Isolation and characterisation of ovine collagen hydrolysates following thermal and different enzymatic treatments
2020
León-López, A. | Aguirre-Cruz, G. | Aguirre-Álvarez, G. | Ángeles-Santos, C. | Jiménez-Alvarado, R.
Ovine collagen was hydrolysed by thermal treatment, followed by treatment with seven different commercial enzymes namely Heliozym (He), Propain 100 (Pro), Curtizyme (Cur), Cocktail (Ck), Fungal (Fu), Rohapon (Roh), and Polizym (Po), and compared with two control treatments (with and without thermal treatment at 50°C). The viscosity, hydroxyproline content, isoelectric point, and molecular weight were measured to establish the optimum conditions for enzymatic hydrolysis. Collagen hydrolysis was conducted at 50°C for 24 h. Treatment with Po resulted in the lowest viscosity (0.23 mPa*s) and yielded low molecular weight collagen fractions of around 20 kDa. The highest yield of hydroxyproline from collagen was reported for the Fu treatment at 12.65 mg/mL. The isoelectric point (pI) values differed significantly (p < 0.05) between the control treatments and the other treatments. The pI shifted from 8.5 (native collagen) to 2.0 in most of the hydrolysed collagens.
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