Extraction of collagen and gelatine from meat industry by-products for food and non food uses

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'.

A mixture of peptides and sugars derived from plant cell walls increases plant defense responses to stress and attenuates ageing-associated molecular changes in cultured skin cells

“…Research has also demonstrated a beneficial effect of synthetic peptides and total protein extracts on wound healing (Bentley et al, 1990) and on the production of new collagen fibers (Katayama et al, 1993). However, most of these peptide and aminoacid mixtures used as ingredients in cosmetics contain either chemically synthesized peptides, or peptides obtained by the partial digestion of animal proteins, like collagen and elastin (Mokrejs et al, 2009;Langmaier et al, 2002). The use of peptides produced by hydrolysis of animal proteins always involves certain risks associated with the use of any product derived from animals.…”

Separation of angiotensin I‐converting enzyme inhibitory peptides from bovine connective tissue and their stability towards temperature, pH and digestive enzymes

“…The meat processing industry produces considerable quantities of slaughter by-products every year. They are highly underutilised and regarded as huge wastes and potential pollution to the environment (Mokrejs et al, 2009). Connective tissue, accounting for 9-12% of meat by weight, is a major constituent of meat slaughter and processing by-products (Jayathilakan et al, 2012).…”

Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

“…Collagen does not express antigenicity in physiological conditions, it is completely resorbable in vivo and its physicochemical properties can be suitably controlled. Because of its unique biological and functional properties, collagen has been widely applied in food, cosmetic, base for smart hydrogels and medicine [8][9][10][11][12][13] . At the present there is wide interest in collagen as biomaterials.…”