Characterization and physicochemical properties of collagen extracted from barramundi (Lates calcarifer, block) skin
TL;DRAbstract
Collagens from barramundi (Lates calcarifer) skins were extracted by alkaline pretreatment with mild acid extraction (0.5 M acetic acid); with and without (ASC) the addition of pepsin (PSC) and papain (PaSC). The use of papain was studied to replace the use of conventional enzyme, pepsin, in the collagen extraction process, which is of haram or non-halal origin. The collagens obtained were evaluated for their physico-chemical properties such as colour, odour, amino acid composition, molecular weight distribution and solubility haracteristics. Optimization for collagen extraction using papain was carried out by Response Surface Methodology (RSM). The selected independent variables were papain concentration (10-50 kUnit/g) and extraction time (12-36 hr) with dependent variables of yield,hydroxyproline, total amino acid and imino acid content. Comparisons were then carried for the collagen obtained from the optimized process with commercial mammalian and tilapia collagens in their am
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Collagens from barramundi (Lates calcarifer) skins were extracted by alkaline pretreatment with mild acid extraction (0.5 M acetic acid); with and without (ASC) the addition of pepsin (PSC) and papain (PaSC). The use of papain was studied to replace the use of conventional enzyme, pepsin, in the collagen extraction process, which is of haram or non-halal origin. The collagens obtained were evaluated for their physico-chemical properties such as colour, odour, amino acid composition, molecular weight distribution and solubility haracteristics. Optimization for collagen extraction using papain was carried out by Response Surface Methodology (RSM). The selected independent variables were papain concentration (10-50 kUnit/g) and extraction time (12-36 hr) with dependent variables of yield,hydroxyproline, total amino acid and imino acid content. Comparisons were then carried for the collagen obtained from the optimized process with commercial mammalian and tilapia collagens in their am
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