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Volumn 7, Issue 12, 2014, Pages 3398-3406

The Cryoprotective Effect of Different Konjac Glucomannan (KGM) Hydrolysates on the Glass Carp (Ctenopharyngodon idella) Myofibrillar During Frozen Storage

Author keywords

Cryoprotection; Glass carp myofibrilliar; KGM hydrolysates

Indexed keywords

FOOD STORAGE; HYDROPHOBICITY; PHYSICOCHEMICAL PROPERTIES;

EID: 84920256091     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-014-1345-3     Document Type: Article
Times cited : (56)

References (34)
  • 1
    • 0032993665 scopus 로고    scopus 로고
    • Highly concentrated branched oligosaccharides as cryoprotectant for surimi
    • COI: 1:CAS:528:DyaK1MXktlOrtr8%3D
    • Auh, J. H., Lee, H. G., Kim, J. W., Yoon, H. S., & Park, K. H. (1999). Highly concentrated branched oligosaccharides as cryoprotectant for surimi. Journal of Food Science, 64, 418–422.
    • (1999) Journal of Food Science , vol.64 , pp. 418-422
    • Auh, J.H.1    Lee, H.G.2    Kim, J.W.3    Yoon, H.S.4    Park, K.H.5
  • 2
    • 0034041511 scopus 로고    scopus 로고
    • Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze–thaw cycles
    • COI: 1:CAS:528:DC%2BD3cXktFSqsro%3D
    • Benjakul, S., & Bauer, F. (2000). Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze–thaw cycles. Journal of the Science of Food and Agriculture, 80, 1143–1150.
    • (2000) Journal of the Science of Food and Agriculture , vol.80 , pp. 1143-1150
    • Benjakul, S.1    Bauer, F.2
  • 3
    • 0031462866 scopus 로고    scopus 로고
    • Physicochemical changes in Pacific whiting muscle proteins during iced storage
    • COI: 1:CAS:528:DyaK2sXlvFegtbw%3D
    • Benjakul, S., Seymour, T. S., Morrissey, M. T., & An, H. (1997). Physicochemical changes in Pacific whiting muscle proteins during iced storage. Journal of Food Science, 62, 729–733.
    • (1997) Journal of Food Science , vol.62 , pp. 729-733
    • Benjakul, S.1    Seymour, T.S.2    Morrissey, M.T.3    An, H.4
  • 4
    • 0035730743 scopus 로고    scopus 로고
    • Gel properties of bigeye snapper (Priacanthus tayenus) surimi as affected by setting and porcine plasma proteins
    • COI: 1:CAS:528:DC%2BD38XlsVegsQ%3D%3D
    • Benjakul, S., Visessanguan, W., & Srivilai, C. (2001). Gel properties of bigeye snapper (Priacanthus tayenus) surimi as affected by setting and porcine plasma proteins. Journal of Food Quality, 24, 453–471.
    • (2001) Journal of Food Quality , vol.24 , pp. 453-471
    • Benjakul, S.1    Visessanguan, W.2    Srivilai, C.3
  • 5
    • 73249123263 scopus 로고    scopus 로고
    • Effect of several cryoprotectants on the physicochemical and rheological properties of suwari gels from frozen squid surimi made by two methods
    • Campo-Dea, L., Tovar, C. A., & Borderías, J. (2010). Effect of several cryoprotectants on the physicochemical and rheological properties of suwari gels from frozen squid surimi made by two methods. Journal of Food Engineering, 97, 457–464.
    • (2010) Journal of Food Engineering , vol.97 , pp. 457-464
    • Campo-Dea, L.1    Tovar, C.A.2    Borderías, J.3
  • 6
    • 67349123669 scopus 로고    scopus 로고
    • Rheological study of giant squid surimi (Dosidicus gigas) made by two methods with different cryoprotectants added
    • Campo-Deaño, L., Tovar, C. A., Pombo, M. J., Solas, M. T., & Borderías, A. J. (2009). Rheological study of giant squid surimi (Dosidicus gigas) made by two methods with different cryoprotectants added. Journal of Food Engineering, 94, 26–33.
    • (2009) Journal of Food Engineering , vol.94 , pp. 26-33
    • Campo-Deaño, L.1    Tovar, C.A.2    Pombo, M.J.3    Solas, M.T.4    Borderías, A.J.5
  • 7
    • 75949091113 scopus 로고    scopus 로고
    • Effects of xylooligosaccharides and sugars on the functionality of porcine myofibrillar proteins during heating and frozen storage
    • COI: 1:CAS:528:DC%2BC3cXhs1Wnu7Y%3D
    • Chou, Y.-T., & Lin, K.-W. (2010). Effects of xylooligosaccharides and sugars on the functionality of porcine myofibrillar proteins during heating and frozen storage. Food Chemistry, 121, 127–131.
    • (2010) Food Chemistry , vol.121 , pp. 127-131
    • Chou, Y.-T.1    Lin, K.-W.2
  • 8
    • 0032031224 scopus 로고    scopus 로고
    • Liquid crystalline, rheological and thermal properties of konjac glucomannan
    • COI: 1:CAS:528:DyaK1cXksFKgsA%3D%3D
    • Dave, V., Sheth, M., McCarthy, S. P., Ratto, J. A., & Kaplan, D. L. (1998). Liquid crystalline, rheological and thermal properties of konjac glucomannan. Polymer, 39, 1139–1148.
    • (1998) Polymer , vol.39 , pp. 1139-1148
    • Dave, V.1    Sheth, M.2    McCarthy, S.P.3    Ratto, J.A.4    Kaplan, D.L.5
  • 10
    • 0034838531 scopus 로고    scopus 로고
    • Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength
    • Feng, Y., & Hultin, H. O. (2001). Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength. Journal of Agricultural and Food Chemistry, 49, 3921–3935.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 3921-3935
    • Feng, Y.1    Hultin, H.O.2
  • 11
    • 85081462019 scopus 로고
    • Biological macromolecule and water
    • Tokyo: Koseisha Koseikaku
    • Hanafusa, N. (1973). Biological macromolecule and water. In: Japanese Society of Fisheries Science. (Ed.) Foods and water (pp. 9e24). Tokyo: Koseisha Koseikaku.
    • (1973) Foods and water (pp. 9e24)
    • Hanafusa, N.1
  • 12
    • 0142106343 scopus 로고    scopus 로고
    • Cryoprotection of frozen-stored actomyosin of farmed rainbow trout (Oncorhynchus mykiss) by some sugars and polyols
    • COI: 1:CAS:528:DC%2BD3sXot1Srsrk%3D
    • Herrera, J. R., & Mackie, I. M. (2004). Cryoprotection of frozen-stored actomyosin of farmed rainbow trout (Oncorhynchus mykiss) by some sugars and polyols. Food Chemistry, 84, 91–97.
    • (2004) Food Chemistry , vol.84 , pp. 91-97
    • Herrera, J.R.1    Mackie, I.M.2
  • 13
    • 77955718344 scopus 로고    scopus 로고
    • Use of konjac glucomannan as additive to reinforce the gels from low-quality squid surimi
    • COI: 1:CAS:528:DC%2BC3cXhtVeksr7P
    • Iglesias-Otero, M. A., Borderías, J., & Tovar, C. A. (2010). Use of konjac glucomannan as additive to reinforce the gels from low-quality squid surimi. Journal of Food Engineering, 101, 281–288.
    • (2010) Journal of Food Engineering , vol.101 , pp. 281-288
    • Iglesias-Otero, M.A.1    Borderías, J.2    Tovar, C.A.3
  • 14
    • 84869890105 scopus 로고    scopus 로고
    • Study on preparation and separation of konjac oligosaccharides
    • COI: 1:CAS:528:DC%2BC3sXisVShu7c%3D
    • Jian, W., Sun, Y., Huanga, H., Yang, Y., Peng, S., Xiong, B., et al. (2013). Study on preparation and separation of konjac oligosaccharides. Carbohydrate Polymers, 92, 1218–1224.
    • (2013) Carbohydrate Polymers , vol.92 , pp. 1218-1224
    • Jian, W.1    Sun, Y.2    Huanga, H.3    Yang, Y.4    Peng, S.5    Xiong, B.6
  • 15
    • 0000616237 scopus 로고
    • Effect of storage temperature on the formation of disulfide and denaturation on milkfish actomyosin (Chanos chanos)
    • COI: 1:CAS:528:DyaL1cXmtV2ktLY%3D
    • Jiang, S. T., Hwang, D. C., & Chen, C. S. (1988). Effect of storage temperature on the formation of disulfide and denaturation on milkfish actomyosin (Chanos chanos). Journal of Food Science, 53, 1333–1335.
    • (1988) Journal of Food Science , vol.53 , pp. 1333-1335
    • Jiang, S.T.1    Hwang, D.C.2    Chen, C.S.3
  • 16
    • 84961006038 scopus 로고
    • The relationship between sulfhydryl groups and the activation of myosin adenosinetriphosphatase
    • COI: 1:CAS:528:DyaG28Xjs1Cgtg%3D%3D
    • Kielley, W. W., & Bradley, L. B. (1956). The relationship between sulfhydryl groups and the activation of myosin adenosinetriphosphatase. The Journal of Biological Chemistry, 218, 653–659.
    • (1956) The Journal of Biological Chemistry , vol.218 , pp. 653-659
    • Kielley, W.W.1    Bradley, L.B.2
  • 17
    • 28444457445 scopus 로고    scopus 로고
    • Single molecular chain geometry of konjac glucomannan as a high quality dietary fiber in East Asia
    • COI: 1:CAS:528:DC%2BD2MXht1OntLjL
    • Li, B., & Xie, B. J. (2006). Single molecular chain geometry of konjac glucomannan as a high quality dietary fiber in East Asia. Food Research International, 39, 127–132.
    • (2006) Food Research International , vol.39 , pp. 127-132
    • Li, B.1    Xie, B.J.2
  • 18
    • 33646873277 scopus 로고    scopus 로고
    • Studies on the molecular morphology of konjac glucomannan
    • COI: 1:CAS:528:DC%2BD28Xlt12mu78%3D
    • Li, B., Xie, B. J., & Kennedy, J. K. (2006). Studies on the molecular morphology of konjac glucomannan. Carbohydrate Polymers, 64, 510–515.
    • (2006) Carbohydrate Polymers , vol.64 , pp. 510-515
    • Li, B.1    Xie, B.J.2    Kennedy, J.K.3
  • 19
    • 84867813061 scopus 로고    scopus 로고
    • Optimization of adding konjac glucomannan to improve gel properties of low-quality surimi
    • COI: 1:CAS:528:DC%2BC38Xhsl2ltbfE
    • Liu, J., Wang, X., & Ding, Y. (2013). Optimization of adding konjac glucomannan to improve gel properties of low-quality surimi. Carbohydrate Polymers, 92, 484–489.
    • (2013) Carbohydrate Polymers , vol.92 , pp. 484-489
    • Liu, J.1    Wang, X.2    Ding, Y.3
  • 20
    • 84873727937 scopus 로고    scopus 로고
    • Effects of fish protein hydrolysate and freeze–thaw treatment on physicochemical and gel properties of natural actomyosin from Pacific cod
    • Malgorzata, K., Imelda, W. Y. C., & Li-Chan, E. C. Y. (2013). Effects of fish protein hydrolysate and freeze–thaw treatment on physicochemical and gel properties of natural actomyosin from Pacific cod. Food Chemistry, 138, 1967–1975.
    • (2013) Food Chemistry , vol.138 , pp. 1967-1975
    • Malgorzata, K.1    Imelda, W.Y.C.2    Li-Chan, E.C.Y.3
  • 21
    • 0001115974 scopus 로고    scopus 로고
    • Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate
    • COI: 1:CAS:528:DyaK28XivVaktb4%3D
    • Mutilangi, W. A. M., Panyam, D., & Kilara, A. (1996). Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate. Journal of Food Science, 61(2), 270–275.
    • (1996) Journal of Food Science , vol.61 , Issue.2 , pp. 270-275
    • Mutilangi, W.A.M.1    Panyam, D.2    Kilara, A.3
  • 22
    • 33947553005 scopus 로고
    • The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins
    • Némethy, G., & Scheraga, H. A. (1962). The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins. Journal of Physical Chemistry, 66(10), 1773–1789.
    • (1962) Journal of Physical Chemistry , vol.66 , Issue.10 , pp. 1773-1789
    • Némethy, G.1    Scheraga, H.A.2
  • 23
    • 84987358135 scopus 로고
    • Differential insolubilization of red hake muscle proteins during frozen storage
    • COI: 1:CAS:528:DyaK38XktVKntLg%3D
    • Owusu-Ansah, Y. J., & Hultin, H. O. (1992). Differential insolubilization of red hake muscle proteins during frozen storage. Journal of Food Science, 57(2), 265–266.
    • (1992) Journal of Food Science , vol.57 , Issue.2 , pp. 265-266
    • Owusu-Ansah, Y.J.1    Hultin, H.O.2
  • 25
    • 0032766852 scopus 로고    scopus 로고
    • Cryostabilization mechanism of fish muscle proteins by maltodextrins
    • Patricio, A. C., Grant, A. M., & Tyre, C. L. (1999). Cryostabilization mechanism of fish muscle proteins by maltodextrins. Cryobiology, 38, 16–26.
    • (1999) Cryobiology , vol.38 , pp. 16-26
    • Patricio, A.C.1    Grant, A.M.2    Tyre, C.L.3
  • 26
    • 0017366898 scopus 로고
    • An evaluation of the Coomassie brilliant blue G-250 dye-binding method for quantitative protein determination
    • COI: 1:CAS:528:DyaE2sXkvFygsbc%3D
    • Pierce, J., & Suelter, C. H. (1977). An evaluation of the Coomassie brilliant blue G-250 dye-binding method for quantitative protein determination. Analytical Biochemistry, 81, 478–480.
    • (1977) Analytical Biochemistry , vol.81 , pp. 478-480
    • Pierce, J.1    Suelter, C.H.2
  • 27
    • 0000665651 scopus 로고
    • Protein denaturation in frozen fish
    • COI: 1:CAS:528:DyaL3MXhtVWgurw%3D
    • Shenouda, S. Y. K. (1980). Protein denaturation in frozen fish. Advances in Food Research, 26, 275–311.
    • (1980) Advances in Food Research , vol.26 , pp. 275-311
    • Shenouda, S.Y.K.1
  • 28
    • 0032447830 scopus 로고    scopus 로고
    • Cryoprotective effects of sugar and polyol blends in ling cod surimi during frozen storage
    • Sultanbawa, Y., & Li-Chan, E. C. Y. (1998). Cryoprotective effects of sugar and polyol blends in ling cod surimi during frozen storage. Food Research International, 31, 87–98.
    • (1998) Food Research International , vol.31 , pp. 87-98
    • Sultanbawa, Y.1    Li-Chan, E.C.Y.2
  • 29
    • 84987280162 scopus 로고
    • Cryoprotective effects of some materials on cod-surimi proteins during frozen storage
    • Sych, J., Lacriox, C., Asambounou, L. T., & Castaigne, F. (1990). Cryoprotective effects of some materials on cod-surimi proteins during frozen storage. Journal of Food Science, 55, 1222–1227.
    • (1990) Journal of Food Science , vol.55 , pp. 1222-1227
    • Sych, J.1    Lacriox, C.2    Asambounou, L.T.3    Castaigne, F.4
  • 30
    • 0038503369 scopus 로고    scopus 로고
    • Konjac mannan
    • Philips GO, Williams PA, (eds), Woodhead, Cambridge:
    • Takigami, S. (2000). Konjac mannan. In G. O. Philips & P. A. Williams (Eds.), Handbook of hydrocolloids (pp. 413–424). Cambridge: Woodhead.
    • (2000) Handbook of hydrocolloids , pp. 413-424
    • Takigami, S.1
  • 32
    • 67349126511 scopus 로고    scopus 로고
    • Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella)
    • Xiong, G., Cheng, W., Ye, L., Du, X., Zhou, M., Lin, R., et al. (2009). Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella). Food Chemistry, 16, 413–418.
    • (2009) Food Chemistry , vol.16 , pp. 413-418
    • Xiong, G.1    Cheng, W.2    Ye, L.3    Du, X.4    Zhou, M.5    Lin, R.6
  • 33
    • 34548664605 scopus 로고    scopus 로고
    • Effect of c-irradiation on some physiochemical properties of konjac glucomannan
    • COI: 1:CAS:528:DC%2BD2sXhtVOmu7rJ
    • Xu, Z., Sun, Y., Yang, Y., Ding, J., & Pang, J. (2007). Effect of c-irradiation on some physiochemical properties of konjac glucomannan. Carbohydrate Polymers, 70, 444–450.
    • (2007) Carbohydrate Polymers , vol.70 , pp. 444-450
    • Xu, Z.1    Sun, Y.2    Yang, Y.3    Ding, J.4    Pang, J.5
  • 34
    • 27144481364 scopus 로고    scopus 로고
    • Cryoprotective effects of trehalose and sodium lactate on tilapia (Sarotherodon nilotica) surimi during frozen storage
    • COI: 1:CAS:528:DC%2BD2MXhtFGht7zE
    • Zhou, A., Benjakul, S., Pan, K., Gong, J., & Liu, X. (2006). Cryoprotective effects of trehalose and sodium lactate on tilapia (Sarotherodon nilotica) surimi during frozen storage. Food Chemistry, 96, 96–103.
    • (2006) Food Chemistry , vol.96 , pp. 96-103
    • Zhou, A.1    Benjakul, S.2    Pan, K.3    Gong, J.4    Liu, X.5


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