcoplamic proteins; Surimi

Indexed keywords

FISH PROTEIN; MYOSIN HEAVY CHAIN; TRYPSIN INHIBITOR;

EID: 84867645443     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2012.02919.x     Document Type: Article
Times cited : (10)

References (34)
  • 2
    • 0022988828 scopus 로고
    • Preparation of unheated soy protein isolates with low trypsin inhibitor content
    • Baker EC, Rackis JJ. 1986. Preparation of unheated soy protein isolates with low trypsin inhibitor content. Adv Exp Med Biol 199:349-55.
    • (1986) Adv Exp Med Biol , vol.199 , pp. 349-355
    • Baker, E.C.1    Rackis, J.J.2
  • 3
    • 77955928577 scopus 로고    scopus 로고
    • Combination effects of whey protein concentrate and calcium chloride on the properties of goatfish surimi gel
    • Benjakul S, Yarnpakdee S, Visessanguan W, Phatcharat S. 2010. Combination effects of whey protein concentrate and calcium chloride on the properties of goatfish surimi gel. J Texture Stud 41:341-57.
    • (2010) J Texture Stud , vol.41 , pp. 341-357
    • Benjakul, S.1    Yarnpakdee, S.2    Visessanguan, W.3    Phatcharat, S.4
  • 4
    • 0035135272 scopus 로고    scopus 로고
    • Purification of a novel myofibril- bound serine proteinase inhibitor (MBSPI) from the skeletal muscle of lizardfish
    • Cao MJ, Osatomi K, Hara K, Ishihara T. 2001. Purification of a novel myofibril- bound serine proteinase inhibitor (MBSPI) from the skeletal muscle of lizardfish. Comp Biochem Physiol Part B 128:19-25.
    • (2001) Comp Biochem Physiol Part B , vol.128 , pp. 19-25
    • Cao, M.J.1    Osatomi, K.2    Hara, K.3    Ishihara, T.4
  • 5
    • 0032697835 scopus 로고    scopus 로고
    • Purification and characterization of proteinase from Atlantic menhaden muscle
    • Choi YJ, Cho YJ, Lanier TC. 1999. Purification and characterization of proteinase from Atlantic menhaden muscle. J Food Sci 64:772-5.
    • (1999) J Food Sci , vol.64 , pp. 772-775
    • Choi, Y.J.1    Cho, Y.J.2    Lanier, T.C.3
  • 6
    • 0036929819 scopus 로고    scopus 로고
    • Purification and characterization of a trypsin inhibitor from the egg of skipjack tuna Katsuwonus pelamis
    • Choi JH, Park PJ, Kim SW. 2002. Purification and characterization of a trypsin inhibitor from the egg of skipjack tuna Katsuwonus pelamis. Fisheries Sci 68:1367-73.
    • (2002) Fisheries Sci , vol.68 , pp. 1367-1373
    • Choi, J.H.1    Park, P.J.2    Kim, S.W.3
  • 7
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular mass of proteinases or proteinaceous proteinase inhibitor
    • Garcia-Carreno FL, Dimes LE, Haard NF. 1993. Substrate-gel electrophoresis for composition and molecular mass of proteinases or proteinaceous proteinase inhibitor. Anal Biochem 214:65-9.
    • (1993) Anal Biochem , vol.214 , pp. 65-69
    • Garcia-Carreno, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 9
    • 0001592750 scopus 로고    scopus 로고
    • Heat-induced interaction and gelation of mixtures of β-lactoglobulin and α-lactalbumin
    • Gezimati J, Creamer LK, Singh H. 1997. Heat-induced interaction and gelation of mixtures of β-lactoglobulin and α-lactalbumin. J Agric Food Chem 45:1130-6.
    • (1997) J Agric Food Chem , vol.45 , pp. 1130-1136
    • Gezimati, J.1    Creamer, L.K.2    Singh, H.3
  • 10
    • 27544442211 scopus 로고    scopus 로고
    • 2+ affects physicochemical and conformational changes of threadfin bream myosin and actin in a setting model
    • 2+ affects physicochemical and conformational changes of threadfin bream myosin and actin in a setting model. J Food Sci 70:C455-C60.
    • (2005) J Food Sci , vol.70
    • Hemung, B.1    Yongsawatdigul, J.2
  • 11
    • 41149114043 scopus 로고    scopus 로고
    • Partial purification and characterization of transglutaminase from threadfin bream (Nemipterus sp.) liver
    • Hemung B, Yongsawatdigul J. 2008. Partial purification and characterization of transglutaminase from threadfin bream (Nemipterus sp.) liver. J Food Biochem 32:182-200.
    • (2008) J Food Biochem , vol.32 , pp. 182-200
    • Hemung, B.1    Yongsawatdigul, J.2
  • 12
    • 58649093481 scopus 로고    scopus 로고
    • Characteristics of sarcoplasmic proteins and their interaction with surimi and kamaboko gel
    • Jafarpour A, Gorczyca EM. 2009. Characteristics of sarcoplasmic proteins and their interaction with surimi and kamaboko gel. J Food Sci 74:N16-N22.
    • (2009) J Food Sci , vol.74
    • Jafarpour, A.1    Gorczyca, E.M.2
  • 13
    • 84857131201 scopus 로고    scopus 로고
    • Contribution of sarcoplasmic proteins to myofibrillar proteins gelation
    • Jafarpour A, Gorczyca EM. 2012. Contribution of sarcoplasmic proteins to myofibrillar proteins gelation. J Food Sci 74:R73-R81.
    • (2012) J Food Sci , vol.74
    • Jafarpour, A.1    Gorczyca, E.M.2
  • 14
    • 34147153407 scopus 로고    scopus 로고
    • Effect of heat treatment on hen's egg ovomucoid: an immunochemical and calorimetric study
    • Julia S, Sanchez L, Perez MD, Lavilla M, Conesa C, Calvo M. 2007. Effect of heat treatment on hen's egg ovomucoid: an immunochemical and calorimetric study. Food Res Intl 40:603-12.
    • (2007) Food Res Intl , vol.40 , pp. 603-612
    • Julia, S.1    Sanchez, L.2    Perez, M.D.3    Lavilla, M.4    Conesa, C.5    Calvo, M.6
  • 15
    • 34347219370 scopus 로고    scopus 로고
    • Characteristics of the protease inhibitor purified from chum salmon (Oncorhynchus keta) eggs
    • Kim KY, Ustadi, Kim SM. 2006. Characteristics of the protease inhibitor purified from chum salmon (Oncorhynchus keta) eggs. Food Sci Biotechnol 15:28-32.
    • (2006) Food Sci Biotechnol , vol.15 , pp. 28-32
    • Kim, K.Y.1    Ustadi2    Kim, S.M.3
  • 16
    • 0025349506 scopus 로고
    • Purification and properties of a novel latent protein showing myosin heavy chain degrading activity from threadfin bream muscle
    • Kinoshita M, Toyohara H, Shimizu Y. 1990. Purification and properties of a novel latent protein showing myosin heavy chain degrading activity from threadfin bream muscle. J Biochem 107:587-91.
    • (1990) J Biochem , vol.107 , pp. 587-591
    • Kinoshita, M.1    Toyohara, H.2    Shimizu, Y.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Park JW, editor. Boca Raton, Fla.: CRC Press Taylor and Francis Group.
    • Lanier TC, Carvajal P, Yongsawatdigul J. 2005. Surimi gelation chemistry. Park JW, editor. Surimi and Surimi seafood. Boca Raton, Fla.: CRC Press Taylor and Francis Group. p 435-89.
    • (2005) Surimi and Surimi seafood , pp. 435-489
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 19
    • 38549113922 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine protease inhibitor from chum salmon (Oncorhynchus keta) plasma
    • Li DK, Lin H, Kim SM. 2008. Purification and characterization of a cysteine protease inhibitor from chum salmon (Oncorhynchus keta) plasma. J Agric Food Chem 56:106-11.
    • (2008) J Agric Food Chem , vol.56 , pp. 106-111
    • Li, D.K.1    Lin, H.2    Kim, S.M.3
  • 21
    • 0026095017 scopus 로고
    • Detection of a trypsin-like serine protease and its endogenous inhibitor in hake skeletal muscle
    • Martone CB, Busconi L, Folco EJ, Sanchez JJ. 1991. Detection of a trypsin-like serine protease and its endogenous inhibitor in hake skeletal muscle. Arch Biochem Biophys 289:1-5.
    • (1991) Arch Biochem Biophys , vol.289 , pp. 1-5
    • Martone, C.B.1    Busconi, L.2    Folco, E.J.3    Sanchez, J.J.4
  • 22
    • 21344479819 scopus 로고
    • Relationship between the heat-gelling property and composition of fish sarcoplasmic proteins
    • Morioka K, Shimizu Y. 1993. Relationship between the heat-gelling property and composition of fish sarcoplasmic proteins. Nippon Suisan Gakk 59:1631.
    • (1993) Nippon Suisan Gakk , vol.59 , pp. 1631
    • Morioka, K.1    Shimizu, Y.2
  • 23
    • 2942511949 scopus 로고    scopus 로고
    • Purification and properties of proteinaceous trypsin inhibitors in the skin mucus of pufferfish Takifugu pardalis
    • Nagashima Y, Takeda M, Ohta I, Shimakura K, Shiomi K. 2004. Purification and properties of proteinaceous trypsin inhibitors in the skin mucus of pufferfish Takifugu pardalis. Comp Biochem Physiol Part B 138:103-10.
    • (2004) Comp Biochem Physiol Part B , vol.138 , pp. 103-110
    • Nagashima, Y.1    Takeda, M.2    Ohta, I.3    Shimakura, K.4    Shiomi, K.5
  • 24
    • 20444386925 scopus 로고    scopus 로고
    • A novel type of myofibril-bound serine protease from white croaker (Argyrosomus argentatus)
    • Ohkubo M, Osatomi K, Hara K, Ishihara T, Aranishi F. 2005. A novel type of myofibril-bound serine protease from white croaker (Argyrosomus argentatus). Comp Biochem Physiol Part B 141:231-6.
    • (2005) Comp Biochem Physiol Part B , vol.141 , pp. 231-236
    • Ohkubo, M.1    Osatomi, K.2    Hara, K.3    Ishihara, T.4    Aranishi, F.5
  • 25
    • 33947601680 scopus 로고    scopus 로고
    • Ingredient technology for surimi and surimi seafood
    • Park JW, editor. Boca Raton, Fla.: CRC Press Taylor and Francis Group.
    • Park JW 2005. Ingredient technology for surimi and surimi seafood. Park JW, editor. Surimi and Surimi seafood. Boca Raton, Fla.: CRC Press Taylor and Francis Group. p 649-707.
    • (2005) Surimi and Surimi seafood , pp. 649-707
    • Park, J.W.1
  • 26
    • 70849100044 scopus 로고    scopus 로고
    • Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.)
    • Piyadhammaviboon P, Yongsawatdigul J. 2010. Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.). J Sci Food Agric 90:291-8.
    • (2010) J Sci Food Agric , vol.90 , pp. 291-298
    • Piyadhammaviboon, P.1    Yongsawatdigul, J.2
  • 27
    • 85008299974 scopus 로고
    • Relation between the Modori phenomenon and myosin heavy chain breakdown in threadfin-bream gel
    • Toyohara H, Shimizu Y. 1988. Relation between the Modori phenomenon and myosin heavy chain breakdown in threadfin-bream gel. Agric Biol Chem 52:255-7.
    • (1988) Agric Biol Chem , vol.52 , pp. 255-257
    • Toyohara, H.1    Shimizu, Y.2
  • 28
    • 27144551320 scopus 로고    scopus 로고
    • Purification and identification of a protease inhibitor from glassfish (Liparis tanakai) eggs
    • Ustadi U, Kim KY, Kim SM. 2005. Purification and identification of a protease inhibitor from glassfish (Liparis tanakai) eggs. J Agric Food Chem 53:7667-72.
    • (2005) J Agric Food Chem , vol.53 , pp. 7667-7672
    • Ustadi, U.1    Kim, K.Y.2    Kim, S.M.3
  • 29
    • 0001064289 scopus 로고    scopus 로고
    • Whey protein concentrate as a proteinase inhibitor in Pacific whiting surimi
    • Weerasinghe VC, Morrissey MT, Chung YC, An H. 1996. Whey protein concentrate as a proteinase inhibitor in Pacific whiting surimi. J Food Sci 61:367-71.
    • (1996) J Food Sci , vol.61 , pp. 367-371
    • Weerasinghe, V.C.1    Morrissey, M.T.2    Chung, Y.C.3    An, H.4
  • 30
    • 20444424985 scopus 로고    scopus 로고
    • Purification and characterization of transglutaminase from tropical tilapia (Oreochromis niloticus)
    • Worratao A, Yongsawatdigul J. 2005. Purification and characterization of transglutaminase from tropical tilapia (Oreochromis niloticus). Food Chem 93:651-8.
    • (2005) Food Chem , vol.93 , pp. 651-658
    • Worratao, A.1    Yongsawatdigul, J.2
  • 31
    • 0033572814 scopus 로고    scopus 로고
    • Atlantic salmon (Salmo salar L.) skin contains a novel kininogen and another cysteine proteinase inhibitor
    • Ylonen A, Rinne A, Herttuainen J, Bogwald J, Jarvinen M, Kalkkinen N. 1999. Atlantic salmon (Salmo salar L.) skin contains a novel kininogen and another cysteine proteinase inhibitor. Eur J Biochem 266:1066-72.
    • (1999) Eur J Biochem , vol.266 , pp. 1066-1072
    • Ylonen, A.1    Rinne, A.2    Herttuainen, J.3    Bogwald, J.4    Jarvinen, M.5    Kalkkinen, N.6
  • 32
    • 2442562651 scopus 로고    scopus 로고
    • Inhibition of autolytic activity of lizardfish surimi by proteinase inhibitors
    • Yongswatdigul J, Piyadhammaviboon P. 2004. Inhibition of autolytic activity of lizardfish surimi by proteinase inhibitors. Food Chem 87:447-55.
    • (2004) Food Chem , vol.87 , pp. 447-455
    • Yongswatdigul, J.1    Piyadhammaviboon, P.2
  • 33
    • 36749076421 scopus 로고    scopus 로고
    • Gel enhancing effect and protein cross-linking ability of tilapia sarcoplasmic proteins
    • Yongsawatdigul J, Piyadhammaviboon P. 2007. Gel enhancing effect and protein cross-linking ability of tilapia sarcoplasmic proteins. J Sci Food Agric 87:2810-6.
    • (2007) J Sci Food Agric , vol.87 , pp. 2810-2816
    • Yongsawatdigul, J.1    Piyadhammaviboon, P.2
  • 34
    • 0036868154 scopus 로고    scopus 로고
    • Effect of endogenous transglutaminase on threadfin bream surimi gelation
    • Yongsawatdigul J, Worratao A, Park JW. 2002. Effect of endogenous transglutaminase on threadfin bream surimi gelation. J Food Sci 67:3258-63.
    • (2002) J Food Sci , vol.67 , pp. 3258-3263
    • Yongsawatdigul, J.1    Worratao, A.2    Park, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.