| Literature DB >> 19220990 |
Pavel Mokrejs1, Ferdinand Langmaier, Milan Mladek, Dagmar Janacova, Karel Kolomaznik, Vladimir Vasek.
Abstract
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'.Entities:
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Year: 2009 PMID: 19220990 DOI: 10.1177/0734242X07081483
Source DB: PubMed Journal: Waste Manag Res