Abstract
Indonesian local “Kacang” goat is an animal species widely known by consumers over the world which possesses many health effects. Goatskin is one of body parts which has potential as collagen sources. The optimal conditions for collagen extraction were determined by response surface methodology in this study. Multiple response optimization designs were applied to evaluate the effects of two independent variables (curing time of NaOH and hydrolysis time) on the pepsin-soluble collagen yield of Indonesian local “Kacang” goatskin. Correlation analysis of the mathematical regression model indicated that quadratic polynomial model could be employed to optimize the extraction of pepsin-soluble collagen. The optimal conditions to obtain the highest yield of pepsin-soluble collagen was without curing NaOH and 24 h time of hydrolysis.
Highlights
Indonesian local “Kacang” goatskin has a high population in Indonesian and it is not too exposed as collagen sources especially as healthy products
The objective of this work was to investigate the collagen extraction from local Indonesian “Kacang” goatskin which has a high population in Indonesian, mainly to the effects of above two variables on the yield of pepsin-soluble collagen by response surface methodology
The yield of pepsin-soluble collagen was decreased with the extension time of treatment of NaOH and hydrolysis time with pepsin
Summary
Indonesian local “Kacang” goatskin has a high population in Indonesian and it is not too exposed as collagen sources especially as healthy products. Previous research has many reported the extraction of collagen sources from by-products of bovine, pig, chicken, rabbit and fish. There was no information about collagen extraction from goatskin. Collagen is a product which highly demanded and it used in the cosmetic, pharmaceutics and food industry. Collagen can be found in all animal parts but is mainly concentrated the skin and bone (Nakamura et al, 2003). Collagen is the product of an almost continuous repeating of the GlyX-Y-sequence and the most abundant structural protein has formed as a unique triple helix by three almost identical polypeptide amino acids chain (Pal et al, 2015; Gómez-Guillén et al, 2011)
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