Calcium binding of peptides derived from enzymatic hydrolysates of whey protein concentrate

被引:12
作者
Rui, X. U. [1 ]
机构
[1] NE Agr Univ, Key Lab Dairy Sci, Minist Educ, Coll Food Sci, Harbin 150030, Peoples R China
关键词
Whey Protein; Enzymatic Hydrolysate; Peptide; Hydrolysis; Trypsin; CASEIN;
D O I
10.1111/j.1471-0307.2009.00477.x
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
This study was carried out to investigate the peptides derived from enzymatic hydrolysates of whey protein concentrate. The physiological activity of peptides in whey protein may be used in food additives to promote the absorption of calcium and prevent bone disorders. The whey protein was hydrolysed by trypsin, and the separation of peptides, the properties of hydrolysates and the analysis of the ability to inhibit the formation of calcium phosphates were then investigated. Calcium-binding peptides were produced by tryptic hydrolysis of whey protein concentrate and further purified by precipitation and chromatography on DEAE-cellulose. The hydrolysates were loaded onto an ion-exchange column, followed by stepwise elution with 0, 0.25, 0.5, and 0.75 m NaCl in equilibration buffer to separate the peptides. Trypsin hydrolysates were shown to peak with 0.25 m NaCl and 0.5 m NaCl. The results of SDS-PAGE analysis showed that the peptides with a small molecular weight of about 1.4 to 3.4 kDa were present in the fraction resulting from 0.25 m and 0.5 m NaCl stepwise elution by ion-exchange chromatography of tryptic hydrolysates. The results of this study show that the whey protein hydrolysates produced by the action of trypsin have the ability to inhibit the formation of calcium phosphates.
引用
收藏
页码:170 / 173
页数:4
相关论文
共 12 条
[1]   The effect of high intakes of casein and casein phosphopeptide on calcium absorption in the rat [J].
Bennett, T ;
Desmond, A ;
Harrington, M ;
McDonagh, D ;
FitzGerald, R ;
Flynn, A ;
Cashman, KD .
BRITISH JOURNAL OF NUTRITION, 2000, 83 (06) :673-680
[2]   TRYPTIC PHOSPHOPEPTIDES FROM WHOLE CASEIN .2. PHYSICOCHEMICAL PROPERTIES RELATED TO THE SOLUBILIZATION OF CALCIUM [J].
BERROCAL, R ;
CHANTON, S ;
JUILLERAT, MA ;
PAVILLARD, B ;
SCHERZ, JC ;
JOST, R .
JOURNAL OF DAIRY RESEARCH, 1989, 56 (03) :335-341
[3]  
Friedlander E J, 1980, Methods Enzymol, V67, P504
[4]   SYMPOSIUM - BIOLOGICAL AND FOOD FUNCTIONAL-CHARACTERISTICS OF MILK PROTEIN HYDROLYSIS PRODUCTS - INTRODUCTION [J].
HARWALKAR, VR ;
MCMAHON, DJ .
JOURNAL OF DAIRY SCIENCE, 1993, 76 (01) :300-300
[5]  
Kitts D. D., 1992, Trends in Food Science & Technology, V3, P31, DOI 10.1016/0924-2244(92)90113-B
[6]  
LOWRY OH, 1951, J BIOL CHEM, V193, P265
[7]  
Osborne CG, 1996, NUTR REV, V54, P365, DOI 10.1111/j.1753-4887.1996.tb03850.x
[8]   TRICINE SODIUM DODECYL-SULFATE POLYACRYLAMIDE-GEL ELECTROPHORESIS FOR THE SEPARATION OF PROTEINS IN THE RANGE FROM 1-KDA TO 100-KDA [J].
SCHAGGER, H ;
VONJAGOW, G .
ANALYTICAL BIOCHEMISTRY, 1987, 166 (02) :368-379
[9]   FACTORS CONTRIBUTING TO OSTEOPOROSIS [J].
SPENCER, H ;
KRAMER, L .
JOURNAL OF NUTRITION, 1986, 116 (02) :316-319
[10]  
Wang J H, 1979, Curr Top Cell Regul, V15, P47