Extraction and Characterization of Gelatin from Rabbitfish Siganus canaliculatus Skin with Enzimatic Methode Using Bromelin Enzyme Dian Haryati, Lulu Nadhifa, Humairah, Nurlaela Abdullah
Hasanuddin University
Abstract
Gelatine basically is a pure protein food ingredient, obtained from thermal denaturation of collagen from animals. Gelatine is used as a stabilizer, gelling agent, binder, thickener, emulsifier, adhesive, whipping agent, and edible coating food wrap. Protein levels in fish skin determine the amount of collagen contained in skin tissue, so the Rabbitfish skin has a great potential as a source of collagen to be hydrolyzed into gelatine. This study aimed to determine the characteristics of gelatine produced from Rabbitfish skin by enzymatic extraction as well as to determine the best treatment of a combination of enzyme concentrations and extraction time. Gelatine production was carried out by hydrolysis using Bromelain enzyme at a level of 1%, 1.5% and 2% with the extraction time of 2 hours, 4 hours, and 6 hours. The result obtained was gelatine with rendement ranging from 3,13 up to 5,83%, the water content ranged from 0,17 up to 3,56%, ash content 0,35 up to 3,65%, and protein levels ranged from 91 up to 94,72%. The chemical characteristics of gelatine from Rabbitfish skin have a yield of up to 6%, water content less than 6%, ash content less than 4% and protein content reaching 94%. The best treatment was obtained at 1% enzyme concentration and 4 hours extraction time, yielded gelatine with a protein content of 94,72%.
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