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Volumn 10, Issue 5, 2017, Pages 866-874

Gelation Properties of Transglutaminase-Induced Soy Protein Isolate and Wheat Gluten Mixture with Ultrahigh Pressure Pretreatment

Author keywords

Gel properties; Microbial transglutaminase; Soy protein isolate; Ultrahigh pressure; Wheat gluten

Indexed keywords

AMINO ACIDS; COVALENT BONDS; CROSSLINKING; GELATION; MIXTURES; PROTEINS; SULFUR COMPOUNDS;

EID: 85009936545     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-017-1864-9     Document Type: Article
Times cited : (77)

References (34)
  • 1
    • 36348995909 scopus 로고    scopus 로고
    • Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate
    • COI: 1:CAS:528:DC%2BD2sXhtlOisL7N
    • Agyare, K. K., Xiong, Y. L., & Addo, K. (2008). Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate. Food Chemistry, 107(3), 1131–1137.
    • (2008) Food Chemistry , vol.107 , Issue.3 , pp. 1131-1137
    • Agyare, K.K.1    Xiong, Y.L.2    Addo, K.3
  • 2
    • 84948696553 scopus 로고    scopus 로고
    • Properties of annealed jackfruit (Artocarpus heterophyllus Lam.) seed starch
    • COI: 1:CAS:528:DC%2BC28XhtFelu7bK
    • Bhattacharjya, B., Dutta, H., Patwari, K., & Mahanta, C. L. (2015). Properties of annealed jackfruit (Artocarpus heterophyllus Lam.) seed starch. Acta Alimentaria, 44(4), 501–510.
    • (2015) Acta Alimentaria , vol.44 , Issue.4 , pp. 501-510
    • Bhattacharjya, B.1    Dutta, H.2    Patwari, K.3    Mahanta, C.L.4
  • 3
    • 84911007216 scopus 로고    scopus 로고
    • Effect of high pressure and/or temperature over gelation of isolated hake myofibrils
    • COI: 1:CAS:528:DC%2BC2cXhvFKltL%2FP
    • Cando, D., Moreno, H. M., Tovar, C. A., Herranz, B., & Borderias, A. J. (2014). Effect of high pressure and/or temperature over gelation of isolated hake myofibrils. Food and Bioprocess Technology, 7(11), 3197–3207.
    • (2014) Food and Bioprocess Technology , vol.7 , Issue.11 , pp. 3197-3207
    • Cando, D.1    Moreno, H.M.2    Tovar, C.A.3    Herranz, B.4    Borderias, A.J.5
  • 4
    • 84870546861 scopus 로고    scopus 로고
    • The mechanism of high pressure-induced gels of rabbit myosin
    • COI: 1:CAS:528:DC%2BC38XhvVSlsr%2FF
    • Cao, Y., Xia, T., Zhou, G., & Xu, X. (2012). The mechanism of high pressure-induced gels of rabbit myosin. Innovative Food Science & Emerging Technologies, 16, 41–46.
    • (2012) Innovative Food Science & Emerging Technologies , vol.16 , pp. 41-46
    • Cao, Y.1    Xia, T.2    Zhou, G.3    Xu, X.4
  • 5
    • 84897941269 scopus 로고    scopus 로고
    • Effects of high pressure processing on the thermal gelling properties of chicken breast myosin containing κ-carrageenan
    • COI: 1:CAS:528:DC%2BC2cXmvFGnuro%3D
    • Chen, X., Chen, C. G., Zhou, Y. Z., Li, P. J., Ma, F., Nishiumi, T., et al. (2014a). Effects of high pressure processing on the thermal gelling properties of chicken breast myosin containing κ-carrageenan. Food Hydrocolloids, 40, 262–272.
    • (2014) Food Hydrocolloids , vol.40 , pp. 262-272
    • Chen, X.1    Chen, C.G.2    Zhou, Y.Z.3    Li, P.J.4    Ma, F.5    Nishiumi, T.6
  • 6
    • 84920258734 scopus 로고    scopus 로고
    • Effects of high-pressure processing on the cooking loss and gel strength of chicken breast actomyosin containing sodium alginate
    • COI: 1:CAS:528:DC%2BC2cXht1aisLnJ
    • Chen, X., Li, P. J., Nishiumi, T., Takumi, H., Suzuki, A., & Chen, C. G. (2014b). Effects of high-pressure processing on the cooking loss and gel strength of chicken breast actomyosin containing sodium alginate. Food and Bioprocess Technology, 7(12), 3608–3617.
    • (2014) Food and Bioprocess Technology , vol.7 , Issue.12 , pp. 3608-3617
    • Chen, X.1    Li, P.J.2    Nishiumi, T.3    Takumi, H.4    Suzuki, A.5    Chen, C.G.6
  • 7
    • 84930621098 scopus 로고    scopus 로고
    • Combination of κ-carrageenan and soy protein isolate effects on functional properties of chopped low-fat pork batters during heat-induced gelation
    • COI: 1:CAS:528:DC%2BC2MXmsl2mtL0%3D
    • Gao, X. Q., Kang, Z. L., Zhang, W. G., Li, Y. P., & Zhou, G. H. (2015). Combination of κ-carrageenan and soy protein isolate effects on functional properties of chopped low-fat pork batters during heat-induced gelation. Food and Bioprocess Technology, 8(7), 1524–1531.
    • (2015) Food and Bioprocess Technology , vol.8 , Issue.7 , pp. 1524-1531
    • Gao, X.Q.1    Kang, Z.L.2    Zhang, W.G.3    Li, Y.P.4    Zhou, G.H.5
  • 8
    • 84907221129 scopus 로고    scopus 로고
    • Action of microbial transglutaminase (MTGase) in the modification of food proteins: a review
    • COI: 1:CAS:528:DC%2BC2cXhsFCns7vK
    • Gaspar, A. L., & de Góes-Favoni, S. P. (2015). Action of microbial transglutaminase (MTGase) in the modification of food proteins: a review. Food Chemistry, 171, 315–322.
    • (2015) Food Chemistry , vol.171 , pp. 315-322
    • Gaspar, A.L.1    de Góes-Favoni, S.P.2
  • 9
    • 84897917258 scopus 로고    scopus 로고
    • Effects of high pressure and heat treatments on physicochemical and gelation properties of rapeseed protein isolate
    • COI: 1:CAS:528:DC%2BC2cXls1Kru7o%3D
    • He, R., He, H. Y., Chao, D., Ju, X., & Aluko, R. (2014). Effects of high pressure and heat treatments on physicochemical and gelation properties of rapeseed protein isolate. Food and Bioprocess Technology, 7(5), 1344–1353.
    • (2014) Food and Bioprocess Technology , vol.7 , Issue.5 , pp. 1344-1353
    • He, R.1    He, H.Y.2    Chao, D.3    Ju, X.4    Aluko, R.5
  • 10
    • 80053183936 scopus 로고    scopus 로고
    • Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions
    • COI: 1:CAS:528:DC%2BC3MXht1ensrfE
    • Hong, G. P., Min, S. G., & Chin, K. B. (2012). Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions. Meat Science, 90(1), 185–193.
    • (2012) Meat Science , vol.90 , Issue.1 , pp. 185-193
    • Hong, G.P.1    Min, S.G.2    Chin, K.B.3
  • 11
    • 84874416406 scopus 로고    scopus 로고
    • The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate
    • COI: 1:CAS:528:DC%2BC3sXlsVKmsrg%3D
    • Hu, H., Li-Chan, E. C., Wan, L., Tian, M., & Pan, S. (2013). The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32(2), 303–311.
    • (2013) Food Hydrocolloids , vol.32 , Issue.2 , pp. 303-311
    • Hu, H.1    Li-Chan, E.C.2    Wan, L.3    Tian, M.4    Pan, S.5
  • 12
    • 84887596928 scopus 로고    scopus 로고
    • Incorporation of Lactobacillus delbrueckii subsp lactis (CIDCA 133) in cold-set gels made from high pressure-treated soybean proteins
    • COI: 1:CAS:528:DC%2BC2cXhtleltL0%3D
    • Hugo, A. A., Pérez, P. F., Añón, M. C., & Speroni, F. (2014). Incorporation of Lactobacillus delbrueckii subsp lactis (CIDCA 133) in cold-set gels made from high pressure-treated soybean proteins. Food Hydrocolloids, 37, 34–39.
    • (2014) Food Hydrocolloids , vol.37 , pp. 34-39
    • Hugo, A.A.1    Pérez, P.F.2    Añón, M.C.3    Speroni, F.4
  • 13
    • 84945232135 scopus 로고    scopus 로고
    • Chemical interactions and gel properties of black carp actomyosin affected by MTGase and their relationships
    • COI: 1:CAS:528:DC%2BC2MXhs1yku77J
    • Jia, D., Huang, Q., & Xiong, S. (2016). Chemical interactions and gel properties of black carp actomyosin affected by MTGase and their relationships. Food Chemistry, 196, 1180–1187.
    • (2016) Food Chemistry , vol.196 , pp. 1180-1187
    • Jia, D.1    Huang, Q.2    Xiong, S.3
  • 14
    • 84869502021 scopus 로고    scopus 로고
    • Transglutaminase cross-linking to enhance elastic properties of soy protein hydrogels with intercalated montmorillonite nanoclay
    • COI: 1:CAS:528:DC%2BC38XhsF2msrrJ
    • Jin, M. F., & Zhong, Q. X. (2013). Transglutaminase cross-linking to enhance elastic properties of soy protein hydrogels with intercalated montmorillonite nanoclay. Journal of Food Engineering, 115(1), 33–40.
    • (2013) Journal of Food Engineering , vol.115 , Issue.1 , pp. 33-40
    • Jin, M.F.1    Zhong, Q.X.2
  • 15
    • 81255195782 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure on some functional and nutritional properties of soy protein isolate for infant formula
    • COI: 1:CAS:528:DC%2BC3MXht1ylurnN
    • Li, H., Zhu, K., Zhou, H., & Peng, W. (2011). Effects of high hydrostatic pressure on some functional and nutritional properties of soy protein isolate for infant formula. Journal of Agricultural and Food Chemistry, 59(22), 12028–12036.
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , Issue.22 , pp. 12028-12036
    • Li, H.1    Zhu, K.2    Zhou, H.3    Peng, W.4
  • 16
    • 77955658949 scopus 로고    scopus 로고
    • Effects of chitosan on the gel properties of salt-soluble meat proteins from silver carp
    • COI: 1:CAS:528:DC%2BC3cXhtVeksLvL
    • Li, X., & Xia, W. (2010). Effects of chitosan on the gel properties of salt-soluble meat proteins from silver carp. Carbohydrate Polymers, 82(3), 958–964.
    • (2010) Carbohydrate Polymers , vol.82 , Issue.3 , pp. 958-964
    • Li, X.1    Xia, W.2
  • 17
    • 84926021669 scopus 로고    scopus 로고
    • Changes in gel properties and water properties of Nemipterus virgatus surimi gel induced by high-pressure processing
    • COI: 1:CAS:528:DC%2BC2MXkslejtA%3D%3D
    • Ma, X. S., Yi, S. M., Yu, Y. M., Li, J. R., & Chen, J. R. (2015). Changes in gel properties and water properties of Nemipterus virgatus surimi gel induced by high-pressure processing. LWT-Food Science and Technology, 61(2), 377–384.
    • (2015) LWT-Food Science and Technology , vol.61 , Issue.2 , pp. 377-384
    • Ma, X.S.1    Yi, S.M.2    Yu, Y.M.3    Li, J.R.4    Chen, J.R.5
  • 18
    • 84924169381 scopus 로고    scopus 로고
    • High pressure applied to frozen flying fish (Parexocoetus brachyterus) surimi: effect on physicochemical and rheological properties of gels
    • COI: 1:CAS:528:DC%2BC2MXjs1Kgtb4%3D
    • Moreno, H. M., Bargiela, V., Tovar, C. A., Cando, D., Borderias, A. J., & Herranz, B. (2015). High pressure applied to frozen flying fish (Parexocoetus brachyterus) surimi: effect on physicochemical and rheological properties of gels. Food Hydrocolloids, 48, 127–134.
    • (2015) Food Hydrocolloids , vol.48 , pp. 127-134
    • Moreno, H.M.1    Bargiela, V.2    Tovar, C.A.3    Cando, D.4    Borderias, A.J.5    Herranz, B.6
  • 19
    • 0031690193 scopus 로고    scopus 로고
    • Transglutaminase and its use for food processing
    • COI: 1:CAS:528:DyaK1cXmtFaktrw%3D
    • Motoki, M., & Seguro, K. (1998). Transglutaminase and its use for food processing. Trends in Food Science & Technology, 9(5), 204–210.
    • (1998) Trends in Food Science & Technology , vol.9 , Issue.5 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 20
    • 84894088317 scopus 로고    scopus 로고
    • Soy proteins: a review on composition, aggregation and emulsification
    • COI: 1:CAS:528:DC%2BC2cXmsVKmtL4%3D
    • Nishinari, K., Fang, Y., Guo, S., & Phillips, G. O. (2014). Soy proteins: a review on composition, aggregation and emulsification. Food Hydrocolloids, 39, 301–318.
    • (2014) Food Hydrocolloids , vol.39 , pp. 301-318
    • Nishinari, K.1    Fang, Y.2    Guo, S.3    Phillips, G.O.4
  • 21
    • 84973636374 scopus 로고    scopus 로고
    • Effects of microwave pretreatment and transglutaminase crosslinking on the gelation properties of soybean protein isolate and wheat gluten mixtures
    • COI: 1:CAS:528:DC%2BC28XhvFemsw%3D%3D
    • Qin, X. S., Luo, S. Z., Cai, J., Zhong, X. Y., Jiang, S. T., Zheng, Z., et al. (2016b). Effects of microwave pretreatment and transglutaminase crosslinking on the gelation properties of soybean protein isolate and wheat gluten mixtures. Journal of the Science of Food and Agriculture, 96(10), 3559–3566.
    • (2016) Journal of the Science of Food and Agriculture , vol.96 , Issue.10 , pp. 3559-3566
    • Qin, X.S.1    Luo, S.Z.2    Cai, J.3    Zhong, X.Y.4    Jiang, S.T.5    Zheng, Z.6
  • 22
    • 84957998662 scopus 로고    scopus 로고
    • Transglutaminase-induced gelation properties of soy protein isolate and wheat gluten mixtures with high intensity ultrasonic pretreatment
    • COI: 1:CAS:528:DC%2BC28XisFKisrw%3D
    • Qin, X. S., Luo, S. Z., Cai, J., Zhong, X. Y., Jiang, S. T., Zhao, Y. Y., et al. (2016a). Transglutaminase-induced gelation properties of soy protein isolate and wheat gluten mixtures with high intensity ultrasonic pretreatment. Ultrasonics Sonochemistry, 31, 590–597.
    • (2016) Ultrasonics Sonochemistry , vol.31 , pp. 590-597
    • Qin, X.S.1    Luo, S.Z.2    Cai, J.3    Zhong, X.Y.4    Jiang, S.T.5    Zhao, Y.Y.6
  • 23
    • 0342963509 scopus 로고
    • Determination of sulfhydryl groups and disulfide bonds in heat-induced gels of soy protein isolate
    • COI: 1:CAS:528:DyaL1cXlsVKntw%3D%3D
    • Shimada, K., & Cheftel, J. C. (1988). Determination of sulfhydryl groups and disulfide bonds in heat-induced gels of soy protein isolate. Journal of Agricultural and Food Chemistry, 36(1), 147–153.
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , Issue.1 , pp. 147-153
    • Shimada, K.1    Cheftel, J.C.2
  • 24
    • 84875762335 scopus 로고    scopus 로고
    • Cold-set gelation of high pressure-treated soybean proteins
    • COI: 1:CAS:528:DC%2BC3sXmtV2nu7c%3D
    • Speroni, F., & Añón, M. C. (2013). Cold-set gelation of high pressure-treated soybean proteins. Food Hydrocolloids, 33(1), 85–91.
    • (2013) Food Hydrocolloids , vol.33 , Issue.1 , pp. 85-91
    • Speroni, F.1    Añón, M.C.2
  • 25
    • 75149183532 scopus 로고    scopus 로고
    • Gelation properties of salt-extracted pea protein induced by heat treatment
    • COI: 1:CAS:528:DC%2BC3cXhtlCks7o%3D
    • Sun, X. D., & Arntfield, S. D. (2010). Gelation properties of salt-extracted pea protein induced by heat treatment. Food Research International, 43(2), 509–515.
    • (2010) Food Research International , vol.43 , Issue.2 , pp. 509-515
    • Sun, X.D.1    Arntfield, S.D.2
  • 26
    • 79961024763 scopus 로고    scopus 로고
    • Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking
    • COI: 1:CAS:528:DC%2BC3MXpvFyjsb8%3D
    • Sun, X. D., & Arntfield, S. D. (2011). Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking. Journal of Food Engineering, 107(2), 226–233.
    • (2011) Journal of Food Engineering , vol.107 , Issue.2 , pp. 226-233
    • Sun, X.D.1    Arntfield, S.D.2
  • 27
    • 55549102634 scopus 로고    scopus 로고
    • Effect of high pressure treatment on aggregation and structural properties of soy protein isolate
    • COI: 1:CAS:528:DC%2BD1cXhtl2qu7zE
    • Tang, C. H., & Ma, C. Y. (2009). Effect of high pressure treatment on aggregation and structural properties of soy protein isolate. LWT-Food Science and Technology, 42(2), 606–611.
    • (2009) LWT-Food Science and Technology , vol.42 , Issue.2 , pp. 606-611
    • Tang, C.H.1    Ma, C.Y.2
  • 28
    • 84924510932 scopus 로고    scopus 로고
    • Future of agricultural water management in Africa
    • Valipour, M. (2015). Future of agricultural water management in Africa. Archives of Agronomy and Soil Science, 61(7), 907–927.
    • (2015) Archives of Agronomy and Soil Science , vol.61 , Issue.7 , pp. 907-927
    • Valipour, M.1
  • 29
    • 84945901995 scopus 로고    scopus 로고
    • Effects of partial hydrolysis and subsequent cross-linking on wheat gluten physicochemical properties and structure
    • COI: 1:CAS:528:DC%2BC2MXhslCqu7rP
    • Wang, K., Luo, S., Cai, J., Sun, Q., Zhao, Y., Zhong, X., et al. (2016). Effects of partial hydrolysis and subsequent cross-linking on wheat gluten physicochemical properties and structure. Food Chemistry, 197, 168–174.
    • (2016) Food Chemistry , vol.197 , pp. 168-174
    • Wang, K.1    Luo, S.2    Cai, J.3    Sun, Q.4    Zhao, Y.5    Zhong, X.6
  • 30
    • 84947794248 scopus 로고    scopus 로고
    • Physicochemical alterations of wheat gluten proteins upon dough formation and frozen storage—a review from gluten, glutenin and gliadin perspectives
    • COI: 1:CAS:528:DC%2BC2MXhs1ChtbzN
    • Wang, P., Jin, Z., & Xu, X. (2015). Physicochemical alterations of wheat gluten proteins upon dough formation and frozen storage—a review from gluten, glutenin and gliadin perspectives. Trends in Food Science & Technology, 46, 189–198.
    • (2015) Trends in Food Science & Technology , vol.46 , pp. 189-198
    • Wang, P.1    Jin, Z.2    Xu, X.3
  • 31
    • 49649095219 scopus 로고    scopus 로고
    • Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein
    • COI: 1:CAS:528:DC%2BD1cXhtVagu73P
    • Xiong, Y. L., Agyare, K. K., & Addo, K. (2008). Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein. Meat Science, 80(2), 535–544.
    • (2008) Meat Science , vol.80 , Issue.2 , pp. 535-544
    • Xiong, Y.L.1    Agyare, K.K.2    Addo, K.3
  • 32
    • 84946924689 scopus 로고    scopus 로고
    • Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel
    • COI: 1:CAS:528:DC%2BC2MXhslCmsL3M
    • Zhang, P., Hu, T., Feng, S., Xu, Q., Zheng, T., Zhou, M., et al. (2016). Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel. Ultrasonics Sonochemistry, 29, 380–387.
    • (2016) Ultrasonics Sonochemistry , vol.29 , pp. 380-387
    • Zhang, P.1    Hu, T.2    Feng, S.3    Xu, Q.4    Zheng, T.5    Zhou, M.6
  • 33
    • 84929459658 scopus 로고    scopus 로고
    • Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure
    • COI: 1:CAS:528:DC%2BC2MXnsFGmt7Y%3D
    • Zhang, Z., Yang, Y., Tang, X., Chen, Y., & You, Y. (2015). Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure. Food Chemistry, 188, 111–118.
    • (2015) Food Chemistry , vol.188 , pp. 111-118
    • Zhang, Z.1    Yang, Y.2    Tang, X.3    Chen, Y.4    You, Y.5
  • 34
    • 84907899400 scopus 로고    scopus 로고
    • High pressure effects on heat-induced gelation of threadfin bream (Nemipterus spp.) surimi
    • COI: 1:CAS:528:DC%2BC2cXhsFShsL3O
    • Zhu, Z., Lanier, T. C., & Farkas, B. E. (2015). High pressure effects on heat-induced gelation of threadfin bream (Nemipterus spp.) surimi. Journal of Food Engineering, 146, 23–27.
    • (2015) Journal of Food Engineering , vol.146 , pp. 23-27
    • Zhu, Z.1    Lanier, T.C.2    Farkas, B.E.3


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