CLC number: Q55
On-line Access:
Received: 2007-04-28
Revision Accepted: 2007-09-19
Crosschecked: 0000-00-00
Cited: 14
Clicked: 5587
ZHU Xu-fen, ZHOU Ying, FENG Jun-li. Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5[J]. Journal of Zhejiang University Science B, 2007, 8(11): 831-838.
@article{title="Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5",
author="ZHU Xu-fen, ZHOU Ying, FENG Jun-li",
journal="Journal of Zhejiang University Science B",
volume="8",
number="11",
pages="831-838",
year="2007",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2007.B0831"
}
%0 Journal Article
%T Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5
%A ZHU Xu-fen
%A ZHOU Ying
%A FENG Jun-li
%J Journal of Zhejiang University SCIENCE B
%V 8
%N 11
%P 831-838
%@ 1673-1581
%D 2007
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2007.B0831
TY - JOUR
T1 - Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5
A1 - ZHU Xu-fen
A1 - ZHOU Ying
A1 - FENG Jun-li
J0 - Journal of Zhejiang University Science B
VL - 8
IS - 11
SP - 831
EP - 838
%@ 1673-1581
Y1 - 2007
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2007.B0831
Abstract: A novel chitinolytic and chitosanolytic bacterium, Sphingomonas sp. CJ-5, has been isolated and characterized. It secretes both chitinase and chitosanase into surrounding medium in response to chitin or chitosan induction. To characterize the enzymes, both chitinase and chitosanase were purified by ammonium sulfate precipitation, Sephadex G-200 gel filtration and DEAE-Sepharose Fast Flow. SDS-PAGE analysis demonstrated molecular masses of chitinase and chitosanase were 230 kDa and 45 kDa respectively. The optimum hydrolysis conditions for chitinase were about pH 7.0 and 36 °C, and these for chitosanase were pH 6.5 and 56 °C, respectively. Both enzymes were quite stable up to 45 °C for one hour at pH 5~8. These results show that CJ-5 may have potential for industrial application particularly in recycling of chitin wastes.
[1] Carstens, M., Vivier, M.A., Pretorius, I.S., 2003. The Saccharomyces cerevisiae chitinase, encoded by the CTS1-2 gene, confers antifungal activity against Botrytis cinerea to transgenic tobacco. Transgenic. Res., 12(4):497-508.
[2] Chernin, L.S., De la Fuente, L., Sobolev, V., Haran, S., Vorgias, C.E., 1997. Molecular cloning, structural analysis and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans. Appl. Environ. Microbiol., 63(3):834-839.
[3] Cohen-Kupiec, R., Che, I., 1998. The molecular biology of chitin digestion. Curr. Opin. Biotechnol., 9(3):270-277.
[4] Dong, X.Z., Cai, M.Y., 2001. Determinative Manual of Common Bacterial Systems. Scientific Press, Beijing (in Chinese).
[5] Flach, J., Pilet, P.E., Jolles, P., 1992. What’s new in chitinase research. Experientia, 48(8):701-716.
[6] Folders, J., Algra, J., Roelofs, M.S., Loon, L.C., Tommmassen, J., Bitter, W., 2001. Characterization of Pseudomonas aeruginosa chitianase, a gradually secreted protein. J. Bacteriol., 183(24):7044-7052.
[7] Gal, S.W., Choi, J.Y., Kim, C.Y., Cheong, Y.H., Cheong, Y.J., Choi, Y.J., Bahk, J.D., Lee, S.Y., Cho, M.J., 1998. Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme. FEMS Microbiol. Lett., 160(1):151-158.
[8] Gleave, A.P., Taylor, R.K., Morris, B.A.M., Greenwood, D.R., 1995. Cloning and sequencing of a gene encoding the 69-kDa extracellular chitinase of Janthinobacterium lividum. FEMS Microbiol. Lett., 131(3):279-288.
[9] Gooday, G.W., 1990. The Ecology of Chitin Degrationtic. In: Marshall, K.C. (Ed.), Advance in Microbiol Ecology. New Plenum Press, NY, Vol. 11, p.387-430.
[10] Gooday, G.W., 1997. The many uses of chitinases in nature. Chitin. Chitosan. Res., 3:233-243.
[11] Hayes, C.K., Klemsdal, S., Lorito, M., Di, P.A., Peterbauer, C., Nakas, J.P., Tronsmo, A., Harman, G.E., 1994. Isolation and sequence of an endochitinase-encoding gene from a cDNA libray of Trichoderma harzianum. Gene, 138(1-2):143-148.
[12] Helistö, P., Aktuganov, G., Galimzianova, N., Melentjev, A., Korpela, T., 2001. Lytic enzyme complex of an antagonistic Bacillus sp. X-b: isolation and purification of components. J. Chromatogr. B Biomed. Sci. Appl., 758(2):197-205.
[13] Henrissat, B., Bairoch, A., 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293(3):781-788.
[14] Henrissat, B., Davies, G., 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol., 7(5):637-644.
[15] Hirano, S., 1989. Production and Application of Chitin and Chitosan in Japan. In: Chitin and Chitosan. Elsevier, Essex, p.37-43.
[16] Hirano, S., 1996. Chitin biotechnology applications. Biotechnol. Annu. Rev., 2:237-258.
[17] Kang, S.C., Sanggyu Park, S., Lee, D.G., 1998. Isolation and characterization of a chitinase cDNA from the entomopathogenic fungus, Metarhizium anisopliae. FEMS Microbiol. Lett., 165(2):267-271.
[18] Kawase, T., Saito, A., Sato, T., Kanai, R., Fujii, T., Nikaidou, N., Miyashita, K., Watanabe, T., 2004. Distribution and phylogenetic analysis of family 19 chitinases in Actinobacteria. Appl. Environ. Microbiol., 70(2):1135-1144.
[19] Kawase, T., Yokokawa, S., Saito, A., Fujii, T., Nikaidou, N., Miyashita, K., Watanabe, T., 2006. Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from Streptomyces coelicolor A3(2). Biosci. Biotechnol. Biochem., 70(4):988-998.
[20] Laemmli, U.K., 1970. Cleavage of structural proteins duing the assembly of the head of bacteriophage T4. Nature, 227(5259):680-685.
[21] Lan, X., Zhang, X., Hu, J., Shimosaka, M., 2006. Cloning, expression and characterization of a chitinase from the chitinolytic bacterium Aeromonas hydrophila strain SUWA-9. Biosci. Biotechnol. Biochem., 70(10):2437-2442.
[22] McCreath, K.J., Specht, C.A., Robbins, P.W., 1995. Molecular cloning and characterization of chitinase genes from Candida albicans. Proc. Natl. Acad. Sci. USA, 92(7):2544-2548.
[23] Mendonsa, E.S., Vartak, P.H., Rao, J.U., Deshpande, M.V., 1996. An enzyme from Myrothecium verrucaria that degrades insect cuticles for biocontrol of Aedes aegypti mosquito. Biotechnol. Lett., 18(4):373-376.
[24] Morimoto, K.S., Karita, T., Kirchman, D.L., 1993. Role of chitinase proteins in the specific attachment of the marine bacterium Vibrio harveyi to chitin. Appl. Environ. Microbiol., 59(2):373-379.
[25] Morimoto, K.S., Karita, T., Kimura, T., Sakka, K., Ohmiya, K., 1997. Cloning, sequencing, and expression of the gene encoding Clostridium paraprtrificum chitinase chiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J. Bacteriol., 179(23):7306-7314.
[26] Park, J.K., Okamoto, T., Yamasaki, Y., Tanaka, K., Nakagawa, T., Kawamukai, M., Matsuda, H., 1997. Molecular cloning, nucleotide sequencing, and regulation of chiA gene encoding one chitinase from Enterobacter sp. G-1. J. Ferment. Bioeng., 84(6):493-501.
[27] Pishko, E.J., Kirkland, T.N., Cole, G.T., 1995. Isolation and characterization of two chitinase-encoding genes (cts1, cts2) from the fungus Coccidioides immittis. Gene, 167(1-2):173-177.
[28] Rivas, L.A., Parro, V., Moreno-Paz, M., Mellado, R., 2000. The Bacillus subtilis 168 csn gene encodes a chitosanas with similar properties to a Streptomyces enzyme. Microbiology, 146:2929-2936.
[29] Saito, J., Kito, A., Higuchi, Y., Nagata, Y., Ando, A., Miki, K., 1999. Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism. J. Biol. Chem., 274(43):30818-30825.
[30] Sakka, K., Kusaka, R., Kawano, A., Karita, S., Sukhumavasi, J., Kimura, T., Ohmiya, K., 1998. Cloning and sequencing of the gene encoding chitinase ChiA from Xanthomonas sp. strain AK and some properties of ChiA. J. Ferment. Bioeng., 86(6):527-533.
[31] Sandorf, P.A., 1989. Chitosan: Commercial Uses and Potential Applications. In: Chitin and Chitosan, Elsevier, London, p.51-69.
[32] Somashekar, D., Joseph, R., 1996. Chitosanase-properities and applications: a review. Bioresource Technology, 55(1):35-45.
[33] Sun, Y., Liu, W., Han, B., Zhang, J., Liu, B., 2006. Purification and characterization of two types of chitosanase from a Microbacterium sp. Biotechnol. lett., 28(17):1393-1399.
[34] Techkarnjanaruk, S., Goodman, A.E., 1999. Multiple genes involved in chitin degradation from the marine bacterium Pseudoalteromonas sp. strain S91. Microbiology, 145(4):925-934.
[35] Tsujibo, H., Orikoshi, H., Tanno, H., Fujimoto, K., Miyamoto, K., Imada, C., Okami, Y., Inamori, Y., 1993. Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J. Bacteriol., 175(1):176-181.
[36] Watanabe, T., Kanai, R., Kawase, T., Tanabe, T., Mitsutomi, M., Sakuda, M., Miyashita, K., 1999. Family 19 chitinases of Streptomyces species: characterization and distribution. Microbiology, 145(12):3353-3363.
[37] Xia, G., Jin, C., Zhou, J., Yang, S., Jin, C., 2001. A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407. Eur. J. Biochem., 268(14):4079-4085.
[38] Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T., 1988. Purification and properties of chitosanase from Bacillus circulans MH-K1. J. Gen. Appl. Microbiol., 34:255-270.
[39] Yamasaki, Y., Ohto, Y., Morita, K., Nakagawa, T., Kawamukai, M., Matsuda, H., 1992. Isolation, identification, and effect of oxygen supply on cultivation of chitin and chitosan degrading bacterium. Biosci. Biotech. Biochem., 56(8):1325-1326.
[40] Yanai, K., Takaya, N., Kojima, N., Horiuchi, H., Ohta, A., Takagi, M., 1992. Purification of two chitinase from Rhizopus oligosporus and isolation and sequencing of the encoding genes. J. Bacteriol., 174(22):7398-7406.
[41] Zhu, X.F., Wu, X.Y., Dai, Y., 2003. Fermentation conditions and properties of a chitosanase from Acinetobacter sp. C-17. Biosci. Biotechnol. Biochem., 67(2):284-290.
Open peer comments: Debate/Discuss/Question/Opinion
<1>