메뉴 건너뛰기




Volumn 42, Issue 2, 2008, Pages 227-236

Protein hydrolysates: Processes and applications;Hidrolizados de proteína: Procesos y aplicaciones

Author keywords

Characterization; Degree of hydrolysis; Enzymatic hydrolysis; Proteases; Proteins

Indexed keywords


EID: 57349155357     PISSN: 03252957     EISSN: 03252957     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (65)

References (60)
  • 1
    • 34548487814 scopus 로고    scopus 로고
    • Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate
    • Yin S, Tang C, Cao J, Hu E, Wen Q, Yang X. Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate. Food Chem 2008; 106 (3): 1004-13.
    • (2008) Food Chem , vol.106 , Issue.3 , pp. 1004-1013
    • Yin, S.1    Tang, C.2    Cao, J.3    Hu, E.4    Wen, Q.5    Yang, X.6
  • 2
    • 33748323487 scopus 로고    scopus 로고
    • Enzymatic preparation and functional properties of wheat gluten hydrolysates
    • Kong X, Zhou H, Qian H. Enzymatic preparation and functional properties of wheat gluten hydrolysates. Food Chem 2007; 101 (2): 615-20.
    • (2007) Food Chem , vol.101 , Issue.2 , pp. 615-620
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 3
    • 33846230958 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates
    • Kong X, Zhou H, Qian H. Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates. Food Chem 2007; 102 (3): 759-63.
    • (2007) Food Chem , vol.102 , Issue.3 , pp. 759-763
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 4
    • 34547900269 scopus 로고    scopus 로고
    • Hydrophobicity, solubility, and emulsifying properties of enzyme-modified rice endosperm protein
    • Paraman I, Hettiarachchy NS, Schaefer C, Beck MI. Hydrophobicity, solubility, and emulsifying properties of enzyme-modified rice endosperm protein. Cereal Chem 2007; 84 (4): 343-9.
    • (2007) Cereal Chem , vol.84 , Issue.4 , pp. 343-349
    • Paraman, I.1    Hettiarachchy, N.S.2    Schaefer, C.3    Beck, M.I.4
  • 6
    • 0020682841 scopus 로고
    • Impact of development of the gastrointestinal tract on infant feeding
    • Lebenthal E, Lee PC, Heittinger LA. Impact of development of the gastrointestinal tract on infant feeding. J Pediatr 1983; 102: 1-9.
    • (1983) J Pediatr , vol.102 , pp. 1-9
    • Lebenthal, E.1    Lee, P.C.2    Heittinger, L.A.3
  • 7
    • 0018318768 scopus 로고
    • The influence of peptide chain length on taste and functional properties of enzymatically modified soy protein
    • Adler-Nissen J, Olsen HS. The influence of peptide chain length on taste and functional properties of enzymatically modified soy protein. ACS Symp Ser 1979; 92: 125-46.
    • (1979) ACS Symp Ser , vol.92 , pp. 125-146
    • Adler-Nissen, J.1    Olsen, H.S.2
  • 8
    • 35448999201 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease
    • Bhaskar N, Benila T, Radha C, Lalitha RG. Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease. Biores Technol 2008; 99(2): 335-43.
    • (2008) Biores Technol , vol.99 , Issue.2 , pp. 335-343
    • Bhaskar, N.1    Benila, T.2    Radha, C.3    Lalitha, R.G.4
  • 9
    • 34548514878 scopus 로고    scopus 로고
    • Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from Silybum marianum flowers
    • Vairo-Cavalli S, Silva SV, Cimino C, Malcata FX, Priolo N. Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from Silybum marianum flowers. Food Chem 2008; 106 (3): 997-1003.
    • (2008) Food Chem , vol.106 , Issue.3 , pp. 997-1003
    • Vairo-Cavalli, S.1    Silva, S.V.2    Cimino, C.3    Malcata, F.X.4    Priolo, N.5
  • 10
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang J, Zhao M, Yang X, Jiang Y. Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. J Cereal Sci 2006; 44(1): 93-100.
    • (2006) J Cereal Sci , vol.44 , Issue.1 , pp. 93-100
    • Wang, J.1    Zhao, M.2    Yang, X.3    Jiang, Y.4
  • 11
    • 35549005384 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of Brewers' spent grain proteins and techno functional properties of the resulting hydrolysates
    • Celus I, Brijs K, Delcour JA. Enzymatic hydrolysis of Brewers' spent grain proteins and techno functional properties of the resulting hydrolysates. J Agric Food Chem 2007; 55 (21): 8703-10.
    • (2007) J Agric Food Chem , vol.55 , Issue.21 , pp. 8703-8710
    • Celus, I.1    Brijs, K.2    Delcour, J.A.3
  • 12
    • 33847311237 scopus 로고    scopus 로고
    • An improvement of potato pulp protein hydrolyzation process by the combination of protease enzyme systems
    • Kamnerdpetch C, Weiss M, Kasper C, Scheper T. An improvement of potato pulp protein hydrolyzation process by the combination of protease enzyme systems. Enzyme Microb Technol 2007; 40(4): 508-14.
    • (2007) Enzyme Microb Technol , vol.40 , Issue.4 , pp. 508-514
    • Kamnerdpetch, C.1    Weiss, M.2    Kasper, C.3    Scheper, T.4
  • 13
    • 57349088404 scopus 로고    scopus 로고
    • Caessens PWJR. Enzymatic hydrolysis of ß-casein and β-lactoglobulin. Foam and emulsion properties of peptides in relation to their molecular structure. Ph D Thesis, Wageningen Agricultural University, The Netherlands 1999.
    • Caessens PWJR. Enzymatic hydrolysis of ß-casein and β-lactoglobulin. Foam and emulsion properties of peptides in relation to their molecular structure. Ph D Thesis, Wageningen Agricultural University, The Netherlands 1999.
  • 14
    • 0029398314 scopus 로고
    • Susceptibility of beta-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin
    • Guo MR, Fox PF, Flynn A, Kindstedt PS. Susceptibility of beta-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. J Dairy Sci 1995; 78: 2336-44.
    • (1995) J Dairy Sci , vol.78 , pp. 2336-2344
    • Guo, M.R.1    Fox, P.F.2    Flynn, A.3    Kindstedt, P.S.4
  • 15
    • 33749342431 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of protein: Mechanism and kinetic model
    • Qi W, He Z. Enzymatic hydrolysis of protein: Mechanism and kinetic model. Front Chem China 2006; 1 (3): 308-14.
    • (2006) Front Chem China , vol.1 , Issue.3 , pp. 308-314
    • Qi, W.1    He, Z.2
  • 16
    • 0000505579 scopus 로고
    • Proteases
    • Nagodawithana T, Reed G, Eds, San Diego USA, Academic Press;
    • Adler-Nissen J. Proteases. In: Nagodawithana T, Reed G, Eds. Enzymes in food processing. San Diego (USA): Academic Press; 1993. p. 159-203.
    • (1993) Enzymes in food processing , pp. 159-203
    • Adler-Nissen, J.1
  • 19
    • 0031453033 scopus 로고    scopus 로고
    • Hydrolysis of β-lactoglobulin by tour different proteinases monitored by capillary electrophoresis and high performance liquid chromatography
    • Madsen JS, Ahmt TO, Halkier T, Qvist KB. Hydrolysis of β-lactoglobulin by tour different proteinases monitored by capillary electrophoresis and high performance liquid chromatography. Int Dairy J 1997; 7: 399-409.
    • (1997) Int Dairy J , vol.7 , pp. 399-409
    • Madsen, J.S.1    Ahmt, T.O.2    Halkier, T.3    Qvist, K.B.4
  • 21
    • 0030762638 scopus 로고    scopus 로고
    • Empirical kinetic models for tryptic whey protein hydrolysis
    • Margot A, Flaschel E, Renken A. Empirical kinetic models for tryptic whey protein hydrolysis. Process Biochem 1997; 32 (3): 217-23.
    • (1997) Process Biochem , vol.32 , Issue.3 , pp. 217-223
    • Margot, A.1    Flaschel, E.2    Renken, A.3
  • 22
    • 0032829926 scopus 로고    scopus 로고
    • β-Lactoglobulin hydrolysis. II. Peptide identification, SH/SS exchange, and functional properties of hydrolysate fractions formed by the action of plasmin
    • Caessens PWJR, Daamen WF, Gruppen H, Visser S, Voragen AGJ. β-Lactoglobulin hydrolysis. II. Peptide identification, SH/SS exchange, and functional properties of hydrolysate fractions formed by the action of plasmin. J Agric Food Chem 1999; 47: 2980-90.
    • (1999) J Agric Food Chem , vol.47 , pp. 2980-2990
    • Caessens, P.W.J.R.1    Daamen, W.F.2    Gruppen, H.3    Visser, S.4    Voragen, A.G.J.5
  • 23
    • 0028526893 scopus 로고
    • Physicochemical and functional properties of protein hydrolysates in nutricional products
    • Mahmoud MI. Physicochemical and functional properties of protein hydrolysates in nutricional products. Food Technol 1994; 48: 89-5.
    • (1994) Food Technol , vol.48 , pp. 89-95
    • Mahmoud, M.I.1
  • 25
    • 0030972073 scopus 로고    scopus 로고
    • Functional and immunological properties of casein hydrolysate produced from a two-stage membrane system
    • Lin SB, Chiang W, Cordle C, Thomas RL. Functional and immunological properties of casein hydrolysate produced from a two-stage membrane system. J Food Sci 1997; 62: 480-3.
    • (1997) J Food Sci , vol.62 , pp. 480-483
    • Lin, S.B.1    Chiang, W.2    Cordle, C.3    Thomas, R.L.4
  • 26
    • 13844320199 scopus 로고    scopus 로고
    • Characteristics of protein fractions generated from hydrolysed cod (Gadus morhua) by-products
    • Sliy̌tǎ R, Daukǎsa E, Falch E, Storrø I, Rustad T. Characteristics of protein fractions generated from hydrolysed cod (Gadus morhua) by-products. Process Biochem 2005; 40 (6): 2021-33.
    • (2005) Process Biochem , vol.40 , Issue.6 , pp. 2021-2033
    • Sliy̌tǎ, R.1    Daukǎsa, E.2    Falch, E.3    Storrø, I.4    Rustad, T.5
  • 27
    • 4344590553 scopus 로고    scopus 로고
    • Separation of calcium-binding protein derived from enzymatic hydrolysates of cheese whey protein
    • Kim SB, Shin HS, Lim JW. Separation of calcium-binding protein derived from enzymatic hydrolysates of cheese whey protein. Asian-Australas. J Anim Sci 2004; 17 (5): 712-8.
    • (2004) Asian-Australas. J Anim Sci , vol.17 , Issue.5 , pp. 712-718
    • Kim, S.B.1    Shin, H.S.2    Lim, J.W.3
  • 28
    • 57349083741 scopus 로고    scopus 로고
    • Novo Industrias. Determination of neutrase using the Anson Hemoglobin Method. Analytical Method. EB-SM-0348.01/01, 2001.
    • Novo Industrias. Determination of neutrase using the Anson Hemoglobin Method. Analytical Method. EB-SM-0348.01/01, 2001.
  • 29
    • 57349140563 scopus 로고    scopus 로고
    • A.O.A.C. Official Methods of Analysis of A.O.A.C International 18th ed., A.O.A.C International, Gaithersburg, MD, USA 2005.
    • A.O.A.C. Official Methods of Analysis of A.O.A.C International 18th ed., A.O.A.C International, Gaithersburg, MD, USA 2005.
  • 30
    • 0032127664 scopus 로고    scopus 로고
    • Determination of alpha-amino nitrogen in pea protein hydrolysates: A comparison of three analytical methods
    • Panasiuk R, Amarowicz R, Kostyra H, Sijtsma L. Determination of alpha-amino nitrogen in pea protein hydrolysates: a comparison of three analytical methods. Food Chem 1998; 62: 363-7.
    • (1998) Food Chem , vol.62 , pp. 363-367
    • Panasiuk, R.1    Amarowicz, R.2    Kostyra, H.3    Sijtsma, L.4
  • 32
    • 0010845331 scopus 로고
    • Relative tryptic digestion rates of food proteins
    • Hung ND, Vas M, Cheke E, Bolcsi SZA. Relative tryptic digestion rates of food proteins. J Food Sci 1984; 49: 1535-42.
    • (1984) J Food Sci , vol.49 , pp. 1535-1542
    • Hung, N.D.1    Vas, M.2    Cheke, E.3    Bolcsi, S.Z.A.4
  • 33
    • 0034927188 scopus 로고    scopus 로고
    • Correlation of base consumption with the degree of hydrolysis in enzymic protein hydrolysis
    • Camacho F, Gonzalez-Tello P, Paez-Duenas MP, Guadiz EM, Guadix A. Correlation of base consumption with the degree of hydrolysis in enzymic protein hydrolysis. J Dairy Res 2001; 68: 251-65.
    • (2001) J Dairy Res , vol.68 , pp. 251-265
    • Camacho, F.1    Gonzalez-Tello, P.2    Paez-Duenas, M.P.3    Guadiz, E.M.4    Guadix, A.5
  • 34
    • 0002541525 scopus 로고
    • Relationship of structure to taste of peptides and peptide mixtures
    • Feeney RE, Whitaker JR, Eds, New York: M Dekker;
    • Adler-Nissen J. Relationship of structure to taste of peptides and peptide mixtures. In: Feeney RE, Whitaker JR, Eds. Protein tailoring for food and medical uses. New York: M Dekker; 1986. p. 97-122.
    • (1986) Protein tailoring for food and medical uses , pp. 97-122
    • Adler-Nissen, J.1
  • 36
    • 0031429629 scopus 로고    scopus 로고
    • Characterisation of a new chromatography matrix for peptide molecular mass determination
    • Smyth M, Fitzgerald RJ. Characterisation of a new chromatography matrix for peptide molecular mass determination. Int Dairy J 1997; 7: 571-7.
    • (1997) Int Dairy J , vol.7 , pp. 571-577
    • Smyth, M.1    Fitzgerald, R.J.2
  • 37
    • 0031588729 scopus 로고    scopus 로고
    • Determination of molecular-mass distribution of food-grade protein hydrolyzates by size-exclusion chromatography and chemiluminescent nitrogen detection
    • Fujinari EM, Manes JD. Determination of molecular-mass distribution of food-grade protein hydrolyzates by size-exclusion chromatography and chemiluminescent nitrogen detection. J Chromatogr A 1997; 763: 323-9.
    • (1997) J Chromatogr A , vol.763 , pp. 323-329
    • Fujinari, E.M.1    Manes, J.D.2
  • 38
    • 35448990075 scopus 로고    scopus 로고
    • Pancreatic hydrolysis of bovine casein: Changes in the aggregate size and molecular weight distribution
    • Zu R, He Z, Qi W. Pancreatic hydrolysis of bovine casein: Changes in the aggregate size and molecular weight distribution. Food chem 2008; 107 (1): 151-7.
    • (2008) Food chem , vol.107 , Issue.1 , pp. 151-157
    • Zu, R.1    He, Z.2    Qi, W.3
  • 39
    • 0037292844 scopus 로고    scopus 로고
    • Product distribution of casein tryptic hydrolysis based on HPSEC analysis and molecular mechanism
    • Qi W, He Z, Shi D. Product distribution of casein tryptic hydrolysis based on HPSEC analysis and molecular mechanism. Chem Eng Sci 2003; 58 (3-6): 767-75.
    • (2003) Chem Eng Sci , vol.58 , Issue.3-6 , pp. 767-775
    • Qi, W.1    He, Z.2    Shi, D.3
  • 41
    • 0023927159 scopus 로고
    • High performance liquid chromatography of amino acids, peptides and proteins. LXXXV: Evaluation of the use of hydrophobicity coefficients for prediction of peptide elution profiles
    • Hearn MTW, Aguilar MI, Mant C, Hodges RS. High performance liquid chromatography of amino acids, peptides and proteins. LXXXV: Evaluation of the use of hydrophobicity coefficients for prediction of peptide elution profiles. J Chromatogr 1988; 438: 197-210.
    • (1988) J Chromatogr , vol.438 , pp. 197-210
    • Hearn, M.T.W.1    Aguilar, M.I.2    Mant, C.3    Hodges, R.S.4
  • 42
    • 0026538267 scopus 로고
    • Prediction of peptide retention time in reversed-phase high-performance liquid chromatography
    • Chabanet C, Yvon M. Prediction of peptide retention time in reversed-phase high-performance liquid chromatography. J Chromatogr 1992; 599: 211-25.
    • (1992) J Chromatogr , vol.599 , pp. 211-225
    • Chabanet, C.1    Yvon, M.2
  • 43
    • 57349171058 scopus 로고    scopus 로고
    • Industrial enzymes and their applications
    • Uhlig H. Industrial enzymes and their applications. New York: Wiley and S; 1998.
    • (1998) New York: Wiley and S
    • Uhlig, H.1
  • 44
    • 9644260726 scopus 로고    scopus 로고
    • Yield and composition of different fractions obtained after enzymatic hydrolysis of cod (Gadus morhua) by-products
    • Sliy̌tǎ R, Daukǎsa E, Falch E, Storrø I, Rustad T. Yield and composition of different fractions obtained after enzymatic hydrolysis of cod (Gadus morhua) by-products. Process Biochem 2005; 40 (3-4): 1415-24.
    • (2005) Process Biochem , vol.40 , Issue.3-4 , pp. 1415-1424
    • Sliy̌tǎ, R.1    Daukǎsa, E.2    Falch, E.3    Storrø, I.4    Rustad, T.5
  • 45
    • 0024315816 scopus 로고
    • Application of reversed-phase high-performance liquid chromatography to separation of peptides from phosphorylated and dephosphorylated casein hydrolysates
    • Lemieux L, Amiot J. Application of reversed-phase high-performance liquid chromatography to separation of peptides from phosphorylated and dephosphorylated casein hydrolysates. J Chromatogr 1989; 73: 189-206.
    • (1989) J Chromatogr , vol.73 , pp. 189-206
    • Lemieux, L.1    Amiot, J.2
  • 46
    • 0025613127 scopus 로고
    • Efficiency of five chromatographic systems for the separation of casein digest
    • Lemieux L, Amiot J. Efficiency of five chromatographic systems for the separation of casein digest. J Liq Chromatogr 1990; 13: 4023-35.
    • (1990) J Liq Chromatogr , vol.13 , pp. 4023-4035
    • Lemieux, L.1    Amiot, J.2
  • 47
    • 22244490000 scopus 로고    scopus 로고
    • Characterization of physicochemical and functional behavior of enzymatically modified spray dried whey protein concentrate
    • Jayaprakasha HM, Yoon YC. Characterization of physicochemical and functional behavior of enzymatically modified spray dried whey protein concentrate. Milchwissenschaft 2005; 60 (3): 305-9.
    • (2005) Milchwissenschaft , vol.60 , Issue.3 , pp. 305-309
    • Jayaprakasha, H.M.1    Yoon, Y.C.2
  • 48
    • 0031834602 scopus 로고    scopus 로고
    • Functional properties and bitterness of sodium caseinate hydrolysatesprepared with a Bacillus proteinase
    • Slattery H, Fitzgerald RJ. Functional properties and bitterness of sodium caseinate hydrolysatesprepared with a Bacillus proteinase. J Food Sci 1998; 63: 418-22.
    • (1998) J Food Sci , vol.63 , pp. 418-422
    • Slattery, H.1    Fitzgerald, R.J.2
  • 49
    • 57349153331 scopus 로고    scopus 로고
    • Svenning C, Molland T, Langsrud T, Vegarud GE. A characterization study of peptides derived from casein proteolysis. In: IDF, Ed. Protein and fat globule modifications by heat treatment, homogenisation and other technological means for high quality dairy products: Proceedings of the IDF seminar held in Munich. Sonthofen (Germany): International Dairy Federation; 1993. p. 96-105.
    • Svenning C, Molland T, Langsrud T, Vegarud GE. A characterization study of peptides derived from casein proteolysis. In: IDF, Ed. Protein and fat globule modifications by heat treatment, homogenisation and other technological means for high quality dairy products: Proceedings of the IDF seminar held in Munich. Sonthofen (Germany): International Dairy Federation; 1993. p. 96-105.
  • 50
    • 34249088376 scopus 로고    scopus 로고
    • Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin
    • Wasswa J, Tang J, Gu X, Yuan X. Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin. Food Chem 2007; 104 (4): 1698-704.
    • (2007) Food Chem , vol.104 , Issue.4 , pp. 1698-1704
    • Wasswa, J.1    Tang, J.2    Gu, X.3    Yuan, X.4
  • 51
    • 33847028271 scopus 로고    scopus 로고
    • Separation of iron-binding protein from whey through enzymatic hydrolysis
    • Kim SB, Seo IS, Khan MA, Ki KS, Nam MS, Kim HS. Separation of iron-binding protein from whey through enzymatic hydrolysis. Int Dairy J 2007; 17 (6): 625-31.
    • (2007) Int Dairy J , vol.17 , Issue.6 , pp. 625-631
    • Kim, S.B.1    Seo, I.S.2    Khan, M.A.3    Ki, K.S.4    Nam, M.S.5    Kim, H.S.6
  • 52
    • 36849058072 scopus 로고    scopus 로고
    • Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates
    • Li L, Yang ZY, Yang XQ, Zhang GH, Tang SZ, Chen F. Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates. J Ind Microbiol Biotechnol 2008; 35 (1): 41-7.
    • (2008) J Ind Microbiol Biotechnol , vol.35 , Issue.1 , pp. 41-47
    • Li, L.1    Yang, Z.Y.2    Yang, X.Q.3    Zhang, G.H.4    Tang, S.Z.5    Chen, F.6
  • 53
    • 35348862011 scopus 로고    scopus 로고
    • Physicochemical and bitterness properties of enzymatic pea protein hydrolysates
    • Humiski LM, Aluko RE. Physicochemical and bitterness properties of enzymatic pea protein hydrolysates. J Food Sci 2007; 72 (8): S605-11.
    • (2007) J Food Sci , vol.72 , Issue.8
    • Humiski, L.M.1    Aluko, R.E.2
  • 55
    • 0032193222 scopus 로고    scopus 로고
    • Assessment of sensory properties of cheese by near-infrared spectroscopy
    • Sorensen LK, Jepsen R. Assessment of sensory properties of cheese by near-infrared spectroscopy. Int Dairy J 1998; 8: 863-71.
    • (1998) Int Dairy J , vol.8 , pp. 863-871
    • Sorensen, L.K.1    Jepsen, R.2
  • 56
    • 33845280838 scopus 로고
    • Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin
    • Chobert J.M, Bertrand-Harb C, Nicolas M.G. Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J Agric Food Chem 1988; 36: 883-92.
    • (1988) J Agric Food Chem , vol.36 , pp. 883-892
    • Chobert, J.M.1    Bertrand-Harb, C.2    Nicolas, M.G.3
  • 57
    • 33847400444 scopus 로고    scopus 로고
    • Controlled enzymatic hydrolysis of glycinin: Susceptibility of acidic and basic subunits to proteolytic enzymes. LWT-Food
    • Govindaraju K, Srinivas H. Controlled enzymatic hydrolysis of glycinin: Susceptibility of acidic and basic subunits to proteolytic enzymes. LWT-Food Sci. Technol 2007; 40 (6): 1056-65.
    • (2007) Sci. Technol , vol.40 , Issue.6 , pp. 1056-1065
    • Govindaraju, K.1    Srinivas, H.2
  • 58
    • 33645115628 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of whey proteins by two different proteases and their effect on the functional properties of resulting protein hydrolysates
    • Severin S, Xia WS. Enzymatic hydrolysis of whey proteins by two different proteases and their effect on the functional properties of resulting protein hydrolysates. J Food Biochem 2006; 30 (1): 77-97.
    • (2006) J Food Biochem , vol.30 , Issue.1 , pp. 77-97
    • Severin, S.1    Xia, W.S.2
  • 59
    • 12344251713 scopus 로고    scopus 로고
    • Effect of limited hydrolysis of sunflower protein on the interactions with polysaccharides in foams
    • Martinez KD, Baeza RI, Millán NF, Pilosof AMR. Effect of limited hydrolysis of sunflower protein on the interactions with polysaccharides in foams. Food Hydrocolloids 2005; 19 (3): 361-9.
    • (2005) Food Hydrocolloids , vol.19 , Issue.3 , pp. 361-369
    • Martinez, K.D.1    Baeza, R.I.2    Millán, N.F.3    Pilosof, A.M.R.4
  • 60
    • 33645277077 scopus 로고    scopus 로고
    • Improvement of emulsifying properties of wheat gluten hydrolysate/I-carrageenan conjugates
    • Wang JS, Zhao MM, Yang XQ, Jiang YM. Improvement of emulsifying properties of wheat gluten hydrolysate/I-carrageenan conjugates. Food Technol Biotechnol 2006; 44 (1): 25-32.
    • (2006) Food Technol Biotechnol , vol.44 , Issue.1 , pp. 25-32
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3    Jiang, Y.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.