메뉴 건너뛰기




Volumn 46, Issue 12, 2011, Pages 2447-2459

Enzymatic hydrolysis of soy proteins and the hydrolysates utilisation

Author keywords

Aglycones; Debittering; Degree of hydrolysis; Enzymatic hydrolysis; Glycosides; Soy proteins

Indexed keywords

ADENOSINE MONOPHOSPHATE; AGLYCONES; DEBITTERING; DEGREE OF HYDROLYSIS; FUNCTIONAL FOODS; FUNCTIONAL PROPERTIES; HIGH COSTS; HIGH PRESSURE TREATMENTS; HUMAN BEING; IMMOBILISATION; MONOSODIUM GLUTAMATE; PRODUCTION COST; PROTEIN SOURCES; SELECTIVE SEPARATION; SOY PROTEIN; SOY PROTEIN HYDROLYSATE;

EID: 81255171576     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2011.02785.x     Document Type: Review
Times cited : (129)

References (131)
  • 1
    • 0001070322 scopus 로고    scopus 로고
    • Comparison of the aroma characteristics of acid-hydrolyzed and enzyme-hydrolyzed vegetable proteins produced from soy
    • Aaslyng, M.D., Elmore, J.S. & Mottram, D.S. (1998). Comparison of the aroma characteristics of acid-hydrolyzed and enzyme-hydrolyzed vegetable proteins produced from soy. Journal of Agricultural and Food Chemistry, 46, 5225-5231.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 5225-5231
    • Aaslyng, M.D.1    Elmore, J.S.2    Mottram, D.S.3
  • 2
    • 0034992888 scopus 로고    scopus 로고
    • Effect of succinylation on the physicochemical properties of soy protein hydrolysate
    • Achouri, A. & Wang, Z. (2001). Effect of succinylation on the physicochemical properties of soy protein hydrolysate. Food Research International, 34, 507-514.
    • (2001) Food Research International , vol.34 , pp. 507-514
    • Achouri, A.1    Wang, Z.2
  • 3
    • 0032446301 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates
    • Achouri, A., Wang, Z. & Xu, S.Y. (1999). Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates. Food Research International, 31, 617-623.
    • (1999) Food Research International , vol.31 , pp. 617-623
    • Achouri, A.1    Wang, Z.2    Xu, S.Y.3
  • 5
    • 0021501055 scopus 로고
    • Control of proteolytic reaction and of the level of bitterness in protein hydrolysis process
    • Adler-Nissen, J. (1984). Control of proteolytic reaction and of the level of bitterness in protein hydrolysis process. Journal of Chemical Technology and Biotechnology, 34B, 215-222.
    • (1984) Journal of Chemical Technology and Biotechnology , vol.34 B , pp. 215-222
    • Adler-Nissen, J.1
  • 7
    • 0018318768 scopus 로고
    • The influence of peptide chain length on taste and functional properties of enzymatically modified soy protein
    • In: (edited by A. Pour-El). Washington, DC: ACS Symposium Series.
    • Adler-Nissen, J. & Olsen, H.S. (1979). The influence of peptide chain length on taste and functional properties of enzymatically modified soy protein. In: Functionality and Protein Structure (edited by A. Pour-El). Pp. 125-146. Washington, DC: ACS Symposium Series.
    • (1979) Functionality and Protein Structure , pp. 125-146
    • Adler-Nissen, J.1    Olsen, H.S.2
  • 8
    • 46749154975 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of soybean protein using lactic acid bacteria
    • Aguirre, L., Garro, M.S. & Giori, G.S. (2008). Enzymatic hydrolysis of soybean protein using lactic acid bacteria. Food Chemistry, 111, 976-982.
    • (2008) Food Chemistry , vol.111 , pp. 976-982
    • Aguirre, L.1    Garro, M.S.2    Giori, G.S.3
  • 9
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Alder-Nissen, J. (1979). Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry, 27, 1256-1262.
    • (1979) Journal of Agricultural and Food Chemistry , vol.27 , pp. 1256-1262
    • Alder-Nissen, J.1
  • 12
    • 33748741530 scopus 로고    scopus 로고
    • Soy protein components active in the regulation of cholesterol homeostasis
    • In. Royal Society of Chemistry (Special Publication).
    • Arnoldi, A., D'Agostina, A., Boschin, G., Lovati, M.R., Manzoni, C. & Sirtori, C.R. (2001). Soy protein components active in the regulation of cholesterol homeostasis. In: Biologically Active Phytochemicals in Food, Vol. 269. Pp. 103-106. Royal Society of Chemistry (Special Publication).
    • (2001) Biologically Active Phytochemicals in Food , vol.269 , pp. 103-106
    • Arnoldi, A.1    D'Agostina, A.2    Boschin, G.3    Lovati, M.R.4    Manzoni, C.5    Sirtori, C.R.6
  • 13
    • 0031181509 scopus 로고    scopus 로고
    • Effect of different proteases on bitterness of hemoglobin hydrolysates
    • Aubes-Dufau, I. & Combes, D. (1997). Effect of different proteases on bitterness of hemoglobin hydrolysates. Applied Biochemistry and Biotechnology, 67, 127-138.
    • (1997) Applied Biochemistry and Biotechnology , vol.67 , pp. 127-138
    • Aubes-Dufau, I.1    Combes, D.2
  • 14
    • 33749564789 scopus 로고    scopus 로고
    • Effect of limited hydrolysis on traditional soy protein concentrate
    • Barac, M.B., Jovanovic, S.T., Stanojevic, S.P. & Pesic, M.B. (2006). Effect of limited hydrolysis on traditional soy protein concentrate. Sensors, 6, 1087-1101.
    • (2006) Sensors , vol.6 , pp. 1087-1101
    • Barac, M.B.1    Jovanovic, S.T.2    Stanojevic, S.P.3    Pesic, M.B.4
  • 15
    • 0004473180 scopus 로고
    • Sweet and bitter compounds: structure and taste relationship
    • In: Boudreau, J. C. (Ed.). ACS Symposium Series
    • Belitz, H.D., Chen, W., Jugel, H., Treleano, R., Wieser, H., Gasteiger, J. & Marsili, M. (1979). Sweet and bitter compounds: structure and taste relationship. In: Food Taste Chemistry. Boudreau, J. C. (Ed.). ACS Symposium Series, 115, Pp. 93-131.
    • (1979) Food Taste Chemistry , vol.115 , pp. 93-131
    • Belitz, H.D.1    Chen, W.2    Jugel, H.3    Treleano, R.4    Wieser, H.5    Gasteiger, J.6    Marsili, M.7
  • 16
    • 81255182013 scopus 로고
    • Enzyme modified soy protein for use as an egg white substitute. US Pat No. 4,632,903.
    • Boyce, C.O.L., Lanzilotta, R.P. & Wong, T.M. (1986). Enzyme modified soy protein for use as an egg white substitute. US Pat No. 4, 632, 903.
    • (1986)
    • Boyce, C.O.L.1    Lanzilotta, R.P.2    Wong, T.M.3
  • 17
    • 0041978315 scopus 로고    scopus 로고
    • Physicochemical properties and yield of sunflower protein enzymatic hydrolysates as affected by enzyme and defatted sunflower meal
    • Cai, T., Chang, K.C. & Lunde, H. (1996). Physicochemical properties and yield of sunflower protein enzymatic hydrolysates as affected by enzyme and defatted sunflower meal. Journal of Agricultural and Food Chemistry, 44, 3500-3506.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 3500-3506
    • Cai, T.1    Chang, K.C.2    Lunde, H.3
  • 18
    • 0342804403 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties
    • Calderón de la Barca, A.M., Ruiz-Salazar, R.A. & Jara-Marini, M.E. (2000). Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties. Journal of Food Science, 65, 246-253.
    • (2000) Journal of Food Science , vol.65 , pp. 246-253
    • Calderón de la Barca, A.M.1    Ruiz-Salazar, R.A.2    Jara-Marini, M.E.3
  • 20
    • 0034677655 scopus 로고    scopus 로고
    • T2Rs function as bitter taste receptors
    • Chandrashekar, J., Mueller, K.L., Hoon, M.A. et al. (2000). T2Rs function as bitter taste receptors. Cell, 100, 703-711.
    • (2000) Cell , vol.100 , pp. 703-711
    • Chandrashekar, J.1    Mueller, K.L.2    Hoon, M.A.3
  • 22
    • 2542545209 scopus 로고    scopus 로고
    • Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein
    • Chen, H.M., Muramoto, K., Yamauchi, F. & Nokihara, K. (1996). Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. Journal of Agricultural and Food Chemistry, 44, 2126-2130.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 2126-2130
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Nokihara, K.4
  • 23
    • 0002384554 scopus 로고    scopus 로고
    • Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein
    • Chen, H.M., Muramoto, K., Yamauchi, F., Fujimoto, K. & Nokihara, K. (1998). Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agricultural and Food Chemistry, 46, 49-53.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 49-53
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5
  • 24
    • 1842631901 scopus 로고    scopus 로고
    • Soybean protein-derived hydrolysate affects blood pressure in spontaneously hypertensive rats
    • Chen, J.R., Yang, S.C., Suetsuna, K. & Chao, J.C.J. (2004). Soybean protein-derived hydrolysate affects blood pressure in spontaneously hypertensive rats. Journal of Food Biochemistry, 28, 61-73.
    • (2004) Journal of Food Biochemistry , vol.28 , pp. 61-73
    • Chen, J.R.1    Yang, S.C.2    Suetsuna, K.3    Chao, J.C.J.4
  • 25
    • 79952533269 scopus 로고    scopus 로고
    • Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties
    • Chen, L., Chen, J.S., Ren, J.Y. & Zhao, M.M. (2011). Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties. Food Hydrocolloids, 25, 887-897.
    • (2011) Food Hydrocolloids , vol.25 , pp. 887-897
    • Chen, L.1    Chen, J.S.2    Ren, J.Y.3    Zhao, M.M.4
  • 26
    • 81255134985 scopus 로고
    • Protein hydrolysis. US Pat. No. 4,443,540.
    • Cheryan, M. & Deeslie, W.D. (1984). Protein hydrolysis. US Pat. No. 4, 443, 540.
    • (1984)
    • Cheryan, M.1    Deeslie, W.D.2
  • 27
    • 0033023593 scopus 로고    scopus 로고
    • Functional properties of soy protein hydrolysate produced from a continuous membrane reactor system
    • Chiang, W.D., Shih, C.J. & Chu, Y.H. (1999). Functional properties of soy protein hydrolysate produced from a continuous membrane reactor system. Food Chemistry, 65, 189-194.
    • (1999) Food Chemistry , vol.65 , pp. 189-194
    • Chiang, W.D.1    Shih, C.J.2    Chu, Y.H.3
  • 29
    • 0036945671 scopus 로고    scopus 로고
    • Hydrolysis of soybean isoflavone glycosides by lactic acid bacteria
    • Choi, Y.B., Kim, K.S. & Rhee, J.S. (2002). Hydrolysis of soybean isoflavone glycosides by lactic acid bacteria. Biotechnology Letters, 24, 2113-2116.
    • (2002) Biotechnology Letters , vol.24 , pp. 2113-2116
    • Choi, Y.B.1    Kim, K.S.2    Rhee, J.S.3
  • 30
    • 33847796872 scopus 로고    scopus 로고
    • Conversion of isoflavone glucosides to aglycones in soymilk by fermentation with lactic acid bacteria
    • Chun, J.Y., Kim, G.M., Lee, K.W. et al. (2007). Conversion of isoflavone glucosides to aglycones in soymilk by fermentation with lactic acid bacteria. Journal of Food Science, 72, M39-M44.
    • (2007) Journal of Food Science , vol.72
    • Chun, J.Y.1    Kim, G.M.2    Lee, K.W.3
  • 31
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church, F.C., Swaisgood, H.E., Porter, D.H. & Catignani, G.L. (1983). Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science, 66, 1219-1227.
    • (1983) Journal of Dairy Science , vol.66 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 34
    • 33947143443 scopus 로고    scopus 로고
    • The effect of enzymatic treatment of a sunflower protein isolate on the rate of adsorption at the air-water interface
    • Conde, J.M. & Patino, J.M.R. (2007). The effect of enzymatic treatment of a sunflower protein isolate on the rate of adsorption at the air-water interface. Journal of Food Engineering, 78, 1001-1009.
    • (2007) Journal of Food Engineering , vol.78 , pp. 1001-1009
    • Conde, J.M.1    Patino, J.M.R.2
  • 35
    • 0028529051 scopus 로고
    • Control of food allergies using protein hydrolysates
    • Cordle, C.T. (1994). Control of food allergies using protein hydrolysates. Food Technology, 48, 72-76.
    • (1994) Food Technology , vol.48 , pp. 72-76
    • Cordle, C.T.1
  • 36
    • 33645242533 scopus 로고    scopus 로고
    • Trpm5 null mice respond to bitter, sweet, and umami compounds
    • Damak, S., Rong, M., Yasumatsu, K. et al. (2006). Trpm5 null mice respond to bitter, sweet, and umami compounds. Chemical Senses, 31, 253-264.
    • (2006) Chemical Senses , vol.31 , pp. 253-264
    • Damak, S.1    Rong, M.2    Yasumatsu, K.3
  • 37
    • 1542334009 scopus 로고    scopus 로고
    • Effect of enzymatic hydrolysis on emulsifying and foaming properties of milk proteins - a review
    • Darwicz, M., Dziuba, J. & Caessens, P.W. Jr (2000). Effect of enzymatic hydrolysis on emulsifying and foaming properties of milk proteins - a review. Poland Journal of Food Nutritional Science, 50, 3-8.
    • (2000) Poland Journal of Food Nutritional Science , vol.50 , pp. 3-8
    • Darwicz, M.1    Dziuba, J.2    Caessens Jr, P.W.3
  • 38
    • 77953906502 scopus 로고    scopus 로고
    • Enhancing the biotransformation of isoflavones in soymilk supplemented with lactose using probiotic bacteria during extended fermentation
    • Ding, W.K. & Shah, N.P. (2010). Enhancing the biotransformation of isoflavones in soymilk supplemented with lactose using probiotic bacteria during extended fermentation. Journal of Food Science, 75, M140-M149.
    • (2010) Journal of Food Science , vol.75
    • Ding, W.K.1    Shah, N.P.2
  • 39
    • 38349057263 scopus 로고    scopus 로고
    • Production of beta-glucosidase and hydrolysis of isoflavone phytoestrogens by Lactobacillus acidophilus, Bifidobacterium lactis, and Lactobacillus casei in soymilk
    • Donkor, O.N. & Shah, N.P. (2008). Production of beta-glucosidase and hydrolysis of isoflavone phytoestrogens by Lactobacillus acidophilus, Bifidobacterium lactis, and Lactobacillus casei in soymilk. Journal of Food Science, 73, M15-M20.
    • (2008) Journal of Food Science , vol.73
    • Donkor, O.N.1    Shah, N.P.2
  • 40
    • 31644441857 scopus 로고    scopus 로고
    • Enzymatic debittering of food protein hydrolysates
    • FitzGerald, R.J. & O'Cuinn, G. (2006). Enzymatic debittering of food protein hydrolysates. Biotechnology Advances, 24, 234-237.
    • (2006) Biotechnology Advances , vol.24 , pp. 234-237
    • FitzGerald, R.J.1    O'Cuinn, G.2
  • 41
    • 0028524317 scopus 로고
    • Use of hydrolysates for protein supplementation
    • Frokjaer, S. (1994). Use of hydrolysates for protein supplementation. Food Technology, 48, 86-88.
    • (1994) Food Technology , vol.48 , pp. 86-88
    • Frokjaer, S.1
  • 42
    • 0000271924 scopus 로고
    • Nature of stem bromelain treatments on the aggregation and gelation of soybean proteins
    • Fuke, Y., Sekiguchi, M. & Matsuoka, H. (1985). Nature of stem bromelain treatments on the aggregation and gelation of soybean proteins. Journal of Food Science, 50, 1283-1288.
    • (1985) Journal of Food Science , vol.50 , pp. 1283-1288
    • Fuke, Y.1    Sekiguchi, M.2    Matsuoka, H.3
  • 43
    • 1242300061 scopus 로고    scopus 로고
    • Production and characterization of bioactive peptides from soy hydrolysate and soy fermented food
    • Gibbs, B.F., Zougman, A., Masse, R. & Mulligan, C. (2004). Production and characterization of bioactive peptides from soy hydrolysate and soy fermented food. Food Research International, 37, 123-131.
    • (2004) Food Research International , vol.37 , pp. 123-131
    • Gibbs, B.F.1    Zougman, A.2    Masse, R.3    Mulligan, C.4
  • 44
    • 0029935309 scopus 로고    scopus 로고
    • Hydrolytic characteristics of chitosan-immobilized as 1.398 neutral proteinase (from B. subtilis) to soybean protein
    • Guo, M.L., Jiang, Y.M., Ma, Z.L. & Li, Y.L. (1996). Hydrolytic characteristics of chitosan-immobilized as 1.398 neutral proteinase (from B. subtilis) to soybean protein. Food Chemistry, 55, 373-377.
    • (1996) Food Chemistry , vol.55 , pp. 373-377
    • Guo, M.L.1    Jiang, Y.M.2    Ma, Z.L.3    Li, Y.L.4
  • 45
    • 0037174121 scopus 로고    scopus 로고
    • Bioavailability of isoflavones
    • Hendrich, S. (2002). Bioavailability of isoflavones. Journal of Chromatography B, 777, 203-210.
    • (2002) Journal of Chromatography B , vol.777 , pp. 203-210
    • Hendrich, S.1
  • 46
    • 1542304014 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates
    • Hrcková, M., Rusñáková, M. & Zemanovic, J. (2002). Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates. Czech Journal of Food Science, 20, 7-14.
    • (2002) Czech Journal of Food Science , vol.20 , pp. 7-14
    • Hrcková, M.1    Rusñáková, M.2    Zemanovic, J.3
  • 47
    • 63549095536 scopus 로고    scopus 로고
    • Comparison between soybean peptides production by enzymatic hydrolysis with and without ultrasound
    • Hu, A.J. & Zheng, J. (2005). Comparison between soybean peptides production by enzymatic hydrolysis with and without ultrasound. Food Science and Technology, 6, 27-30.
    • (2005) Food Science and Technology , vol.6 , pp. 27-30
    • Hu, A.J.1    Zheng, J.2
  • 48
  • 51
    • 0033949949 scopus 로고    scopus 로고
    • Soy isoflavone aglycones are absorbed faster and in higher amounts than their glucosides in humans
    • Izumi, T., Piskula, M.K., Osawa, S. et al. (2000). Soy isoflavone aglycones are absorbed faster and in higher amounts than their glucosides in humans. Journal of Nutrition, 130, 1695-1699.
    • (2000) Journal of Nutrition , vol.130 , pp. 1695-1699
    • Izumi, T.1    Piskula, M.K.2    Osawa, S.3
  • 54
    • 14844310248 scopus 로고    scopus 로고
    • Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis
    • Jung, S., Murphy, P.A. & Johnson, L.A. (2005). Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis. Journal of Food Science, 70, 180-186.
    • (2005) Journal of Food Science , vol.70 , pp. 180-186
    • Jung, S.1    Murphy, P.A.2    Johnson, L.A.3
  • 57
    • 0032831306 scopus 로고    scopus 로고
    • Molecular characterization and bitter taste formation of tryptic hydropysis of 11S glycinin
    • Kim, M.R., Choi, S.Y. & Lee, C.H. (1999). Molecular characterization and bitter taste formation of tryptic hydropysis of 11S glycinin. Journal of Microbiology and Biotechnology, 9, 509-513.
    • (1999) Journal of Microbiology and Biotechnology , vol.9 , pp. 509-513
    • Kim, M.R.1    Choi, S.Y.2    Lee, C.H.3
  • 58
    • 33845429978 scopus 로고    scopus 로고
    • Characteristic property of low bitterness in protein hydrolysates by a novel soybean protease D3
    • Kodera, T., Asano, M. & Nio, N. (2006). Characteristic property of low bitterness in protein hydrolysates by a novel soybean protease D3. Journal of Food Science, 71, 609-614.
    • (2006) Journal of Food Science , vol.71 , pp. 609-614
    • Kodera, T.1    Asano, M.2    Nio, N.3
  • 59
    • 50349093170 scopus 로고    scopus 로고
    • Enzymatic preparation of immunomodulating hydrolysates from soy proteins
    • Kong, X.Z., Guo, M.M., Hua, Y.F., Cao, G. & Zhang, C.M. (2008). Enzymatic preparation of immunomodulating hydrolysates from soy proteins. Bioresource Technology, 99, 8873-8879.
    • (2008) Bioresource Technology , vol.99 , pp. 8873-8879
    • Kong, X.Z.1    Guo, M.M.2    Hua, Y.F.3    Cao, G.4    Zhang, C.M.5
  • 60
    • 0033793853 scopus 로고    scopus 로고
    • Comprehensive study on G-protein α-subunits in taste bud cells, with special reference to the occurrence of Gαi2 as a major Gα species
    • Kusakabe, Y., Yasuoka, A., Asano-Miyoshi, M. et al. (2000). Comprehensive study on G-protein α-subunits in taste bud cells, with special reference to the occurrence of Gαi2 as a major Gα species. Chemical Senses, 25, 525-531.
    • (2000) Chemical Senses , vol.25 , pp. 525-531
    • Kusakabe, Y.1    Yasuoka, A.2    Asano-Miyoshi, M.3
  • 61
    • 0028526562 scopus 로고
    • Enzymatic production of protein hydrolysates for food use
    • Lahl, W.J. & Braun, S.D. (1994). Enzymatic production of protein hydrolysates for food use. Food Technology, 48, 68-71.
    • (1994) Food Technology , vol.48 , pp. 68-71
    • Lahl, W.J.1    Braun, S.D.2
  • 62
    • 0035078028 scopus 로고    scopus 로고
    • Characterization of hydrolysates produced by mild acid treatment and enzymatic hydrolysis of defatted soybean flour
    • Lee, J.Y., Lee, H.D. & Lee, C.H. (2001). Characterization of hydrolysates produced by mild acid treatment and enzymatic hydrolysis of defatted soybean flour. Food Research International, 34, 217-222.
    • (2001) Food Research International , vol.34 , pp. 217-222
    • Lee, J.Y.1    Lee, H.D.2    Lee, C.H.3
  • 63
    • 81255126473 scopus 로고    scopus 로고
    • Changing taste by targeting the ion channel TRPM5
    • Liman, E.R. (2010). Changing taste by targeting the ion channel TRPM5. The Open Drug Discovery Journal, 2, 98-102.
    • (2010) The Open Drug Discovery Journal , vol.2 , pp. 98-102
    • Liman, E.R.1
  • 65
    • 0031453033 scopus 로고    scopus 로고
    • Hydrolysis of β-lactoglobulin by four different proteinases monitored by capillary electrophoresis and high performance liquid chromatography
    • Madsen, J.S., Ahmt, T.O., Otte, J., Halkier, T. & Qvist, K.B. (1997). Hydrolysis of β-lactoglobulin by four different proteinases monitored by capillary electrophoresis and high performance liquid chromatography. International Dairy Journal, 7, 399-409.
    • (1997) International Dairy Journal , vol.7 , pp. 399-409
    • Madsen, J.S.1    Ahmt, T.O.2    Otte, J.3    Halkier, T.4    Qvist, K.B.5
  • 67
    • 0037016771 scopus 로고    scopus 로고
    • Molecular mechanisms of bitter and sweet taste transduction
    • Margolskee, R.F. (2002). Molecular mechanisms of bitter and sweet taste transduction. Journal of Biological Chemistry, 277, 1-4.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 1-4
    • Margolskee, R.F.1
  • 68
    • 0027947857 scopus 로고
    • Continuous monitoring of enzymatic whey protein hydrolysis. Correlation of base consumption with soluble nitrogen content
    • Margot, A., Flaschel, E. & Renken, A. (1994). Continuous monitoring of enzymatic whey protein hydrolysis. Correlation of base consumption with soluble nitrogen content. Process Biochemistry, 29, 257-262.
    • (1994) Process Biochemistry , vol.29 , pp. 257-262
    • Margot, A.1    Flaschel, E.2    Renken, A.3
  • 70
    • 79956306782 scopus 로고    scopus 로고
    • Effects of soy protein hydrolysis and polysaccharides addition on foaming properties studied by cluster analysis
    • Martínez, K.D., Farías, M.E. & Pilosof, A.M.R. (2011). Effects of soy protein hydrolysis and polysaccharides addition on foaming properties studied by cluster analysis. Food Hydrocolloids, 25, 1667-1676.
    • (2011) Food Hydrocolloids , vol.25 , pp. 1667-1676
    • Martínez, K.D.1    Farías, M.E.2    Pilosof, A.M.R.3
  • 71
    • 0031999039 scopus 로고    scopus 로고
    • Effects of high-pressure treatment on the tryptic hydrolysis of bovine β-lactoglobulin AB
    • Maynard, F., Weingand, A., Hau, J. & Lost, R. (1998). Effects of high-pressure treatment on the tryptic hydrolysis of bovine β-lactoglobulin AB. International Dairy Journal, 8, 125-133.
    • (1998) International Dairy Journal , vol.8 , pp. 125-133
    • Maynard, F.1    Weingand, A.2    Hau, J.3    Lost, R.4
  • 72
    • 35648946057 scopus 로고    scopus 로고
    • Transduction mechanisms in taste cells
    • In: (edited by S. Frings & J. Bradley). Germany: Wiley-VCH.
    • Medler, K. & Kinnamon, S. (2004). Transduction mechanisms in taste cells. In: Transduction Channels in Sensory Cells (edited by S. Frings & J. Bradley). Pp. 153-174. Germany: Wiley-VCH.
    • (2004) Transduction Channels in Sensory Cells , pp. 153-174
    • Medler, K.1    Kinnamon, S.2
  • 73
    • 81255134984 scopus 로고
    • Process for preparing mayonnaise-like foods. US Patent No. 4,302,474.
    • Mikami, Y., Kanda, H. & Uno, A. (1981). Process for preparing mayonnaise-like foods. US Patent No. 4, 302, 474.
    • (1981)
    • Mikami, Y.1    Kanda, H.2    Uno, A.3
  • 74
    • 0033578410 scopus 로고    scopus 로고
    • Blocking taste receptor activation of gustducin inhibits gustatory responses to bitter compounds
    • Ming, D., Ninomilya, Y. & Margolskee, R.F. (1999). Blocking taste receptor activation of gustducin inhibits gustatory responses to bitter compounds. Proceedings of the National Academy of Sciences, 96, 9903-9908.
    • (1999) Proceedings of the National Academy of Sciences , vol.96 , pp. 9903-9908
    • Ming, D.1    Ninomilya, Y.2    Margolskee, R.F.3
  • 75
    • 0036392199 scopus 로고    scopus 로고
    • Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties
    • Molina, S.E. & Wagner, J.R. (2002). Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties. Food Research International, 35, 511-518.
    • (2002) Food Research International , vol.35 , pp. 511-518
    • Molina, S.E.1    Wagner, J.R.2
  • 78
    • 29244443998 scopus 로고    scopus 로고
    • Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates
    • Moure, A., Domínguez, H. & Parajó, J.C. (2006). Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates. Process Biochemistry, 41, 447-456.
    • (2006) Process Biochemistry , vol.41 , pp. 447-456
    • Moure, A.1    Domínguez, H.2    Parajó, J.C.3
  • 81
    • 23044461422 scopus 로고
    • Prediction of bitterness of peptides from their amino acid composition
    • Ney, K.H. (1971). Prediction of bitterness of peptides from their amino acid composition. Zeitschrift Fur Lebensmittel-untersuchung und-forschung, 147, 64-68.
    • (1971) Zeitschrift Fur Lebensmittel-untersuchung und-forschung , vol.147 , pp. 64-68
    • Ney, K.H.1
  • 82
    • 0000974831 scopus 로고
    • Bitterness of peptides: amino acid composition and chain length
    • In: (edited by J.C. Boudreau). Washington, DC: American Chemical Society.
    • Ney, K.H. (1979). Bitterness of peptides: amino acid composition and chain length. In: Food Taste Chemistry (edited by J.C. Boudreau). Pp. 149-173. Washington, DC: American Chemical Society.
    • (1979) Food Taste Chemistry , pp. 149-173
    • Ney, K.H.1
  • 83
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen, P.M., Petersen, D. & Dambmann, C. (2001). Improved method for determining food protein degree of hydrolysis. Journal of Food Science, 66, 642-646.
    • (2001) Journal of Food Science , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 84
    • 0036189875 scopus 로고    scopus 로고
    • Debittering of enzymatic hydrolysates using an aminopeptidase from the edible basidiomycete Grifola frondosa
    • Nishiwaki, T., Yoshimizu, S., Furuta, M. & Hayashi, K. (2002). Debittering of enzymatic hydrolysates using an aminopeptidase from the edible basidiomycete Grifola frondosa. Journal of Bioscience and Bioengineering, 93, 60-63.
    • (2002) Journal of Bioscience and Bioengineering , vol.93 , pp. 60-63
    • Nishiwaki, T.1    Yoshimizu, S.2    Furuta, M.3    Hayashi, K.4
  • 85
    • 81255126474 scopus 로고
    • Method of producing an egg white substitute material. US Patent. No. 4,431,629.
    • Olsen, H.A.S. (1984). Method of producing an egg white substitute material. US Patent. No. 4, 431, 629.
    • (1984)
    • Olsen, H.A.S.1
  • 86
    • 23844554843 scopus 로고    scopus 로고
    • Soybean foods and their benefits: potential mechanisms of action
    • Omoni, A.O. & Aluko, R.E. (2005). Soybean foods and their benefits: potential mechanisms of action. Nutrition Reviews, 63, 272-283.
    • (2005) Nutrition Reviews , vol.63 , pp. 272-283
    • Omoni, A.O.1    Aluko, R.E.2
  • 87
    • 0343725673 scopus 로고    scopus 로고
    • Analysis of products, mechanisms of reaction, and some functional properties of soy protein hydrolysates
    • Ortiz, S.E.M. & An, M.C. (2000). Analysis of products, mechanisms of reaction, and some functional properties of soy protein hydrolysates. Journal of the American Oil Chemists' Society, 77, 1293-1301.
    • (2000) Journal of the American Oil Chemists' Society , vol.77 , pp. 1293-1301
    • Ortiz, S.E.M.1    An, M.C.2
  • 88
    • 0036392199 scopus 로고    scopus 로고
    • Hydrolysates of native and modified soy protein isolates: structural characteristics, solubility and foaming properties
    • Ortiz, S.E.M. & Wagner, J.R. (2002). Hydrolysates of native and modified soy protein isolates: structural characteristics, solubility and foaming properties. Food Research International, 35, 511-518.
    • (2002) Food Research International , vol.35 , pp. 511-518
    • Ortiz, S.E.M.1    Wagner, J.R.2
  • 89
    • 19444384615 scopus 로고    scopus 로고
    • Stability of β-glucosidase activity produced by Bifidobacterium and Lactobacillus spp. in fermented soymilk during processing and storage
    • Otieno, D.O., Ashton, J.F. & Shah, N.P. (2005). Stability of β-glucosidase activity produced by Bifidobacterium and Lactobacillus spp. in fermented soymilk during processing and storage. Journal of Food Science, 70, M236-M241.
    • (2005) Journal of Food Science , vol.70
    • Otieno, D.O.1    Ashton, J.F.2    Shah, N.P.3
  • 90
    • 32544443662 scopus 로고    scopus 로고
    • Evaluation of enzymic potential for biotransformation of isoflavone phytoestrogen in soymilk by Bifidobacterium animalis, Lactobacillus acidophilus and Lactobacillus casei
    • Otieno, D.O., Ashton, J.F. & Shah, N.P. (2006). Evaluation of enzymic potential for biotransformation of isoflavone phytoestrogen in soymilk by Bifidobacterium animalis, Lactobacillus acidophilus and Lactobacillus casei. Food Research International, 39, 394-407.
    • (2006) Food Research International , vol.39 , pp. 394-407
    • Otieno, D.O.1    Ashton, J.F.2    Shah, N.P.3
  • 91
    • 1942426992 scopus 로고    scopus 로고
    • Conversion of malonyl β-glucoside isoflavones into glycoside isoflavones found in some cultivars of Brazilian soybeans
    • Park, Y.K., Aguiar, C.L., Alencar, S.M., Mascrenhas, H.A.A. & Scamparini, A.R.P. (2002). Conversion of malonyl β-glucoside isoflavones into glycoside isoflavones found in some cultivars of Brazilian soybeans. Ciência e Tecnologia de Alimentos, 22, 130-135.
    • (2002) Ciência e Tecnologia de Alimentos , vol.22 , pp. 130-135
    • Park, Y.K.1    Aguiar, C.L.2    Alencar, S.M.3    Mascrenhas, H.A.A.4    Scamparini, A.R.P.5
  • 92
    • 1942426995 scopus 로고    scopus 로고
    • Production of enriched isoflavone aglycones during processing of soy protein isolates and soy protein concentrates [Abstract]
    • In. Chicago, Illinois: Institute of Food Technologists.
    • Park, Y.K., Lui, M.C.Y. & Aguiar, C.L. (2003). Production of enriched isoflavone aglycones during processing of soy protein isolates and soy protein concentrates [Abstract]. In: 2003 IFT Annual Meeting Book of Abstracts, 12-16 July 2003. Pp. 215. Chicago, Illinois: Institute of Food Technologists.
    • (2003) 2003 IFT Annual Meeting Book of Abstracts, 12-16 July 2003 , pp. 215
    • Park, Y.K.1    Lui, M.C.Y.2    Aguiar, C.L.3
  • 94
    • 0002050733 scopus 로고
    • Soy proteins
    • In: (edited by B.J.F. Hudson). Essex: Applied Science Publishers.
    • Pearson, A.M. (1983). Soy proteins. In: Developments in Food Proteins - 2 (edited by B.J.F. Hudson). Pp. 67-108. Essex: Applied Science Publishers.
    • (1983) Developments in Food Proteins - 2 , pp. 67-108
    • Pearson, A.M.1
  • 95
    • 0028523477 scopus 로고
    • Removing bitterness from protein hydrolysates
    • Pedersen, B. (1994). Removing bitterness from protein hydrolysates. Food Technology, 48, 96-98.
    • (1994) Food Technology , vol.48 , pp. 96-98
    • Pedersen, B.1
  • 96
    • 0036813306 scopus 로고    scopus 로고
    • Antioxidant activity of soy protein hydrolyzates in a liposomial system
    • Peña-Ramos, E.A. & Xiong, Y.L. (2002). Antioxidant activity of soy protein hydrolyzates in a liposomial system. Journal of Food Science, 67, 2952-2956.
    • (2002) Journal of Food Science , vol.67 , pp. 2952-2956
    • Peña-Ramos, E.A.1    Xiong, Y.L.2
  • 98
    • 0942278928 scopus 로고    scopus 로고
    • High pressure and the enzymatic hydrolysis of soybean whey proteins
    • Peñas, E., Préstamo, G. & Gomez, R. (2004). High pressure and the enzymatic hydrolysis of soybean whey proteins. Food Chemistry, 85, 641-648.
    • (2004) Food Chemistry , vol.85 , pp. 641-648
    • Peñas, E.1    Préstamo, G.2    Gomez, R.3
  • 99
    • 33646696127 scopus 로고    scopus 로고
    • Enzymatic proteolysis, under high pressure of soybean whey: analysis of peptides and the allergen Gly m 1 in the hydrolysates
    • Peñas, E., Préstamo, G., Polo, F. & Gomez, R. (2006). Enzymatic proteolysis, under high pressure of soybean whey: analysis of peptides and the allergen Gly m 1 in the hydrolysates. Food Chemistry, 99, 569-573.
    • (2006) Food Chemistry , vol.99 , pp. 569-573
    • Peñas, E.1    Préstamo, G.2    Polo, F.3    Gomez, R.4
  • 100
    • 0036830145 scopus 로고    scopus 로고
    • A transient receptor potential channel expressed in taste receptor cells
    • Perez, C.A., Huang, L., Rong, M. et al. (2002). A transient receptor potential channel expressed in taste receptor cells. Nature Neuroscience, 5, 1169-1176.
    • (2002) Nature Neuroscience , vol.5 , pp. 1169-1176
    • Perez, C.A.1    Huang, L.2    Rong, M.3
  • 101
    • 0036712527 scopus 로고    scopus 로고
    • Hydrolysis of isoflavone glycosides to aglycones by β-glycosidase does not alter plasma and urine isoflavone pharmacokinetics in post-menopausal women
    • Richelle, M., Pridmore-Merten, S., Bodenstab, S., Enslen, M. & Offord, E.A. (2002). Hydrolysis of isoflavone glycosides to aglycones by β-glycosidase does not alter plasma and urine isoflavone pharmacokinetics in post-menopausal women. Journal of Nutrition, 132, 2587-2592.
    • (2002) Journal of Nutrition , vol.132 , pp. 2587-2592
    • Richelle, M.1    Pridmore-Merten, S.2    Bodenstab, S.3    Enslen, M.4    Offord, E.A.5
  • 102
    • 0029053161 scopus 로고
    • Coupling of bitter receptor to phosphodiesterase through transducin in taste receptor cells
    • Ruiz-Avila, L., McLaughlin, S.K., Wildman, D. et al. (1995). Coupling of bitter receptor to phosphodiesterase through transducin in taste receptor cells. Nature, 376, 80-85.
    • (1995) Nature , vol.376 , pp. 80-85
    • Ruiz-Avila, L.1    McLaughlin, S.K.2    Wildman, D.3
  • 103
    • 0034868610 scopus 로고    scopus 로고
    • Debittering of protein hydrolysates
    • Saha, B.C. & Hayashi, K. (2001). Debittering of protein hydrolysates. Biotechnology Advances., 5, 355-370.
    • (2001) Biotechnology Advances. , vol.5 , pp. 355-370
    • Saha, B.C.1    Hayashi, K.2
  • 104
    • 0036073599 scopus 로고    scopus 로고
    • Evidence for the lack of absorption of soy isoflavone glycosides in humans, supporting the crucial role of intestinal metabolism for bioavailability
    • Setchell, K.D.R., Brown, N.M., Zimmer-Nechemias, L. et al. (2002). Evidence for the lack of absorption of soy isoflavone glycosides in humans, supporting the crucial role of intestinal metabolism for bioavailability. American Journal of Clinical Nutrition, 76, 447-453.
    • (2002) American Journal of Clinical Nutrition , vol.76 , pp. 447-453
    • Setchell, K.D.R.1    Brown, N.M.2    Zimmer-Nechemias, L.3
  • 106
  • 107
    • 0030078033 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on enzymatic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin
    • Stapelfeldt, H., Petersen, P.H., Kristiansen, K.R., Qvist, K.B. & Skibsted, L.H. (1996). Effect of high hydrostatic pressure on enzymatic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin. Journal of Dairy Research, 6, 111-118.
    • (1996) Journal of Dairy Research , vol.6 , pp. 111-118
    • Stapelfeldt, H.1    Petersen, P.H.2    Kristiansen, K.R.3    Qvist, K.B.4    Skibsted, L.H.5
  • 109
    • 1542380567 scopus 로고    scopus 로고
    • Enzymic modification of extruded soy protein concentrates as a method of obtaining new functional food components
    • Surówka, K., Zmudziński, D. & Surówka, J. (2004b). Enzymic modification of extruded soy protein concentrates as a method of obtaining new functional food components. Trends in Food Science & Technology, 15, 153-160.
    • (2004) Trends in Food Science & Technology , vol.15 , pp. 153-160
    • Surówka, K.1    Zmudziński, D.2    Surówka, J.3
  • 111
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. A straight forward fractionation and their characterization
    • Thanh, V.H. & Shibasaki, K. (1976). Major proteins of soybean seeds. A straight forward fractionation and their characterization. Journal of Agricultural and Food Chemistry, 24, 1117-1121.
    • (1976) Journal of Agricultural and Food Chemistry , vol.24 , pp. 1117-1121
    • Thanh, V.H.1    Shibasaki, K.2
  • 112
    • 43649086418 scopus 로고    scopus 로고
    • Sensomics mapping and identification of the key bitter metabolites in Gouda cheese
    • Toelstede, S. & Hofmann, T. (2008). Sensomics mapping and identification of the key bitter metabolites in Gouda cheese. Journal of Agricultural and Food Chemistry, 56, 2795-2804.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 2795-2804
    • Toelstede, S.1    Hofmann, T.2
  • 113
    • 0036812272 scopus 로고    scopus 로고
    • Enzymatic transformation of isoflavone phytoestrogens in soymilk by β-glucosidase producing bifidobacteria
    • Tsangalis, D., Ashton, J.F., McGill, A.E.J. & Shah, N.P. (2002). Enzymatic transformation of isoflavone phytoestrogens in soymilk by β-glucosidase producing bifidobacteria. Journal of Food Science, 67, 3104-3113.
    • (2002) Journal of Food Science , vol.67 , pp. 3104-3113
    • Tsangalis, D.1    Ashton, J.F.2    McGill, A.E.J.3    Shah, N.P.4
  • 114
    • 0141448749 scopus 로고    scopus 로고
    • Biotransformation of isoflavones by bifidobacteria in fermented soymilk supplemented with D-glucose and L-cysteine
    • Tsangalis, D., Ashton, J.F., McGill, A.E.J. & Shah, N.P. (2003). Biotransformation of isoflavones by bifidobacteria in fermented soymilk supplemented with D-glucose and L-cysteine. Journal of Food Science, 68, 623-631.
    • (2003) Journal of Food Science , vol.68 , pp. 623-631
    • Tsangalis, D.1    Ashton, J.F.2    McGill, A.E.J.3    Shah, N.P.4
  • 115
    • 1942470443 scopus 로고    scopus 로고
    • Development of an isoflavone aglycone-enriched soymilk using soy germ, soy protein isolate and bifidobacteria
    • Tsangalis, D., Ashton, J.F., Stojanovska, L., Wilcox, G. & Shah, N.P. (2004). Development of an isoflavone aglycone-enriched soymilk using soy germ, soy protein isolate and bifidobacteria. Food Research International, 37, 301-312.
    • (2004) Food Research International , vol.37 , pp. 301-312
    • Tsangalis, D.1    Ashton, J.F.2    Stojanovska, L.3    Wilcox, G.4    Shah, N.P.5
  • 116
    • 77950574364 scopus 로고    scopus 로고
    • Enhancing the anti-adipogenic activity of soy protein by limited hydrolysis with Flavourzyme and ultrafiltration
    • Tsou, M.J., Kao, F.J., Tseng, C.K. & Chiang, W.D. (2010). Enhancing the anti-adipogenic activity of soy protein by limited hydrolysis with Flavourzyme and ultrafiltration. Food Chemistry, 122, 243-248.
    • (2010) Food Chemistry , vol.122 , pp. 243-248
    • Tsou, M.J.1    Kao, F.J.2    Tseng, C.K.3    Chiang, W.D.4
  • 118
    • 0141832166 scopus 로고    scopus 로고
    • Bioactive isoflavones in functional foods: the importance of gut microflora on bioavailability
    • Turner, N.J., Thomson, B.M. & Shaw, I.C. (2003). Bioactive isoflavones in functional foods: the importance of gut microflora on bioavailability. Nutrition Reviews, 61, 204-213.
    • (2003) Nutrition Reviews , vol.61 , pp. 204-213
    • Turner, N.J.1    Thomson, B.M.2    Shaw, I.C.3
  • 119
    • 0042739015 scopus 로고    scopus 로고
    • Functional interaction between T2R taste receptors and G-protein α subunits expressed in taste receptor cells
    • Ueda, T., Ugawa, S., Yamamura, H., Imaizumi, Y. & Shimada, S. (2003). Functional interaction between T2R taste receptors and G-protein α subunits expressed in taste receptor cells. The Journal of Neuroscience, 23, 7376-7380.
    • (2003) The Journal of Neuroscience , vol.23 , pp. 7376-7380
    • Ueda, T.1    Ugawa, S.2    Yamamura, H.3    Imaizumi, Y.4    Shimada, S.5
  • 120
    • 85052678887 scopus 로고    scopus 로고
    • Structure-function relationships of soy proteins
    • In: (edited by S. Damodaran & A. Paraf). New York: Marcel Dekker.
    • Utsumi, S., Matsumura, Y. & Mori, T. (1997). Structure-function relationships of soy proteins. In: Food Proteins and Their Applications (edited by S. Damodaran & A. Paraf). Pp. 257-291. New York: Marcel Dekker.
    • (1997) Food Proteins and Their Applications , pp. 257-291
    • Utsumi, S.1    Matsumura, Y.2    Mori, T.3
  • 122
    • 0033852356 scopus 로고    scopus 로고
    • Relation between solubility and surface aromatic hydrophobicity as an indicator of modification during preparation processes of commercial and laboratory prepared soy protein isolates
    • Wagner, J.R., Sorgentini, D.A. & Añón, M.C. (2000). Relation between solubility and surface aromatic hydrophobicity as an indicator of modification during preparation processes of commercial and laboratory prepared soy protein isolates. Journal of Agricultural and Food Chemistry, 48, 3159-3165.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 3159-3165
    • Wagner, J.R.1    Sorgentini, D.A.2    Añón, M.C.3
  • 123
    • 0037861889 scopus 로고    scopus 로고
    • Modification of the nitrogen solubility properties of soy protein isolate following proteolysis and transglutaminase cross-linking
    • Walsh, D.J., Cleary, D., McCarthy, E., Murphy, S. & FitzGerald, R.J. (2003). Modification of the nitrogen solubility properties of soy protein isolate following proteolysis and transglutaminase cross-linking. Food Research International, 36, 677-683.
    • (2003) Food Research International , vol.36 , pp. 677-683
    • Walsh, D.J.1    Cleary, D.2    McCarthy, E.3    Murphy, S.4    FitzGerald, R.J.5
  • 125
    • 34248396839 scopus 로고    scopus 로고
    • Using of Lactobacillus and Bifidobacterium to product the isoflavone aglycones in fermented soymilk
    • Wei, Q.K., Chen, T.R. & Chen, J.T. (2007). Using of Lactobacillus and Bifidobacterium to product the isoflavone aglycones in fermented soymilk. International Journal of Food Microbiology, 117, 120-124.
    • (2007) International Journal of Food Microbiology , vol.117 , pp. 120-124
    • Wei, Q.K.1    Chen, T.R.2    Chen, J.T.3
  • 126
    • 81255134983 scopus 로고    scopus 로고
    • Control of bitterness in enzymatic hydrolysis of protein
    • Xu, Y.H. (1997). Control of bitterness in enzymatic hydrolysis of protein. Shipin Gongye Keji, 3, 1-3.
    • (1997) Shipin Gongye Keji , vol.3 , pp. 1-3
    • Xu, Y.H.1
  • 127
    • 0012262764 scopus 로고
    • Soy protein hydrolysate debittering by lysine-acetylation
    • Yeom, H.W., Kim, K.S. & Rhee, J.S. (1994). Soy protein hydrolysate debittering by lysine-acetylation. Journal of Food Science, 59, 1123-1126.
    • (1994) Journal of Food Science , vol.59 , pp. 1123-1126
    • Yeom, H.W.1    Kim, K.S.2    Rhee, J.S.3
  • 128
    • 0037423367 scopus 로고    scopus 로고
    • Coding of sweet, bitter, and umami tastes: different receptor cells sharing similar signaling pathways
    • Zhang, Y., Hoon, M.A., Chandrashekar, J. et al. (2003). Coding of sweet, bitter, and umami tastes: different receptor cells sharing similar signaling pathways. Cell, 112, 293-301.
    • (2003) Cell , vol.112 , pp. 293-301
    • Zhang, Y.1    Hoon, M.A.2    Chandrashekar, J.3
  • 129
    • 68949101211 scopus 로고    scopus 로고
    • Limited hydrolysis of soybean protein concentrate and isolate with two proteases and the impact on emulsifying activity index of hydrolysates
    • Zhao, X.H. & Hou, Y. (2009). Limited hydrolysis of soybean protein concentrate and isolate with two proteases and the impact on emulsifying activity index of hydrolysates. African Journal of Biotechnology, 8, 3314-3319.
    • (2009) African Journal of Biotechnology , vol.8 , pp. 3314-3319
    • Zhao, X.H.1    Hou, Y.2
  • 130
    • 0025223230 scopus 로고
    • Efficiency of enteral nitrogen support in surgical patients: small peptides vs. non-degraded proteins
    • Ziegler, F., Ollivier, J.M., Cynober, L. et al. (1990). Efficiency of enteral nitrogen support in surgical patients: small peptides vs. non-degraded proteins. Gut, 31, 1277-1283.
    • (1990) Gut , vol.31 , pp. 1277-1283
    • Ziegler, F.1    Ollivier, J.M.2    Cynober, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.