메뉴 건너뛰기




Volumn 54, Issue 2, 2013, Pages 1528-1534

Effect of pressure or temperature pretreatment of isolated pea protein on properties of the enzymatic hydrolysates

Author keywords

Alcalase; Angiotensin converting enzyme; High pressure pretreatment; Isolated pea protein (IPP); Protein hydrolysate; Renin

Indexed keywords

ALCALASE; ANGIOTENSIN-CONVERTING ENZYME; PEA PROTEINS; PRE-TREATMENT; PROTEIN HYDROLYSATE; RENIN;

EID: 84887001596     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2013.09.020     Document Type: Article
Times cited : (70)

References (34)
  • 1
    • 84867895162 scopus 로고    scopus 로고
    • Screening of whey protein isolate hydrolysates for their dual functionality: Influence of heat pre-treatment and enzyme specificity
    • Adjonu R., Doran G., Torley P., Agboola S. Screening of whey protein isolate hydrolysates for their dual functionality: Influence of heat pre-treatment and enzyme specificity. Food Chemistry 2013, 136:1435-1443.
    • (2013) Food Chemistry , vol.136 , pp. 1435-1443
    • Adjonu, R.1    Doran, G.2    Torley, P.3    Agboola, S.4
  • 2
    • 84877667238 scopus 로고    scopus 로고
    • Renin and angiotensin converting enzyme inhibition with antioxidant properties of African yam bean protein hydrolysate and reverse-phase HPLC-separated peptide fractions
    • Ajibola C.F., Fashakin J.B., Fagbemi T.N., Aluko R.E. Renin and angiotensin converting enzyme inhibition with antioxidant properties of African yam bean protein hydrolysate and reverse-phase HPLC-separated peptide fractions. Food Research International 2013, 52:437-444.
    • (2013) Food Research International , vol.52 , pp. 437-444
    • Ajibola, C.F.1    Fashakin, J.B.2    Fagbemi, T.N.3    Aluko, R.E.4
  • 3
    • 77955977361 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties and angiotensin I-converting enzyme-inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products
    • Balti R., Bougatef A., El-Hadj Ali N., Zekri D., Barkia A., Nasri M. Influence of degree of hydrolysis on functional properties and angiotensin I-converting enzyme-inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products. Journal of the Science of Food and Agriculture 2010, 90:2006-2014.
    • (2010) Journal of the Science of Food and Agriculture , vol.90 , pp. 2006-2014
    • Balti, R.1    Bougatef, A.2    El-Hadj Ali, N.3    Zekri, D.4    Barkia, A.5    Nasri, M.6
  • 4
    • 77949802114 scopus 로고    scopus 로고
    • Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins
    • Balti R., Nedjar-Arroume N., Adje E.Y., Guillochon D., Nasri M. Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins. Journal of Agricultural and Food Chemistry 2010, 58:3840-3846.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 3840-3846
    • Balti, R.1    Nedjar-Arroume, N.2    Adje, E.Y.3    Guillochon, D.4    Nasri, M.5
  • 5
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and microstructural studies of thermal denaturation and gelation of beta-lactoglobulins A and B
    • Boye J.I., Ma C.Y., Ismail A., Harwalkar V.R., Kalab M. Molecular and microstructural studies of thermal denaturation and gelation of beta-lactoglobulins A and B. Journal of Agricultural and Food Chemistry 1997, 45(5):1608-1618.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.5 , pp. 1608-1618
    • Boye, J.I.1    Ma, C.Y.2    Ismail, A.3    Harwalkar, V.R.4    Kalab, M.5
  • 7
    • 0031758168 scopus 로고    scopus 로고
    • Protein modification by thermal processing
    • Davis P.J., Williams S.C. Protein modification by thermal processing. Allergy 1998, 53:102-105.
    • (1998) Allergy , vol.53 , pp. 102-105
    • Davis, P.J.1    Williams, S.C.2
  • 8
  • 9
    • 0002102027 scopus 로고
    • The microbe as a high pressure target
    • Nottingham University Press, Loughborough, UK, D.A. Ledward, D.E. Johnston, R.G. Earnshaw, A.P.M. Hastings (Eds.)
    • Gould G.W. The microbe as a high pressure target. High pressure processing of foods 1995, 27-35. Nottingham University Press, Loughborough, UK. D.A. Ledward, D.E. Johnston, R.G. Earnshaw, A.P.M. Hastings (Eds.).
    • (1995) High pressure processing of foods , pp. 27-35
    • Gould, G.W.1
  • 10
    • 70449116398 scopus 로고    scopus 로고
    • Purification, activity and sequence of angiotensin I converting enzyme inhibitory peptide from alcalase hydrolysate of peanut flour
    • Guang C., Phillips R.D. Purification, activity and sequence of angiotensin I converting enzyme inhibitory peptide from alcalase hydrolysate of peanut flour. Journal of Agricultural and Food Chemistry 2009, 57:10102-10106.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 10102-10106
    • Guang, C.1    Phillips, R.D.2
  • 11
    • 67649185517 scopus 로고    scopus 로고
    • Plant food-derived angiotensin I converting enzyme inhibitory peptides
    • Guang C., Phillips R.D. Plant food-derived angiotensin I converting enzyme inhibitory peptides. Journal of Agricultural and Food Chemistry 2009, 57:5113-5120.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 5113-5120
    • Guang, C.1    Phillips, R.D.2
  • 12
    • 0018398672 scopus 로고
    • A continuous spectrophotometric assay for angiotensin converting enzyme
    • Holmquist B., Bunning P., Riordan J.F. A continuous spectrophotometric assay for angiotensin converting enzyme. Analytical Biochemistry 1979, 95:540-548.
    • (1979) Analytical Biochemistry , vol.95 , pp. 540-548
    • Holmquist, B.1    Bunning, P.2    Riordan, J.F.3
  • 14
    • 0035818615 scopus 로고    scopus 로고
    • Upregulation of phosphodiesterase 1A1 expression is associated with the development of nitrate tolerance
    • Kim D., Rybalkin S.D., Pi X., Wang Y., Zhang C., Munzel T., et al. Upregulation of phosphodiesterase 1A1 expression is associated with the development of nitrate tolerance. Circulation 2001, 104:2338-2343.
    • (2001) Circulation , vol.104 , pp. 2338-2343
    • Kim, D.1    Rybalkin, S.D.2    Pi, X.3    Wang, Y.4    Zhang, C.5    Munzel, T.6
  • 15
    • 0011513632 scopus 로고    scopus 로고
    • Process assessment of high pressure processing of foods: an overview
    • CRC Press, Boca Raton, FL, USA, F.A.R. Oliveira, J.C. Oliveira, D. Hendricks, D. Knorr, G.L.M. Gorris (Eds.)
    • Knorr D. Process assessment of high pressure processing of foods: an overview. Processing of foods: Quality optimization and process assessment 1999, 249-267. CRC Press, Boca Raton, FL, USA. F.A.R. Oliveira, J.C. Oliveira, D. Hendricks, D. Knorr, G.L.M. Gorris (Eds.).
    • (1999) Processing of foods: Quality optimization and process assessment , pp. 249-267
    • Knorr, D.1
  • 16
    • 34447629532 scopus 로고    scopus 로고
    • Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis
    • Kuipers B.J.H., Gruppen H. Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis. Journal of Agricultural and Food Chemistry 2007, 55:5445-5451.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 5445-5451
    • Kuipers, B.J.H.1    Gruppen, H.2
  • 17
    • 0001183694 scopus 로고
    • Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH
    • Lee S.-Y., Morr C.V., Ha E.Y.W. Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH. Journal of Food Science 1992, 57:1210-1229.
    • (1992) Journal of Food Science , vol.57 , pp. 1210-1229
    • Lee, S.-Y.1    Morr, C.V.2    Ha, E.Y.W.3
  • 18
    • 78149344550 scopus 로고    scopus 로고
    • Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate
    • Li H., Aluko R.E. Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate. Journal of Agricultural and Food Chemistry 2010, 58:11471-11476.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 11471-11476
    • Li, H.1    Aluko, R.E.2
  • 19
    • 33747231180 scopus 로고    scopus 로고
    • Novel angiotensin I-converting enzyme inhibitory peptides isolated from alcalase hydrolysate of mung bean protein
    • Li G.H., Wan J.Z., Le G.W., Shi Y.H. Novel angiotensin I-converting enzyme inhibitory peptides isolated from alcalase hydrolysate of mung bean protein. Journal of Peptide Science 2006, 12:509-514.
    • (2006) Journal of Peptide Science , vol.12 , pp. 509-514
    • Li, G.H.1    Wan, J.Z.2    Le, G.W.3    Shi, Y.H.4
  • 20
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and in protein samples
    • Markwell M.A., Hass S.M., Bieber L.L., Tolbert N.E. A modification of the Lowry procedure to simplify protein determination in membrane and in protein samples. Analytical Biochemistry 1978, 87:206-210.
    • (1978) Analytical Biochemistry , vol.87 , pp. 206-210
    • Markwell, M.A.1    Hass, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 21
    • 84886993833 scopus 로고
    • Process for preparing products from legumes. Canadian Patent, 1104871.
    • Nickel, G. B. (1981). Process for preparing products from legumes. Canadian Patent, 1104871.
    • (1981)
    • Nickel, G.B.1
  • 22
    • 0037290864 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on the steady-state kinetics of tryptic hydrolysis of β-lactoglobulin
    • Olsen K., Kristiansen K.R., Skibsted L.H. Effect of high hydrostatic pressure on the steady-state kinetics of tryptic hydrolysis of β-lactoglobulin. Food Chemistry 2003, 80:235-260.
    • (2003) Food Chemistry , vol.80 , pp. 235-260
    • Olsen, K.1    Kristiansen, K.R.2    Skibsted, L.H.3
  • 23
    • 0017413556 scopus 로고    scopus 로고
    • Renin-angiotensin system: biochemistry and mechanisms of action
    • Peach M.J. Renin-angiotensin system: biochemistry and mechanisms of action. Physiological Reviews 1997, 57:313-370.
    • (1997) Physiological Reviews , vol.57 , pp. 313-370
    • Peach, M.J.1
  • 24
    • 0942278928 scopus 로고    scopus 로고
    • High pressure and the enzymatic hydrolysis of soybean whey proteins
    • Penas E., Prestamo G., Gomez R. High pressure and the enzymatic hydrolysis of soybean whey proteins. Food Chemistry 2004, 85:641-648.
    • (2004) Food Chemistry , vol.85 , pp. 641-648
    • Penas, E.1    Prestamo, G.2    Gomez, R.3
  • 26
    • 0000722070 scopus 로고
    • Spectra methods of characterizing protein conformation and conformational changes
    • IRL Press, Oxford, T.E. Creighton (Ed.)
    • Schmid F.X. Spectra methods of characterizing protein conformation and conformational changes. Protein structure: A practical approach 1989, 251-285. IRL Press, Oxford. T.E. Creighton (Ed.).
    • (1989) Protein structure: A practical approach , pp. 251-285
    • Schmid, F.X.1
  • 27
    • 55949132286 scopus 로고    scopus 로고
    • Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study
    • Tang C.-H., Chen L., Ma C.-Y. Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study. Food Chemistry 2009, 113:957-963.
    • (2009) Food Chemistry , vol.113 , pp. 957-963
    • Tang, C.-H.1    Chen, L.2    Ma, C.-Y.3
  • 28
    • 84856784002 scopus 로고    scopus 로고
    • Multifunctional cationic peptide fractions from flaxseed protein hydrolysates
    • Udenigwe C.C., Aluko R.E. Multifunctional cationic peptide fractions from flaxseed protein hydrolysates. Plant Foods for Human Nutrition 2012, 67:1-9.
    • (2012) Plant Foods for Human Nutrition , vol.67 , pp. 1-9
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 29
    • 84862684869 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship modeling of renin-inhibiting dipeptides
    • Udenigwe C.C., Li H., Aluko R.E. Quantitative structure-activity relationship modeling of renin-inhibiting dipeptides. Amino Acids 2012, 42:1379-1386.
    • (2012) Amino Acids , vol.42 , pp. 1379-1386
    • Udenigwe, C.C.1    Li, H.2    Aluko, R.E.3
  • 30
    • 64549083283 scopus 로고    scopus 로고
    • Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions
    • Udenigwe C.C., Lin Y.-S., Hou W.-C., Aluko R.E. Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions. Journal of Functional Foods 2009, 1:199-207.
    • (2009) Journal of Functional Foods , vol.1 , pp. 199-207
    • Udenigwe, C.C.1    Lin, Y.-S.2    Hou, W.-C.3    Aluko, R.E.4
  • 31
    • 4444270688 scopus 로고    scopus 로고
    • Kinetic study on the changes in the susceptibility of egg white proteins to enzymatic hydrolysis induced by heat and high hydrostatic pressure pretreatment
    • van der Plancken I., Delattre M., Indrawati, van Loey A., Hendrickx M.E.G. Kinetic study on the changes in the susceptibility of egg white proteins to enzymatic hydrolysis induced by heat and high hydrostatic pressure pretreatment. Journal of Agricultural and Food Chemistry 2004, 52:5621-5626.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 5621-5626
    • van der Plancken, I.1    Delattre, M.2    Indrawati, I.3    van Loey, A.4    Hendrickx, M.E.G.5
  • 32
    • 34948841863 scopus 로고    scopus 로고
    • Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal
    • Yang Y., Tao G., Liu P., Liu J. Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal. Journal of Agricultural and Food Chemistry 2007, 55:7891-7895.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 7891-7895
    • Yang, Y.1    Tao, G.2    Liu, P.3    Liu, J.4
  • 33
    • 43449126795 scopus 로고    scopus 로고
    • Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: Effect of high-pressure treatment
    • Yin S.-W., Tang C.-H., Wen Q.-B., Yang X.-Q., Li L. Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: Effect of high-pressure treatment. Food Chemistry 2008, 110:938-945.
    • (2008) Food Chemistry , vol.110 , pp. 938-945
    • Yin, S.-W.1    Tang, C.-H.2    Wen, Q.-B.3    Yang, X.-Q.4    Li, L.5
  • 34
    • 84865766793 scopus 로고    scopus 로고
    • Combined effects of high-pressure and enzymatic treatments on the hydrolysis of chickpea protein isolates and antioxidant activity of the hydrolysates
    • Zhang T., Jiang B., Miao M., Mu W., Li Y. Combined effects of high-pressure and enzymatic treatments on the hydrolysis of chickpea protein isolates and antioxidant activity of the hydrolysates. Food Chemistry 2012, 135:904-912.
    • (2012) Food Chemistry , vol.135 , pp. 904-912
    • Zhang, T.1    Jiang, B.2    Miao, M.3    Mu, W.4    Li, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.