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Volumn 36, Issue 8, 2016, Pages 798-807

Herring roe protein has a high Digestible Indispensable Amino Acid Score (DIAAS) using a dynamic in vitro gastrointestinal model

Author keywords

DIAAS; Herring egg protein; In vitro digestion; Indispensable amino acid; True protein digestibility

Indexed keywords

AMINO ACID; CASEIN; EGG PROTEIN; EGG WHITE; HERRING ROE PROTEIN; INDISPENSABLE AMINO ACID; OVALBUMIN; UNCLASSIFIED DRUG; FISH PROTEIN;

EID: 84976561332     PISSN: 02715317     EISSN: 18790739     Source Type: Journal    
DOI: 10.1016/j.nutres.2016.05.004     Document Type: Article
Times cited : (38)

References (32)
  • 2
    • 84922204369 scopus 로고    scopus 로고
    • Protein digestibility-corrected amino acid scores and digestible indispensable amino acid scores differentially describe protein quality in growing male rats
    • [2] Rutherfurd, SM, Fanning, AC, Miller, BJ, Moughan, PJ, Protein digestibility-corrected amino acid scores and digestible indispensable amino acid scores differentially describe protein quality in growing male rats. J Nutr 145 (2015), 372–379.
    • (2015) J Nutr , vol.145 , pp. 372-379
    • Rutherfurd, S.M.1    Fanning, A.C.2    Miller, B.J.3    Moughan, P.J.4
  • 4
    • 74949084066 scopus 로고    scopus 로고
    • Ileal digestibility of dietary protein in the growing pig and adult human
    • [4] Deglaire, A, Bos, C, Tomé, D, Moughan, PJ, Ileal digestibility of dietary protein in the growing pig and adult human. Br J Nutr 102 (2009), 1752–1759.
    • (2009) Br J Nutr , vol.102 , pp. 1752-1759
    • Deglaire, A.1    Bos, C.2    Tomé, D.3    Moughan, P.J.4
  • 5
    • 0028047623 scopus 로고
    • Comparison of the ileal and fecal digestibility of dietary amino acids in adult humans and evaluation of the pig as model animal for digestion studies in man
    • [5] Rowan, AM, Moughan, PJ, Wilson, MN, Maher, K, Tasman-Jones, C, Comparison of the ileal and fecal digestibility of dietary amino acids in adult humans and evaluation of the pig as model animal for digestion studies in man. Br J Nutr 71 (1994), 29–42.
    • (1994) Br J Nutr , vol.71 , pp. 29-42
    • Rowan, A.M.1    Moughan, P.J.2    Wilson, M.N.3    Maher, K.4    Tasman-Jones, C.5
  • 6
    • 0019154211 scopus 로고
    • Protein digestibility of the same protein preparations by humans and rat assays and by in vitro enzymatic digestion methods
    • [6] Bodwell, CE, Satterlee, LD, Hackler, LR, Protein digestibility of the same protein preparations by humans and rat assays and by in vitro enzymatic digestion methods. Am J Clin Nutr 33 (1980), 677–686.
    • (1980) Am J Clin Nutr , vol.33 , pp. 677-686
    • Bodwell, C.E.1    Satterlee, L.D.2    Hackler, L.R.3
  • 7
    • 33846567968 scopus 로고    scopus 로고
    • Gastrointestinal digestion of food allergens: effect on their allergenicity
    • [7] Moreno, FJ, Gastrointestinal digestion of food allergens: effect on their allergenicity. Biomed Pharmacother 61 (2007), 50–60.
    • (2007) Biomed Pharmacother , vol.61 , pp. 50-60
    • Moreno, F.J.1
  • 8
    • 69149106437 scopus 로고    scopus 로고
    • In vitro digestion methods for assessing the effect of food structure on allergen breakdown
    • [8] Wickham, M, Faulks, R, Mills, C, In vitro digestion methods for assessing the effect of food structure on allergen breakdown. Mol Nutr Food Res 53 (2009), 952–958.
    • (2009) Mol Nutr Food Res , vol.53 , pp. 952-958
    • Wickham, M.1    Faulks, R.2    Mills, C.3
  • 9
    • 0001151974 scopus 로고
    • A multi compartmental dynamic computer-controlled model simulating the stomach and small intestine
    • [9] Minekus, M, Marteau, P, Havenaar, R, Huis in‘t Veld, JHJ, A multi compartmental dynamic computer-controlled model simulating the stomach and small intestine. ATLA 23 (1995), 197–209.
    • (1995) ATLA , vol.23 , pp. 197-209
    • Minekus, M.1    Marteau, P.2    Havenaar, R.3    Huis in‘t Veld, J.H.J.4
  • 10
    • 38349083815 scopus 로고    scopus 로고
    • Efficient degradation of gluten by prolyl endoprotease in a gastrointestinal model: implications for coeliac disease
    • [10] Mitea, C, Havenaar, R, Drijfhout, JW, Edens, L, Dekking, L, Koning, F, Efficient degradation of gluten by prolyl endoprotease in a gastrointestinal model: implications for coeliac disease. Gut 57 (2008), 25–32.
    • (2008) Gut , vol.57 , pp. 25-32
    • Mitea, C.1    Havenaar, R.2    Drijfhout, J.W.3    Edens, L.4    Dekking, L.5    Koning, F.6
  • 11
    • 84856255535 scopus 로고    scopus 로고
    • In vitro digestion of proteins and growth factors in a bovine whey protein extract as determined using a computer-controlled dynamic gastrointestinal system (TIM-1)
    • [11] Nabil, S, Gauthier, SF, Drouin, R, Poubelle, PE, Pouliot, Y, In vitro digestion of proteins and growth factors in a bovine whey protein extract as determined using a computer-controlled dynamic gastrointestinal system (TIM-1). Food Dig 22 (2011), 13–22.
    • (2011) Food Dig , vol.22 , pp. 13-22
    • Nabil, S.1    Gauthier, S.F.2    Drouin, R.3    Poubelle, P.E.4    Pouliot, Y.5
  • 12
    • 84975467739 scopus 로고    scopus 로고
    • Comparison of nitrogen bioaccessibility from salmon and whey protein hydrolysates using a human gastrointestinal model (TIM-1)
    • [12] Framroze, B, Savard, P, Gagnon, D, Richard, V, Gauthier, SF, Comparison of nitrogen bioaccessibility from salmon and whey protein hydrolysates using a human gastrointestinal model (TIM-1). Funct Foods Health Dis 4 (2014), 222–231.
    • (2014) Funct Foods Health Dis , vol.4 , pp. 222-231
    • Framroze, B.1    Savard, P.2    Gagnon, D.3    Richard, V.4    Gauthier, S.F.5
  • 13
    • 84860738206 scopus 로고    scopus 로고
    • An investigation into the utility of a multi-compartmental, dynamic, system of the upper gastrointestinal tract to support formulation development and establish bioequivalence of poorly soluble drugs
    • [13] Dickinson, PA, Abu Rmaileh, R, Ashworth, L, Barker, RA, Burke, WM, Patterson, CM, et al. An investigation into the utility of a multi-compartmental, dynamic, system of the upper gastrointestinal tract to support formulation development and establish bioequivalence of poorly soluble drugs. AAPS J 14 (2012), 196–205.
    • (2012) AAPS J , vol.14 , pp. 196-205
    • Dickinson, P.A.1    Abu Rmaileh, R.2    Ashworth, L.3    Barker, R.A.4    Burke, W.M.5    Patterson, C.M.6
  • 14
    • 84915748542 scopus 로고    scopus 로고
    • Application and validation of an advanced gastrointestinal in vitro model for evaluation of drug product performance in pharmaceutical development
    • [14] Barker, R, Abrahamsson, B, Kruusmägi, M, Application and validation of an advanced gastrointestinal in vitro model for evaluation of drug product performance in pharmaceutical development. J Pharm Sci 43 (2014), 3704–3712.
    • (2014) J Pharm Sci , vol.43 , pp. 3704-3712
    • Barker, R.1    Abrahamsson, B.2    Kruusmägi, M.3
  • 15
    • 23044498572 scopus 로고    scopus 로고
    • The protein digestibility-corrected amino acid score (PDCAAS). A concept for describing protein quality in foods and food ingredients: a critical review
    • [15] Schaafsma, G, The protein digestibility-corrected amino acid score (PDCAAS). A concept for describing protein quality in foods and food ingredients: a critical review. J AOAC Int 88 (2005), 988–994.
    • (2005) J AOAC Int , vol.88 , pp. 988-994
    • Schaafsma, G.1
  • 16
    • 84865432100 scopus 로고    scopus 로고
    • Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review
    • [16] Chalamaiah, M, Dinesh Kumar, B, Hemalatha, R, Jyothirmayi, T, Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review. Food Chem 135 (2012), 3020–3038.
    • (2012) Food Chem , vol.135 , pp. 3020-3038
    • Chalamaiah, M.1    Dinesh Kumar, B.2    Hemalatha, R.3    Jyothirmayi, T.4
  • 17
    • 84869111631 scopus 로고    scopus 로고
    • Functions, applications and production of protein hydrolysates from fish processing co-products. (FPCP)
    • [17] He, S, Franco, C, Zhang, W, Functions, applications and production of protein hydrolysates from fish processing co-products. (FPCP). Food Res Int 50 (2013), 289–297.
    • (2013) Food Res Int , vol.50 , pp. 289-297
    • He, S.1    Franco, C.2    Zhang, W.3
  • 18
    • 0141590645 scopus 로고    scopus 로고
    • Biochemical and functional properties of herring (Clupea harengus) byproduct hydrolysates
    • [18] Sathivel, S, Bechtel, PJ, Babbitt, J, Smiley, S, Crapo, C, Reppond, KD, et al. Biochemical and functional properties of herring (Clupea harengus) byproduct hydrolysates. Food Chem Toxicol 68 (2003), 2196–2200.
    • (2003) Food Chem Toxicol , vol.68 , pp. 2196-2200
    • Sathivel, S.1    Bechtel, P.J.2    Babbitt, J.3    Smiley, S.4    Crapo, C.5    Reppond, K.D.6
  • 19
    • 84986501982 scopus 로고
    • Biochemical property of the membrane of the herring egg, with special reference to the role of the micropyle in fertilization
    • [19] Yamamoto, TS, Biochemical property of the membrane of the herring egg, with special reference to the role of the micropyle in fertilization. J Fac Sci Hokkaido Univ 14 (1958), 9–17.
    • (1958) J Fac Sci Hokkaido Univ , vol.14 , pp. 9-17
    • Yamamoto, T.S.1
  • 20
    • 0031664420 scopus 로고    scopus 로고
    • Digestibility of cooked and raw egg protein in humans as assessed by stable isotope techniques
    • [20] Evenepoel, P, Geypens, B, Luypaerts, A, Hiele, M, Ghoos, Y, Rutgeerts, P, Digestibility of cooked and raw egg protein in humans as assessed by stable isotope techniques. J Nutr 128 (1998), 1716–1722.
    • (1998) J Nutr , vol.128 , pp. 1716-1722
    • Evenepoel, P.1    Geypens, B.2    Luypaerts, A.3    Hiele, M.4    Ghoos, Y.5    Rutgeerts, P.6
  • 21
    • 14944374476 scopus 로고    scopus 로고
    • An acute ileal amino acid digestibility assay is a valid procedure for use in human ileostomates
    • [21] Moughan, PJ, Butts, CA, van Wijk, H, Rowan, A, Reynolds, W, An acute ileal amino acid digestibility assay is a valid procedure for use in human ileostomates. J Nutr 135 (2007), 404–409.
    • (2007) J Nutr , vol.135 , pp. 404-409
    • Moughan, P.J.1    Butts, C.A.2    van Wijk, H.3    Rowan, A.4    Reynolds, W.5
  • 22
    • 84881238066 scopus 로고    scopus 로고
    • Digestibility of transglutaminase cross-linked caseinate versus native caseinate in an in vitro multi-compartmental model simulating young child and adult gastrointestinal conditions
    • [22] Havenaar, R, de Jong, A, Koenen, MJ, van Bilsen, J, Janssen, AM, Labij, E, et al. Digestibility of transglutaminase cross-linked caseinate versus native caseinate in an in vitro multi-compartmental model simulating young child and adult gastrointestinal conditions. J Agric Food Chem 16 (2013), 7636–7644.
    • (2013) J Agric Food Chem , vol.16 , pp. 7636-7644
    • Havenaar, R.1    de Jong, A.2    Koenen, M.J.3    van Bilsen, J.4    Janssen, A.M.5    Labij, E.6
  • 23
    • 0003697743 scopus 로고    scopus 로고
    • Development and validation of a dynamic model of the gastrointestinal tract
    • PhD Thesis Utrecht University The Netherlands
    • [23] Minekus, M, Development and validation of a dynamic model of the gastrointestinal tract. PhD Thesis, 1998, Utrecht University, The Netherlands.
    • (1998)
    • Minekus, M.1
  • 24
    • 84976539883 scopus 로고    scopus 로고
    • Comprehensive review of scientific literature pertaining to nitrogen protein conversion factors
    • IDF Brussels
    • [24] International Dairy Federation (IDF), Comprehensive review of scientific literature pertaining to nitrogen protein conversion factors. Bulletin no. 405, 2006, IDF, Brussels.
    • (2006) Bulletin no. 405
    • International Dairy Federation (IDF)1
  • 26
    • 0019065619 scopus 로고
    • Amino acid content of Baltic herring and rainbow trout roe
    • [26] Kaitaranta, JK, Lamppu, R, Linko, RR, Amino acid content of Baltic herring and rainbow trout roe. J Agric Food Chem 28 (1980), 908–911.
    • (1980) J Agric Food Chem , vol.28 , pp. 908-911
    • Kaitaranta, J.K.1    Lamppu, R.2    Linko, R.R.3
  • 29
    • 84903588792 scopus 로고    scopus 로고
    • Biochemical composition and quality of turbot (Scophthalmus maximus) eggs throughout the reproductive season
    • [29] Jia, Y, Meng, Z, Liu, X, Biochemical composition and quality of turbot (Scophthalmus maximus) eggs throughout the reproductive season. Fish Physiol Biochem 40 (2014), 1093–1104.
    • (2014) Fish Physiol Biochem , vol.40 , pp. 1093-1104
    • Jia, Y.1    Meng, Z.2    Liu, X.3
  • 30
    • 84868106709 scopus 로고    scopus 로고
    • Digestibility and availability of nitrogen for whey protein hydrolysate products assessed using a dynamic in vitro gastrointestinal model
    • [30] Venema, K, Dohnalek, MH, Digestibility and availability of nitrogen for whey protein hydrolysate products assessed using a dynamic in vitro gastrointestinal model. J Allergy Clin Immunol, 2, 2006, S304.
    • (2006) J Allergy Clin Immunol , vol.2 , pp. S304
    • Venema, K.1    Dohnalek, M.H.2
  • 31
    • 84938992274 scopus 로고    scopus 로고
    • Biophysical aspects of lipid digestion in human breast milk and Similac infant formulas
    • [31] Fondaco, D, AlHasawi, F, Lan, Y, Ben-Elazar, S, Connolly, K, Rogers, MA, Biophysical aspects of lipid digestion in human breast milk and Similac infant formulas. Food Biophys 10 (2015), 282–291.
    • (2015) Food Biophys , vol.10 , pp. 282-291
    • Fondaco, D.1    AlHasawi, F.2    Lan, Y.3    Ben-Elazar, S.4    Connolly, K.5    Rogers, M.A.6
  • 32
    • 84925653705 scopus 로고    scopus 로고
    • Three differently generated salmon protein hydrolysates reveal opposite effects on hepatic lipid metabolism in mice fed a high-fat diet
    • [32] Vik, R, Tillander, V, Skorve, J, Vihervaara, T, Ekroos, K, Alexson, SHE, et al. Three differently generated salmon protein hydrolysates reveal opposite effects on hepatic lipid metabolism in mice fed a high-fat diet. Food Chem 183 (2015), 101–110.
    • (2015) Food Chem , vol.183 , pp. 101-110
    • Vik, R.1    Tillander, V.2    Skorve, J.3    Vihervaara, T.4    Ekroos, K.5    Alexson, S.H.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.