Isolation and characterisation of ovine collagen hydrolysates following thermal and different enzymatic treatments


Citation

León-López A., . and Aguirre-Cruz G., . and Aguirre-�lvarez G., . and �ngeles-Santos C., . and Jiménez-Alvarado R., . Isolation and characterisation of ovine collagen hydrolysates following thermal and different enzymatic treatments. pp. 1038-1045. ISSN 2231-7546

Abstract

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 50C). The viscosity hydroxyproline content isoelectric point and molecular weight were measured to establish the optimum conditions for enzymatic hydrolysis. Collagen hydrolysis was conducted at 50C for 24 h. Treatment with Po resulted in the lowest viscosity (0.23 mPas) 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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Abstract

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 50C). The viscosity hydroxyproline content isoelectric point and molecular weight were measured to establish the optimum conditions for enzymatic hydrolysis. Collagen hydrolysis was conducted at 50C for 24 h. Treatment with Po resulted in the lowest viscosity (0.23 mPas) 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.

Additional Metadata

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Item Type: Article
AGROVOC Term: Collagen
AGROVOC Term: Sheep
AGROVOC Term: Hydrolysis
AGROVOC Term: Enzymatic hydrolysis
AGROVOC Term: Thermal treatment
AGROVOC Term: Enzymes
AGROVOC Term: Viscosity
AGROVOC Term: Hydroxyproline
AGROVOC Term: Isoelectric point
AGROVOC Term: Molecular weight
Depositing User: Mr. AFANDI ABDUL MALEK
Last Modified: 24 Apr 2025 00:55
URI: http://webagris.upm.edu.my/id/eprint/9445

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