Obtenção de colágeno hidrolisado a partir da hidrólise enzimática da raspa do couro bovino

Abstract

Hydrolyzed collagen is used as food supplement, with intention to supply the collagen loss that occurs by aging. With long polypeptide chain and molecular weight of about 300 kDa, the native form of collagen presents low absorption by the human body. To obtain an easy absorbable product, hydrolysis of collagen by enzymes action is necessary, whereas collagen from variables fonts has been used as raw material as fish leather, chicken leather, and others. The aim of this work was to treat collagen from bovine hide splits by deferent enzymes to obtain collagen peptides fractions easy absorbable by the human body. The isolated collagen was digested by 6 deferent enzymes (pepsin, collagenase, neutrase, trypsin, papain and alcalase) in concentrations of 0,5 e 1 g/100g E/S by 1, 2 and 4 hours treatment. After treatments, the products from digestions were submitted to electrophoresis (SDS-PAGE) for evaluation of molecular weight obtained. Independent of time and concentration of enzymes used, the treatment with pepsin and collagenase showed peptidic fraction over 40 kDa. Treatments with neutrase and trypsin showed wide interval of peptidic fraction, being that the products obtained ranged from 10 to 120 kDa. The best peptidic fractions were obtained by treatments with the enzymes papain and alcalase. The papain did not produced defined band and the fractioning showed dependent of time and concentration of enzyme, whereas produced only fractions lower than 25 kDa after 4 hours treatment with 1 g/100g E/S. however the treatment containing 0,5 g/100g of alcalase by 4 hours, and the ones with 1 g/100g of this enzyme were capable to fractionate all the collagen content in band lower than 25 kDa. The papain although has produced fraction lower than 25 kDa, showed lower efficiency when compared to alcalase, that reached the goal in a shorter time and concentration. In this way papain and alcalase showed potential on hydrolyzed collagen production. Further studies involving booth enzymes should be made, to characterize the hydrolysate produced and the commercial application.