Interactions of Casein Components with lmmobilized γ-Casein
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چکیده
منابع مشابه
The chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie
Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagentK(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperoneability of modified system by UV-Vis and fluorescence spectroscopy and theor...
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Over 40 new compounds were isolated and identified from a cold-finger molecular distillate obtained from a dichloromethane extract of a lactose-casein browning system, in connection with studies on off-flavor development in dairy products. These compounds consist of 15 C-5 to C-14 furanics, five pyrazines, three pyrroles, three lactones, 2-acetylpyridine, acrolein, cyclopentanone, 2-methyltetra...
متن کاملCasein Viscosity Studies
1. Viscosity and pH curves of casein dissolved in NaOH, KOH, LiOH, and NH(4)OH are shown and it is found that a maximum viscosity occurs at about the same pH point with each alkali; i.e., 9.1 to 9.25. The magnitude of the viscosity is largest in ammonia solutions. 2. The maximum viscosity occurs in 8 to 10 per cent solutions of casein in alkalies when about 98 x 10(-5) gram equivalents of base ...
متن کاملthe chaperone ability comparison of norma ii-casein and modified d-casein upon interaction with lysozinie
diminishing protein aggregation by chaperone is very important factor in medicine and industry. in this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by woodward reagentk(wrk) and examined on lysozyme as a target protein at ph 7.2 and outlined the mechanism for chaperoneability of modified system by uv-vis and fluorescence spectroscopy and theor...
متن کاملCasein phosphopeptides from casein micelles by successive digestion with pepsin and trypsin.
When milk is ingested, casein micelles will be successively digested by pepsin in the stomach and trypsin in the intestine. Therefore, we digested casein micelles successively with pepsin at pH 4.0 and trypsin at pH 7.0, and recovered casein phosphopeptides (CPP) as CPP-calcium phosphate (CP) complexes. The CPP-CP complexes contained 248 mg of calcium/g peptides and 175 mg of inorganic phosphor...
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ژورنال
عنوان ژورنال: Nihon Chikusan Gakkaiho
سال: 1982
ISSN: 1346-907X,1880-8255
DOI: 10.2508/chikusan.53.56