Poultry feathers make up for as much as 8.5% of chicken weight and represent a considerable amount of almost pure keratin waste which is not being adequately utilized at the present time. The present study dealt with the processing of poultry feathers through a two-stage alkaline-enzymatic hydrolysis. In the first stage, feathers were mixed with a 0.1 or 0.3% KOH water solution in a 1 : 50 ratio and were incubated at 70°C for 24 h. After adjusting pH to 9, the effects examined in the second processing stage on the amount of degraded feathers were those of proteolytic enzyme additions (1-5%), time (4-8 h) and temperature (50-70°C). Processing feathers in 0.3% KOH and hydrolysing for 8 h in the second stage at 70°C with a 5% dose of enzyme (relative to dry feathers weight) produced approx. 91% degradation. Keratin hydrolysate is distinct for its high nitrogen content and reasonable inorganic solids level. Two-stage technology of alkaline-enzymatic hydrolysing of poultry feathers in an environment of 0.3% KOH achieves high efficiency under quite mild reaction conditions (temperature not exceeding 70°C with pH in a mildly alkaline region), and is feasible from an economic viewpoint. Keratin hydrolysate can find particular application in packaging technology (films, foils and encapsulates).
Every year, the poultry industry produces a large number of by-products such as chicken heads containing a considerable proportion of proteins, particularly collagen. To prepare gelatin is one of the possibilities to advantageously utilize these by-products as raw materials. The aim of the paper was to process chicken heads into gelatins. An innovative method for conditioning starting raw material was using the proteolytic enzyme. Three technological factors influencing the yield and properties of extracted gelatins were monitored including the amount of enzyme used in the conditioning of the raw material (0.4% and 1.6%), the time of the conditioning (18 and 48 h), and the first gelatin extraction time (1 and 4 h). The gelatin yield was between 20% and 36%. The gelatin gel strength ranged from 113 to 355 Bloom. The viscosity of the gelatin solution was determined between 1.4 and 9.5 mPa.s. The content of inorganic solids varied from 2.3% to 3.9% and the melting point of the gelatin gel was recorded between 34.5 and 42.2 °C. This study has shown that gelatin obtained from chicken heads has a promising potential with diverse possible applications in the food industry, pharmacy, and cosmetics.
Short tendons of slaughtered cattle, which consist of relatively pure collagen, were cleaned of lipoid substances and non-collagen proteins using a commercial enzymatic preparation. Diluted acetic acid was used to separate the acid-soluble collagen (M(N) approximately 300 kDa) for a yield of around 5%. The residue was extracted with water and the extraction conditions were derived to produce gelatine with a gel rigidity of 350-410 degrees Bloom and a yield of 55-60%. Prolonged extraction time, as well as increased extraction temperature, led to a deterioration in the gelatine quality and, therefore, the residue after aqueous extraction was processed by enzymatic hydrolysis into a collagen hydrolysate of M(N) = 500-1000 Da. Such hydrolysates can be utilized in industry as humectants in cosmetic skin-care preparations or as a secondary industrial raw material for producing surfactants of acylamino-carboxy acid type, which are known for their favourable dermatological effects. Apart from a maximum of 7% lipoid substances the proposed procedure produced no further waste so it may be regarded as a 'clean technology'.
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