Extraction of collagen and gelatine from meat industry by-products for food and non food uses.
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'.
Mokrejs
Pavel
P
Faculty of Technology, Department of Protein and Leather, Tomas Bata University, Zlin, The Czech Republic. mokrejs@ft.utb.cz
Langmaier
Ferdinand
F
Mladek
Milan
M
Janacova
Dagmar
D
Kolomaznik
Karel
K
Vasek
Vladimir
V
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D005502:Food; D005506:Food Contamination; D019649:Food Industry; D005780:Gelatin / Q000737:chemistry*; D008460:Meat; D013710:Tendons / Q000737:chemistry*
D005780:Gelatin; D003094:Collagen