HEAT-INDUCED CHANGES IN CASEIN-DERIVED PHOSPHOPEPTIDES

被引:22
作者
MEISEL, H
ANDERSSON, HB
BUHL, K
ERBERSDOBLER, HF
SCHLIMME, E
机构
[1] Federal Dairy Research Centre, Institute for Chemistry and Physics, Kiel
[2] Department of Dairy and Food Science, The Royal Veterinary and Agricultural University, Frederiksberg
[3] Institute of Human Nutrition and Food Science, University of Kiel
来源
ZEITSCHRIFT FUR ERNAHRUNGSWISSENSCHAFT | 1991年 / 30卷 / 03期
关键词
PHOSPHOPEPTIDES; CASEIN; HEATING; DEPHOSPHORYLATION; NUTRITIVE VALUE OF PROTEINS;
D O I
10.1007/BF01610346
中图分类号
R15 [营养卫生、食品卫生]; TS201 [基础科学];
学科分类号
100403 ;
摘要
Phosphopeptides derived from casein may function as carriers for calcium and trace elements. In regard to such specific nutritive effects, the heat-induced changes in tryptic phosphopeptides liberated from bovine sodium caseinate as a model system were investigated. Both microwave and oven heating resulted in a marked loss of peptide-bound phosphorous (dephosphorylation) and a decrease of caseinophosphopeptides in the soluble part of the tryptic hydrolysate. It is concluded that hydrolysis of phosphoseryl to seryl residues was the prevailing degradation step to soluble proteolytic products, whereas lysinoalanyl-casein is claimed to be present almost exclusively in the pH 4.6-insoluble part of the tryptic digest.
引用
收藏
页码:227 / 232
页数:6
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