메뉴 건너뛰기




Volumn 46, Issue 8, 2011, Pages 1705-1710

Preparation and characteristics of yak casein hydrolysate-iron complex

Author keywords

Ferrous binding capacity; Iron releasing percentage; Yak casein; Yak casein hydrolysate iron complex

Indexed keywords

AMIDE GROUPS; BASIC CONDITIONS; CARBOXYLATE GROUPS; CASEIN HYDROLYSATE; DELIVERY VEHICLE; FERROUS SULPHATE; FERROUS-BINDING CAPACITY; HOLDING TIME; HYDROLYSIS DEGREE; IRON-RELEASING PERCENTAGE; MASS RATIO; OPTIMAL BINDING; REACTION TEMPERATURE; STRUCTURAL CHARACTERISTICS; YAK CASEIN; YAK CASEIN HYDROLYSATE-IRON COMPLEX;

EID: 79959976470     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2011.02672.x     Document Type: Article
Times cited : (42)

References (34)
  • 1
    • 34250207588 scopus 로고
    • Approved method for nitrogen solubility index
    • AACC In: St Paul, MN: AOAC International.
    • AACC (1983). Approved method for nitrogen solubility index. In: Approved Methods of the American Association of Cereal Chemists. Pp. 13-46. St Paul, MN: AOAC International.
    • (1983) Approved Methods of the American Association of Cereal Chemists , pp. 13-46
  • 4
    • 21344463555 scopus 로고    scopus 로고
    • Improved absorption of caseinophosphopeptide-bound iron: role of alkaline phosphatase
    • Ani-Kibangou, B., Bouhallab, S., Molle, D. et al. (2005). Improved absorption of caseinophosphopeptide-bound iron: role of alkaline phosphatase. Journal of Nutritional Biochemistry, 16, 398-401.
    • (2005) Journal of Nutritional Biochemistry , vol.16 , pp. 398-401
    • Ani-Kibangou, B.1    Bouhallab, S.2    Molle, D.3
  • 5
    • 0343892762 scopus 로고
    • Biological evaluation of protein quality
    • AOAC (Association of Official Analytical Chemists). In:, 12th edn. AOAC International, Washington, DC: AOAC.
    • AOAC (Association of Official Analytical Chemists). (1975). Biological evaluation of protein quality. In: Official Methods of Analysis of the Association of Official Analytical Chemists, 12th edn. Pp. 857-861. AOAC International, Washington, DC: AOAC.
    • (1975) Official Methods of Analysis of the Association of Official Analytical Chemists , pp. 857-861
  • 7
    • 0035153971 scopus 로고    scopus 로고
    • Iron biology in immune function, muscle metabolism and neuronal functioning
    • Beard, J.L. (2001). Iron biology in immune function, muscle metabolism and neuronal functioning. Journal of Nutrition, 131, 568S-580S.
    • (2001) Journal of Nutrition , vol.131
    • Beard, J.L.1
  • 8
    • 0032031714 scopus 로고    scopus 로고
    • Iron absorption and bioavailability: an updated review
    • Benito, P. & Miller, D. (1998). Iron absorption and bioavailability: an updated review. Nutrition Reviews, 18, 581-603.
    • (1998) Nutrition Reviews , vol.18 , pp. 581-603
    • Benito, P.1    Miller, D.2
  • 14
    • 0036071917 scopus 로고    scopus 로고
    • How to ensure adequate iron absorption from iron-fortified food
    • Hurrell, R. (2002). How to ensure adequate iron absorption from iron-fortified food. Nutrition Reviews, 60, S7-S15.
    • (2002) Nutrition Reviews , vol.60
    • Hurrell, R.1
  • 16
    • 84985204933 scopus 로고
    • Effects of meat and selected food components on the valence of nonheme iron during in vitro digestion
    • 358.
    • Kapsokefalou, M. & Miller, D.D. (1991). Effects of meat and selected food components on the valence of nonheme iron during in vitro digestion. Journal of Food Science, 56, 352-355, 358.
    • (1991) Journal of Food Science , vol.56 , pp. 352-355
    • Kapsokefalou, M.1    Miller, D.D.2
  • 17
    • 25444450750 scopus 로고    scopus 로고
    • Milk proteins and iron absorption: contrasting effects of different caseinophosphopeptides
    • Kibangou, I.B., Bouhallab, S., Henry, G. et al. (2005). Milk proteins and iron absorption: contrasting effects of different caseinophosphopeptides. Pediatric Research, 58, 731-734.
    • (2005) Pediatric Research , vol.58 , pp. 731-734
    • Kibangou, I.B.1    Bouhallab, S.2    Henry, G.3
  • 21
    • 84920780688 scopus 로고
    • Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties
    • Mahmoud, M.I., Malone, W.T. & Cordle, C.T. (1992). Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties. Journal of Food Science, 57, 1223-1229.
    • (1992) Journal of Food Science , vol.57 , pp. 1223-1229
    • Mahmoud, M.I.1    Malone, W.T.2    Cordle, C.T.3
  • 22
    • 34247869873 scopus 로고    scopus 로고
    • Effect of yak milk casein hydrolysate on Th1/Th2 cytokines production by murine spleen lymphocytes in vitro
    • Mao, X.Y., Yang, H.Y., Song, J.P., Li, Y.H. & Ren, F.Z. (2007). Effect of yak milk casein hydrolysate on Th1/Th2 cytokines production by murine spleen lymphocytes in vitro. Journal of Agricultural and Food Chemistry, 55, 638-642.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 638-642
    • Mao, X.Y.1    Yang, H.Y.2    Song, J.P.3    Li, Y.H.4    Ren, F.Z.5
  • 23
    • 0024321174 scopus 로고
    • Is solubility in vitro a reliable predictor of iron bioavailability?
    • Miller, D.D. & Berner, L.A. (1989). Is solubility in vitro a reliable predictor of iron bioavailability? Biological Trace Element Research, 19, 11-24.
    • (1989) Biological Trace Element Research , vol.19 , pp. 11-24
    • Miller, D.D.1    Berner, L.A.2
  • 24
    • 33847640985 scopus 로고    scopus 로고
    • Effects and future trends of casein phosphopeptides on zinc bioavailability
    • Miquel, E. & Farre, R. (2007). Effects and future trends of casein phosphopeptides on zinc bioavailability. Trends in Food Science and Technology, 18, 139-143.
    • (2007) Trends in Food Science and Technology , vol.18 , pp. 139-143
    • Miquel, E.1    Farre, R.2
  • 25
    • 0031527044 scopus 로고    scopus 로고
    • Characterisation of caseins from Mongolian yak, khainak, and bactrian camel
    • Ochirkhuyag, B., Chobert, J.M., Dalgalarrondo, M., Choiset, Y. & Haertle, T. (1997). Characterisation of caseins from Mongolian yak, khainak, and bactrian camel. Lait, 77, 601-613.
    • (1997) Lait , vol.77 , pp. 601-613
    • Ochirkhuyag, B.1    Chobert, J.M.2    Dalgalarrondo, M.3    Choiset, Y.4    Haertle, T.5
  • 26
    • 0036992614 scopus 로고    scopus 로고
    • Bioavailability of minerals in legumes
    • Sandberg, A.S. (2002). Bioavailability of minerals in legumes. British Journal of Nutrition, 88, 281-285.
    • (2002) British Journal of Nutrition , vol.88 , pp. 281-285
    • Sandberg, A.S.1
  • 28
    • 59649116856 scopus 로고    scopus 로고
    • Characterisation of binding of iron to sodium caseinate and whey protein isolate
    • Sugiarto, M., Ye, A. & Singh, H. (2009). Characterisation of binding of iron to sodium caseinate and whey protein isolate. Food Chemistry, 114, 1007-1013.
    • (2009) Food Chemistry , vol.114 , pp. 1007-1013
    • Sugiarto, M.1    Ye, A.2    Singh, H.3
  • 30
    • 0034492053 scopus 로고    scopus 로고
    • Mineral-binding milk proteins and peptides: occurrence, biochemical and technological characteristics
    • Vegarud, G.E., Langsrud, T. & Svenning, C. (2000). Mineral-binding milk proteins and peptides: occurrence, biochemical and technological characteristics. British Journal of Nutrition, 84(Suppl. 1), S91-S98.
    • (2000) British Journal of Nutrition , vol.84 , Issue.SUPPL. 1
    • Vegarud, G.E.1    Langsrud, T.2    Svenning, C.3
  • 32
    • 0347300479 scopus 로고    scopus 로고
    • Speciation of Fe(III) and Fe(II) in water samples by liquid-liquid extraction combined with low-temperature electrothermal vaporization (ETV) ICP-AES
    • Xia, L.B., Wu, Y.L., Jiang, Z.C., Li, S.Q. & Hu, B. (2003). Speciation of Fe(III) and Fe(II) in water samples by liquid-liquid extraction combined with low-temperature electrothermal vaporization (ETV) ICP-AES. International Journal of Environment Analytical Chemistry, 83, 953-962.
    • (2003) International Journal of Environment Analytical Chemistry , vol.83 , pp. 953-962
    • Xia, L.B.1    Wu, Y.L.2    Jiang, Z.C.3    Li, S.Q.4    Hu, B.5
  • 33
    • 0035004974 scopus 로고    scopus 로고
    • Dephosphorylation of sodium caseinate, enzymatically hydrolyzed casein and casein phosphopeptides by intestinal alkaline phosphatase: implications for iron bioavailability
    • Yeung, A.C., Glahn, R.P. & Miller, D.D. (2001). Dephosphorylation of sodium caseinate, enzymatically hydrolyzed casein and casein phosphopeptides by intestinal alkaline phosphatase: implications for iron bioavailability. Journal of Nutritional Biochemistry, 12, 292-299.
    • (2001) Journal of Nutritional Biochemistry , vol.12 , pp. 292-299
    • Yeung, A.C.1    Glahn, R.P.2    Miller, D.D.3
  • 34
    • 0036262829 scopus 로고    scopus 로고
    • Effects of iron source on iron availability from casein and casein phosphopeptides
    • Yeung, A.C., Glahn, R.P. & Miller, D.D. (2002). Effects of iron source on iron availability from casein and casein phosphopeptides. Journal of Food Science, 67, 1271-1275.
    • (2002) Journal of Food Science , vol.67 , pp. 1271-1275
    • Yeung, A.C.1    Glahn, R.P.2    Miller, D.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.