Production and Characterization of Collagenolytic Protease from Bacillus licheniformis F11.4 Originated from Indonesia

Ace Baehaki; Dahrul Syah; Siswa Setyahadi; Maggy T. Suhartono

doi:10.14233/ajchem.2014.15863

Issue

Vol. 26 No. 10 (2014): Vol 26 Issue 10

Issue Published : May 10, 2014

This work is licensed under a Creative Commons Attribution 4.0 International License.

Production and Characterization of Collagenolytic Protease from Bacillus licheniformis F11.4 Originated from Indonesia

https://doi.org/10.14233/ajchem.2014.15863

Ace Baehaki

Department of Fisheries Product Technology, Faculty of Agriculture, Sriwijaya University, Indralaya, South Sumatera, Indonesia

Dahrul Syah

Department of Food Science and Technology, Faculty of Agricultural Technology, Bogor Agricultural University, Bogor, Indonesia

Siswa Setyahadi

Agency for the Assessment and Application of Technology, Republic of Indonesia, Jakarta, Indonesia

Maggy T. Suhartono

Department of Food Science and Technology, Faculty of Agricultural Technology, Bogor Agricultural University, Bogor, Indonesia

Corresponding Author(s) : Maggy T. Suhartono

mthenawidjaja@yahoo.com

Asian Journal of Chemistry, Vol. 26 No. 10 (2014): Vol 26 Issue 10
Article Published : May 10, 2014

Abstract

Two mutant derivatives of the potent protease producing Bacillus licheniformis strain F11, originally isolated from Palembang, Sumatera, were checked for their capacity to secrete proteases: B. licheniformis F11.1, with a frame shift mutation in chiA and having deleted the genes for polyglutamate synthesis (genotype DchiA; Dpga) and B. licheniformis F11.4 with a deletion spanning both of the chitinase encoding genes (genotype DchiAB; Dpga). Bacillus licheniformis F11.4 was screened and isolated from Palembang, Indonesia. The bacteria produced collagenase enzyme when grown in a collagen media. The purpose of this study was to characterize the collagenase enzyme. Addition of collagen in the media accelerated the collagenase production time and increase the activity. The optimal temperature and pH of the enzyme were 50 °C and pH 9, respectively. At pH 12, the collagenase activity was still high. Collagenase activity was inhibited by Cu²⁺ (I mM) and stimulated by Co²⁺ (1 mM), Mg²⁺ (1 mM) and Ca²⁺ (1 mM). The collagenase from B. licheniformis F11.4 was capable of hydrolyzing collagen and other protein substrates such as casein, gelatin and fibrin.

Keywords

Collagenase Characterization Bacillus licheniformis F11.4

Baehaki, A., Syah, D., Setyahadi, S., & T. Suhartono, M. (2014). Production and Characterization of Collagenolytic Protease from Bacillus licheniformis F11.4 Originated from Indonesia. Asian Journal of Chemistry, 26(10), 2861–2864. https://doi.org/10.14233/ajchem.2014.15863

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References

M.D. Bond and H.E. Van Wart, Biochem., 23, 3085 (1984); doi:10.1021/bi00308a036.
T. Hisano, S. Abe, M. Wakashiro, A. Kimura and K. Murata, J. Ferment. Bioeng., 68, 399 (1989); doi:10.1016/0922-338X(89)90094-9.
S. Asdornnithee, K. Akiyama, T. Sasaki and R. Takata, J. Ferment. Bioeng., 78, 283 (1994); doi:10.1016/0922-338X(94)90358-1.
Q. Wu, C. Li, C. Li, H. Chen and L. Shuliang, Appl. Biochem. Biotechnol., 160, 129 (2010); doi:10.1007/s12010-009-8673-1.
Y. Sakurai, H. Inoue, W. Nishii, T. Takahashi, Y. Iino, M. Yamamoto and K. Takahashi, Biosci. Biotechnol. Biochem., 73, 21 (2009); doi:10.1271/bbb.80357.
D. Petrova, A. Derekova and S. Vlahov, Folia Microbiol., 51, 93 (2006); doi:10.1007/BF02932162.
S. Asdornnithee, K. Akiyama, T. Sasaki and R. Takata, Biosci. Biotechnol. Biochem., 57, 1894 (1993); doi:10.1271/bbb.57.1894.
J. Waldeck, D. Daum, B. Bisping and F. Meinhardt, Appl. Environ. Microbiol., 72, 7879 (2006); doi:10.1128/AEM.00938-06.
K. Hoffmann, G. Daum, M. Koster, W.M. Kulicke, H. Meyer-Rammes, B. Bisping and F. Meinhardt, Appl. Environ. Microbiol., 76, 8211 (2010); doi:10.1128/AEM.01404-10.
H.U. Bergmeyer, M. Graßl and H.E. Walter, in ed.: H.U. Bergmeyer and M. Grapl, Methods of Enzymatic Analysis, Weinheim: Verlag Chemie (1983).
M.M. Bradford, Anal. Biochem., 72, 248 (1976); doi:10.1016/0003-2697(76)90527-3.
U.K. Laemmli, Nature, 227, 680 (1970); doi:10.1038/227680a0.
N.S. Choi, K.S. Yoon, J.Y. Lee, K.Y. Han and S.H. Kim, J. Biochem. Mol. Biol., 34, 531 (2001).
I.H. Tran and H. Nagano, J. Food Sci., 67, 1184 (2002); doi:10.1111/j.1365-2621.2002.tb09474.x.
W.C.A. Nascimento and M.L.L. Martins, Braz. J. Microbiol., 35, 91 (2004); doi:10.1590/S1517-83822004000100015.
K. Adinarayana, P. Ellaiah and D.S. Prasad, AAPS PharmSciTech, 4, 440 (2003); doi:10.1208/pt040456.
M. Okamoto, Y. Yonejima, Y. Tsujimoto, Y. Suzuki and K. Watanabe, Appl. Microbiol. Biotechnol., 57, 103 (2001); doi:10.1007/s002530100731.
N. Hiroko and A.T. Kim, Biosci. Biotechnol. Biochem., 64, 181 (1999).
R. Chakraborty and A.L. Chandra, J. Appl. Bacteriol., 61, 331 (1986); doi:10.1111/j.1365-2672.1986.tb04294.x.
K.B. Beg, V. Sahai and R. Gupta, Process Biochem., 39, 203 (2003); doi:10.1016/S0032-9592(03)00064-5.

References

M.D. Bond and H.E. Van Wart, Biochem., 23, 3085 (1984); doi:10.1021/bi00308a036.

T. Hisano, S. Abe, M. Wakashiro, A. Kimura and K. Murata, J. Ferment. Bioeng., 68, 399 (1989); doi:10.1016/0922-338X(89)90094-9.

S. Asdornnithee, K. Akiyama, T. Sasaki and R. Takata, J. Ferment. Bioeng., 78, 283 (1994); doi:10.1016/0922-338X(94)90358-1.

Q. Wu, C. Li, C. Li, H. Chen and L. Shuliang, Appl. Biochem. Biotechnol., 160, 129 (2010); doi:10.1007/s12010-009-8673-1.

Y. Sakurai, H. Inoue, W. Nishii, T. Takahashi, Y. Iino, M. Yamamoto and K. Takahashi, Biosci. Biotechnol. Biochem., 73, 21 (2009); doi:10.1271/bbb.80357.

D. Petrova, A. Derekova and S. Vlahov, Folia Microbiol., 51, 93 (2006); doi:10.1007/BF02932162.

S. Asdornnithee, K. Akiyama, T. Sasaki and R. Takata, Biosci. Biotechnol. Biochem., 57, 1894 (1993); doi:10.1271/bbb.57.1894.

J. Waldeck, D. Daum, B. Bisping and F. Meinhardt, Appl. Environ. Microbiol., 72, 7879 (2006); doi:10.1128/AEM.00938-06.

K. Hoffmann, G. Daum, M. Koster, W.M. Kulicke, H. Meyer-Rammes, B. Bisping and F. Meinhardt, Appl. Environ. Microbiol., 76, 8211 (2010); doi:10.1128/AEM.01404-10.

H.U. Bergmeyer, M. Graßl and H.E. Walter, in ed.: H.U. Bergmeyer and M. Grapl, Methods of Enzymatic Analysis, Weinheim: Verlag Chemie (1983).

M.M. Bradford, Anal. Biochem., 72, 248 (1976); doi:10.1016/0003-2697(76)90527-3.

U.K. Laemmli, Nature, 227, 680 (1970); doi:10.1038/227680a0.

N.S. Choi, K.S. Yoon, J.Y. Lee, K.Y. Han and S.H. Kim, J. Biochem. Mol. Biol., 34, 531 (2001).

I.H. Tran and H. Nagano, J. Food Sci., 67, 1184 (2002); doi:10.1111/j.1365-2621.2002.tb09474.x.

W.C.A. Nascimento and M.L.L. Martins, Braz. J. Microbiol., 35, 91 (2004); doi:10.1590/S1517-83822004000100015.

K. Adinarayana, P. Ellaiah and D.S. Prasad, AAPS PharmSciTech, 4, 440 (2003); doi:10.1208/pt040456.

M. Okamoto, Y. Yonejima, Y. Tsujimoto, Y. Suzuki and K. Watanabe, Appl. Microbiol. Biotechnol., 57, 103 (2001); doi:10.1007/s002530100731.

N. Hiroko and A.T. Kim, Biosci. Biotechnol. Biochem., 64, 181 (1999).

R. Chakraborty and A.L. Chandra, J. Appl. Bacteriol., 61, 331 (1986); doi:10.1111/j.1365-2672.1986.tb04294.x.

K.B. Beg, V. Sahai and R. Gupta, Process Biochem., 39, 203 (2003); doi:10.1016/S0032-9592(03)00064-5.

Issue

Vol. 26 No. 10 (2014): Vol 26 Issue 10

Production and Characterization of Collagenolytic Protease from Bacillus licheniformis F11.4 Originated from Indonesia

Corresponding Author(s) : Maggy T. Suhartono

Abstract

Keywords

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