Purification and characterization of collagenase from Bacillus licheniformis F11.4

Baehaki, Ace and Suhartono, Maggy Thenawidjaja and Sukarno, Sukarno and Syah, Dahrul and Sitanggang, Azis B. and Setyahadi, Siswa and Meinhardt, Friedhelm (2012) Purification and characterization of collagenase from Bacillus licheniformis F11.4. African Journal of Microbiology Research, 6 (10). pp. 2373-2379. ISSN 1996-0808

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Abstract

The extracellular collagenase, produced by Bacillus licheniformis F11.4, was purified by ammonium sulfate precipitation followed by DEAE Sephadex A-50. The purified collagenase showed a 26.3-fold increase in specific activity being 1.0 U/mg and 2.6% recovery. The collagenase has an apparent molecular weight of 124 and 26 kD as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymography. The optimal temperature and pH were 50°C and pH 7.0, respectively. The collagenase activity was inhibited by Fe2+ (1 mM), Mg2+ (1 mM), Mn2+ (1 mM), Co2+ (1 mM), EDTA (1 mM), and β-mercaptoetanol (1 mM). However, Ca2+ (1 mM) and Cu2+ (1 mM) increased its activity. The collagenase from B. licheniformis F11.4 was capable of hydrolyzing other protein substrates such as casein, gelatin, and fibrin. The Km and Vmax of the enzyme for collagen were 0.26 mg/ml and 0.27 U, respectively

Item Type:	Article
Uncontrolled Keywords:	Collagenase, Bacillus licheniformis F11.4, purification, characterization.
Subjects:	S Agriculture > SH Aquaculture. Fisheries. Angling > SH201-399 Fisheries
Divisions:	05-Faculty of Agriculture > 54244-Fisheries Product Technology (S1)
Depositing User:	Dr. Ace Baihaki
Date Deposited:	02 Aug 2019 08:52
Last Modified:	02 Aug 2019 08:52
URI:	http://repository.unsri.ac.id/id/eprint/1976

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