Photochemical behaviour of hydrolysed keratin

Abstract

An investigation into the influence of UV irradiation on keratin hydrolysates was carried out using UV-Vis spectroscopy, Fourier transform infrared spectroscopy (FTIR) and fluorescence spectroscopy. It was found that the absorption of keratin hydrolysates in solution increased during irradiation of the sample, most notably between 250-280 and 320-410 nm. The increase in absorbance in the region 320-410 was because of the new photoproducts formed during UV irradiation of keratin hydrolysates. The fluorescence of keratin hydrolysates was observed at 328 nm after excitation at 270 nm. UV irradiation caused fluorescence fading at 328 nm, and after 60 min of irradiation, a new broad weak band of fluorescence, attributable to new photoproducts, emerged in the UV wavelength region with emission maximum between 400 and 500 nm. FTIR spectroscopy results showed degradation of keratin under UV irradiation. A slight increase in oxidized sulphur species was also observed. The results obtained suggest that UV irradiation can be used as modifying agent for preparation of keratin hydrolysates for cosmetic applications.

Feather keratin hydrolysates obtained from microbial keratinases: effect on hair fiber

“…These reactions lead to a deterioration of hair properties, noticeable to consumers in the form of poor manageability, dryness and brittleness, loss of shine and, in extreme cases, decreased strength [2]. Some cosmetic treatments like permanent curling, permanent coloring, bleaching and relaxing/straightening are known to alter hair properties [9,31]. Even cosmetic handling such as daily combing and brushing can damage hair [32].…”

“…Sionkowska, et al [9] using UV–Vis spectroscopy, Fourier transform, infrared spectroscopy (FTIR) and fluorescence spectroscopy, evaluated the influence of UV irradiation on keratin hydrolysates. New photoproducts were formed during UV irradiation of keratin hydrolysates and a slight increase in oxidized sulfur species was also observed.…”

“…High concentrations of amino acid cysteine are responsible for its unique structure due to the strong chemical bond known as a disulfide bridge [8]. Keratin is found in other epidermic structures such as feathers, nails, scales and horns of mammals, reptiles and birds [9]. …”

“…The addition of protein hydrolysates to hair coloring sprays and toners enables hair to absorb the dyes more uniformly. In the leave-on products, a natural conditioning effect of protein hydrolysates is reported [9,10]. Many types of proteic hydrolysates from plants and animals had been used in hair repair products and in also in skin cosmetics such as wheat protein [11] and keratin from nails, horns and wool [12].…”

Fluorescence detection of protein content in house dust: the possible role of keratin

“…However, several approaches to bioaerosol particles' assessment were developed and successfully applied. [39][40][41] The fluorescent properties of fibrillary proteins are close to that of NAD(P) H, and different spectra deconvolution methods are used to separate their impacts into the overall skin fluorescence signal. The major fluorophores of interest are considered to be aromatic amino acids, NAD(P)H, flavins-that is, the typical fluorophores of living cells.…”