Produksi Kolagenase dari Isolat Bacillus licheniformis F-11.1 dan F-11.4
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Date
2012Author
Octivianti, Cindy Theresia
Budiarti, Sri
Suhartono, Maggy Thenawidjaja
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Hydrolysis by collagenase enzyme could increase nutrition and function of food proteins. This research was conducted to produce collagenase enzyme from Bacillus licheniformis F-11.1 and F- 11.4. B. licheniformis isolate F-11.1 and F-11.4 were cultured in three types of production media, which is Luria Bertani (LB) media consisted of 5% collagen (LBC), 50% LB media consisted of 5% collagen (LBHC), and 5% collagen (CLG). The activity of collagenase, protein content, and cell turbidity of B. licheniformis F-11.1 and F-11.4 were measured every 5 hours during 50 hours incubation. The result showed that optimum collagenase production of B. licheniformis isolate F- 11.1 was reached in LBC and LBHC media with activity of 2,057 U/mg and 2,037 U/mg, respectively. Optimum collagenase production of B. licheniformis isolate F-11.4 was reached in LBC media with activity of 4,695 U/mg. Isolate F-11.4 in LBHC media possesed the optimum collagenase activity of 2,811 U/mg. CLG media gave optimum collagenase activity of B. licheniformis F-11.1 and F-11.4 at 0,807 U/mg and 0,306 U/mg respectively. These research concluded that LBC and LBHC media was the best choice for collagenase production of B. licheniformis F-11.1 and F-11.4.
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