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Substantivity to hair and skin of 125 l‐labelled collagen hydrolysates under application simulating conditions
Author(s) -
TUROWSKI A.,
ADELMANNGRILL B. C.
Publication year - 1985
Publication title -
international journal of cosmetic science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.532
H-Index - 62
eISSN - 1468-2494
pISSN - 0142-5463
DOI - 10.1111/j.1467-2494.1985.tb00398.x
Subject(s) - hydrolysate , isoelectric point , chemistry , shampoo , chromatography , adsorption , hydrolysis , organic chemistry , enzyme
Synopsis Substantivity of various 125 I‐labelled collagen hydrolysates to virgin or bleached and dyed European hair or human callus was tested under conditions which simulated actual application of such hydrolysates in shampoos or foam baths. Factors which most strongly influence protein substantivity were identified. The molecular properties of the hydrolysate are the most important factor. The hydrolysate which adsorbed best had the lowest overall isoelectric point, the highest pH in solution and the largest content of high molecular weight peptides. The extent of adsorption was also a function of concentration of protein, of the duration of application and of the nature of the components of the formulation. Thus, the combination of shampoo and hydrolysate can be adjusted so that a desired substantivity is attained.