메뉴 건너뛰기




Volumn 57, Issue 12, 2009, Pages 5563-5570

Fractionation and characterization of brewers' spent grain protein hydrolysates

Author keywords

Brewers' spent grain; Fractionation; Hydrolysates; Proteolysis; Technofunctional properties

Indexed keywords

BACTERIAL PROTEIN; SUBTILISIN; VEGETABLE PROTEIN;

EID: 67649170627     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf900626j     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 35549005384 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates
    • Celus, I.; Brijs, K.; Delcour, J. A. Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. J. Agrie. Food Chem. 2007, 55, 8703-8710.
    • (2007) J. Agrie. Food Chem , vol.55 , pp. 8703-8710
    • Celus, I.1    Brijs, K.2    Delcour, J.A.3
  • 2
    • 77957067862 scopus 로고    scopus 로고
    • Functional properties
    • Aalbersberg, W. Y, Hamer, R. J, Jasperse, P, de Jongh, H. H. J, de Kruif, C. G, Walstra, P, de Wolf, F. A, Eds, Elsevier Science B.V, Amsterdam, The Netherlands
    • Walstra, P.; van Vliet, T. Functional properties. In Industrial Proteins in Perspective; Aalbersberg, W. Y., Hamer, R. J., Jasperse, P., de Jongh, H. H. J., de Kruif, C. G., Walstra, P., de Wolf, F. A., Eds.; Elsevier Science B.V.: Amsterdam, The Netherlands, 2003; Vol. 23, pp 9-30.
    • (2003) Industrial Proteins in Perspective , vol.23 , pp. 9-30
    • Walstra, P.1    van Vliet, T.2
  • 3
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang, J. S.; Zhao, M. M.; Yang, X. Q.; Jiang, Y. M. Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. J. Cereal Sci. 2006, 44, 93-100.
    • (2006) J. Cereal Sci , vol.44 , pp. 93-100
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3    Jiang, Y.M.4
  • 4
    • 44349101790 scopus 로고    scopus 로고
    • Preparation and characterization of modified wheat gluten by enzymatic hydrolysis- ultrafiltration
    • Wang, J. S.; Zhao, M. M.; Bao, Y.; Hong, T.; Rosella, G M. Preparation and characterization of modified wheat gluten by enzymatic hydrolysis- ultrafiltration. J. Food Biochem. 2008, 32, 316-334.
    • (2008) J. Food Biochem , vol.32 , pp. 316-334
    • Wang, J.S.1    Zhao, M.M.2    Bao, Y.3    Hong, T.4    Rosella, G.M.5
  • 7
    • 1542708368 scopus 로고    scopus 로고
    • Recent advances in enzymatic modifications of food proteins for improving their functional properties
    • Chobert, J. M.; Briand, L.; Gueguen, J.; Popineau, Y.; Larre, C.; Haertle, T. Recent advances in enzymatic modifications of food proteins for improving their functional properties. Nahrung 1996, 40, 177-182.
    • (1996) Nahrung , vol.40 , pp. 177-182
    • Chobert, J.M.1    Briand, L.2    Gueguen, J.3    Popineau, Y.4    Larre, C.5    Haertle, T.6
  • 9
    • 0036314589 scopus 로고    scopus 로고
    • Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration
    • Popineau, Y.; Huchet, B.; Larre, C.; Berot, S. Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration. J. Cereal Sci. 2002, 35, 327-335.
    • (2002) J. Cereal Sci , vol.35 , pp. 327-335
    • Popineau, Y.1    Huchet, B.2    Larre, C.3    Berot, S.4
  • 10
    • 0032891162 scopus 로고    scopus 로고
    • Influence of double enzymic hydrolyses on gluten functionality
    • Mimouni, B.; Azanza, J. L.; Raymond, J. Influence of double enzymic hydrolyses on gluten functionality. J. Sci. Food Agrie. 1999, 79, 1048-1053.
    • (1999) J. Sci. Food Agrie , vol.79 , pp. 1048-1053
    • Mimouni, B.1    Azanza, J.L.2    Raymond, J.3
  • 11
    • 67649195404 scopus 로고
    • Influence of peptide chain-length on taste and functional properties of enzymatically modified soy protein
    • Adler-Nissen, J.; Olsen, H. S. Influence of peptide chain-length on taste and functional properties of enzymatically modified soy protein. Abstr. Pap. Am. Chem. Soc. 1978, 175, 13.
    • (1978) Abstr. Pap. Am. Chem. Soc , vol.175 , pp. 13
    • Adler-Nissen, J.1    Olsen, H.S.2
  • 12
    • 0032116216 scopus 로고    scopus 로고
    • Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration
    • Wu, W. U.; Hettiarachchy, N. S.; Qi, M. Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. J. Am. Oil Chem. Soc. 1998, 75, 845-850.
    • (1998) J. Am. Oil Chem. Soc , vol.75 , pp. 845-850
    • Wu, W.U.1    Hettiarachchy, N.S.2    Qi, M.3
  • 13
    • 0031423685 scopus 로고    scopus 로고
    • Solubility and emulsifying properties of soy protein isolates modified by pancreatin
    • Qi, M.; Hettiarachchy, N. S.; Kalapathy, U. Solubility and emulsifying properties of soy protein isolates modified by pancreatin. J. Food Sci. 1997, 52, 1110-1115.
    • (1997) J. Food Sci , vol.52 , pp. 1110-1115
    • Qi, M.1    Hettiarachchy, N.S.2    Kalapathy, U.3
  • 14
    • 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. Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis. J. Food Sci. 2005, 70, C180-C187.
    • (2005) J. Food Sci , vol.70
    • Jung, S.1    Murphy, P.A.2    Johnson, L.A.3
  • 15
    • 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. Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties. Food Res. Int. 2002, 35, 511-518.
    • (2002) Food Res. Int , vol.35 , pp. 511-518
    • Ortiz, S.E.M.1    Wagner, J.R.2
  • 16
    • 21244482606 scopus 로고    scopus 로고
    • Enhancement of angiotensin I converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of corn gluten hydrolysate using ultrafiltration membranes
    • Kim, J. M.; Whang, J. H.; Suh, H. J. Enhancement of angiotensin I converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of corn gluten hydrolysate using ultrafiltration membranes. Eur. Food Res. Technol. 2004, 218, 133-138.
    • (2004) Eur. Food Res. Technol , vol.218 , pp. 133-138
    • Kim, J.M.1    Whang, J.H.2    Suh, H.J.3
  • 17
    • 0038189847 scopus 로고    scopus 로고
    • Functional and bioactive properties of quinoa seed protein hydrolysates
    • Aluko, R. E.; Monu, E. Functional and bioactive properties of quinoa seed protein hydrolysates. J. Food Sci. 2003, 68, 1254-1258.
    • (2003) J. Food Sci , vol.68 , pp. 1254-1258
    • Aluko, R.E.1    Monu, E.2
  • 19
    • 0000050670 scopus 로고    scopus 로고
    • Plasmin hydrolysis of ß-casein: Foaming and emulsifying properties of the fractionated hydrolysate
    • Caessens, P. W. J. R.; Gruppen, H.; Visser, S.; van Aken, G. A.; Voragen, A. G. J. Plasmin hydrolysis of ß-casein: Foaming and emulsifying properties of the fractionated hydrolysate. J. Agric. Food Chem. 1997, 45, 2935-2941.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 2935-2941
    • Caessens, P.W.J.R.1    Gruppen, H.2    Visser, S.3    van Aken, G.A.4    Voragen, A.G.J.5
  • 20
    • 0032843780 scopus 로고    scopus 로고
    • Functionality of ß-casein peptides: Importance of amphipathicity for emulsion-stabilizing properties
    • Caessens, P. W. J. R.; Gruppen, H.; Slangen, C. J.; Visser, S.; Voragen, A. G. J. Functionality of ß-casein peptides: Importance of amphipathicity for emulsion-stabilizing properties. J. Agric. Food Chem. 1999, 47, 1856-1862.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 1856-1862
    • Caessens, P.W.J.R.1    Gruppen, H.2    Slangen, C.J.3    Visser, S.4    Voragen, A.G.J.5
  • 21
    • 0034775381 scopus 로고    scopus 로고
    • Emulsion properties of casein and whey protein hydrolysates and the relation with other hydrolysate characteristics
    • van der Ven, C.; Gruppen, H.; de Bont, D. B. A.; Voragen, A. G. J. Emulsion properties of casein and whey protein hydrolysates and the relation with other hydrolysate characteristics. J. Agric. Food Chem. 2001, 49, 5005-5012.
    • (2001) J. Agric. Food Chem , vol.49 , pp. 5005-5012
    • van der Ven, C.1    Gruppen, H.2    de Bont, D.B.A.3    Voragen, A.G.J.4
  • 22
    • 0037041933 scopus 로고    scopus 로고
    • Correlations between biochemical characteristics and foam-forming and -stabilizing ability of whey and casein hydrolysates
    • van der Ven, C.; Gruppen, H.; de Bont, D. B. A.; Voragen, A. G. J. Correlations between biochemical characteristics and foam-forming and -stabilizing ability of whey and casein hydrolysates. J. Agric. Food Chem. 2002, 50, 2938-2946.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 2938-2946
    • van der Ven, C.1    Gruppen, H.2    de Bont, D.B.A.3    Voragen, A.G.J.4
  • 23
    • 33746914723 scopus 로고    scopus 로고
    • The effects of malting and mashing on barley protein extractability
    • Celus, I.; Brijs, K.; Delcour, J. A. The effects of malting and mashing on barley protein extractability. J. Cereal Sci. 2006, 44, 203-211.
    • (2006) J. Cereal Sci , vol.44 , pp. 203-211
    • Celus, I.1    Brijs, K.2    Delcour, J.A.3
  • 24
    • 0032855358 scopus 로고    scopus 로고
    • Brijs, K.; Bleukx, W.; Delcour, J. A. Proteolytic activities in dormant rye (Sécale céréale L.) grain. J. Agric. Food Chem. 1999, 47, 35723578.
    • Brijs, K.; Bleukx, W.; Delcour, J. A. Proteolytic activities in dormant rye (Sécale céréale L.) grain. J. Agric. Food Chem. 1999, 47, 35723578.
  • 25
    • 67649159496 scopus 로고    scopus 로고
    • Association of Official Analytical Chemists (AOAC). Method 990.03. In Official Methods of Analysis, 16th ed.; AOAC: Washington, D.G, 1995.
    • Association of Official Analytical Chemists (AOAC). Method 990.03. In Official Methods of Analysis, 16th ed.; AOAC: Washington, D.G, 1995.
  • 27
    • 67649183185 scopus 로고    scopus 로고
    • AACC Methods 44-15A, 08-12
    • Amercan Association of Cereal Chemists AACC, 76-13, AACC: St. Paul, MN
    • Amercan Association of Cereal Chemists (AACC). AACC Methods 44-15A, 08-12, 32-23, 76-13. In Approved Methods of the AACC; AACC: St. Paul, MN, 2000.
    • (2000) Approved Methods of the AACC , vol.32 -23
  • 28
    • 37049108995 scopus 로고
    • Simplified method for the measurement of total non-starch polysaccharides by gas-liquid chromatography of constituent sugars as alditol acetates
    • Englyst, H. N.; Cummings, J. H. Simplified method for the measurement of total non-starch polysaccharides by gas-liquid chromatography of constituent sugars as alditol acetates. Analyst 1984, 109, 937-942.
    • (1984) Analyst , vol.109 , pp. 937-942
    • Englyst, H.N.1    Cummings, J.H.2
  • 29
    • 0001443821 scopus 로고    scopus 로고
    • Contents and structural features of water-extractable arabinogalactan in wheat flour fractions
    • Loosveld, A. M. A.; Grobet, P. J.; Delcour, J. A. Contents and structural features of water-extractable arabinogalactan in wheat flour fractions. J. Agric. Food Chem. 1997, 45, 1998-2002.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 1998-2002
    • Loosveld, A.M.A.1    Grobet, P.J.2    Delcour, J.A.3
  • 30
    • 33947092713 scopus 로고
    • Emulsifying properties of proteinsEvaluation of a turbidimetric technique
    • Pearce, K. N.; Kinsella, J. E. Emulsifying properties of proteinsEvaluation of a turbidimetric technique. J. Agric. Food Chem. 1978, 26, 716-723.
    • (1978) J. Agric. Food Chem , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 33
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S. Protein stabilization of emulsions and foams. J. Food Sci. 2005, 70, R54-R66.
    • (2005) J. Food Sci , vol.70
    • Damodaran, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.