Abstrak 
Water Soluble Collagen Of Oreochromis Niloticus Skin As Substrate For Collagenase Produced By Bacillus Subtilis ATCC 6633
Nadia Sekar Ayuningtyas, Junianto, Emma Rochima
Universitas Padjadjaran, International Journal of Fisheries and Aquatic Studies 2016; 4(5): 123-126 ISSN: 2347-5129
Bahasa Inggris
Universitas Padjadjaran, International Journal of Fisheries and Aquatic Studies 2016; 4(5): 123-126 ISSN: 2347-5129
Collagenolytic activity, eukaryotic enzyme, freshwater fish, nile tilapia, tilapia
Collagen is the major insoluble fibrous protein in the extra cellular matrix and connective tissues. It has a wide range of application in cosmetics, biomedical, pharmaceutical, leather and food industries. Collagen can be extracted from fish scales and skin by enzymatic digestion methods. The aim of this research was to study the water soluble collagen isolated from Oreochromis niloticus skin with collagenase produced by Bacillus subtilis ATCC 6633 (a collection of Microbiology Laboratory, Faculty of Pharmacy, Universitas Padjadjaran, Indonesia). Oreochromis niloticus was selected as collagen source due to its high content of collagen. Results showed that water soluble collagen (WSC) substrate isolated from Oreochromis niloticus skin contained 1.978 mg/mL of protein, whilst collagenase extracted from Bacillus subtilis ATCC 6633 contained 0.326 mg/mL of protein. Furthermore, the highest collagenolytic activity was obtained at 50 °C (1.298 U/ml) and pH 8 (1.696 U/ml). Water soluble collagen of Oreochromis niloticus skin as substrate for collagenase extracted from Bacillus subtilis ATCC 6633 positively exerted collagenolytic activity. It can be concluded that the optimum condition for collagenolytic activity of the enzyme is at temperature 50 oC and pH 8.