Zimogram aktivitas kolagenase dari bacillus licheniformis F-11.1 dan F-11.4.

Abstract

Bacillus licheniformis F-11.1 and F-11.4 are strains from B. lichniformis F-11 were isolated from shrimp shell waste in Palembang, Indonesia. They has poliglutamat acid mutation in the operon (PGA) and chitinase AB, so it doesn’t have chitinase activity, but high protease activity. Collagenase plays an important role in the softening of meat and the wound healing process. Precipitation enzyme can use ammonium sulfate to stabilize the enzyme, therebly reducing protein denaturation. Zimogram is an electrophoresis technique to determine the activity of an enzyme in situ and qualitative results of the gel electrophoresis. This research was conduct to analyze the activity Bacillus licheniformis F-11.1 and F-11.4 collagenase qualitatively using techniques zimogram. Analysis is performed on both isolates that grown in three growth media, ie LB + 5% collagen (LBC), ½ LB + 5% collagen (LBHC), and 5% collagen (CLG). Bacillus licheniformis F-11.1 and F-11.4 produce collagenase in the three growth media were added collagen as the substrate growth. Cell growth both isolates best on LBC media. Zimogram showed B. licheniformis F-11.1 and F-11.4 produce collagenase. It shown by the formation of clear zone on the gel due to degradation of collagen by collagenase. Isolates B. licheniformis F-11.1 produce the highest fraction of enzyme crude extract derived from LBC media is 32 fraction. Meanwhile isolates B. lichniformis F-11.4 produce the highest fraction of crude extract derived from LBHC media is 37 fraction