| dc.description.abstract | Collagen is a protein composed of a triple helix structure of amino acids glycine,
proline and hydroxyproline in a repeating manner. Chicken feet are a potential
source of collagen due to its abundant availability, but has not been optimally
utilized. The combination of two types of protease, namely papain and calotropin
enzymes, is expected to produce a good correlation and improve the enzyme
performance. The objective of this study is to determine the effect of papain and
calotropin enzyme concentration ratio on the properties of chicken foot collagen.
This study used a one-factor randomized group design (RAK) with variations in
papain and calotropin enzyme ratio of 100:0, 80:20, 60:40, 50:50, 40:60, 20:80,
and 0:100 (%, v/v). The chicken foot collagen extract was analyzed for enzyme
activity, yield, pH, water holding capacity, oil holding capacity, viscosity, collagen
solubility, antioxidant activity, effectiveness test, and collagen functional
groups.The best treatment was shown by 100% concentration of calotropin enzyme
with an effectiveness value of 0.69%. The value of each test parameter in the best
treatment included yield of 9.15%, pH of 6.73, water binding capacity of 0.35 g/g,
oil binding capacity of 2.90 g/g, viscosity of 2.14 cps, collagen solubility of 85.99%,
and antioxidant activity of 16.06%. A treatment with a combination of papain and
calotropin enzymes (20%:80%) was analyzed for its functional groups to confirm
the characteristics of the collagen peptides. The results of Fourier Transform
Infrared Spectroscopy (FTIR) spectra showed the absorption peaks of amides A, B,
I, II, and III at wave numbers 3306.15 2934.89 1642.72 1534.55 and 1241.15,
respectively. The analysis showed that the concentration ratio of papain and
calotropin enzymes significantly affected the properties of chicken foot collagen
extract, including yield, pH, water holding capacity, oil holding capacity, viscosity,
collagen solubility, and antioxidant activity. | en_US |
