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Volumn 133, Issue , 2013, Pages 213-220

Chitinase A from Stenotrophomonas maltophilia shows transglycosylation and antifungal activities

Author keywords

Antifungal activity; Chitinase; Chitooligosaccharides; Stenotrophomonas maltophilia; Transglycosylation

Indexed keywords

CLONING; ENZYMES; ESCHERICHIA COLI; GLYCOSYLATION;

EID: 84874354501     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2013.01.103     Document Type: Article
Times cited : (58)

References (32)
  • 1
    • 31444442746 scopus 로고    scopus 로고
    • Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation
    • Aronson N.N., Halloran B.A., Alexeyev M.F., Zhou X.E., Wang Y., Meehan E.J., Chen L. Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation. Biosci. Biotechnol. Biochem. 2006, 70:243-251.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 243-251
    • Aronson, N.N.1    Halloran, B.A.2    Alexeyev, M.F.3    Zhou, X.E.4    Wang, Y.5    Meehan, E.J.6    Chen, L.7
  • 2
    • 0035206324 scopus 로고    scopus 로고
    • Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48
    • Frankowski J., Lorito M., Scala F., Schmid R., Berg G., Bahl H. Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48. Arch. Microbiol. 2001, 176:421-426.
    • (2001) Arch. Microbiol. , vol.176 , pp. 421-426
    • Frankowski, J.1    Lorito, M.2    Scala, F.3    Schmid, R.4    Berg, G.5    Bahl, H.6
  • 3
    • 0035957051 scopus 로고    scopus 로고
    • Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis
    • Fukamizo T., Sasaki C., Schelp E., Bortone K., Robertus J.D. Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis. Biochemistry 2001, 40:2448-2454.
    • (2001) Biochemistry , vol.40 , pp. 2448-2454
    • Fukamizo, T.1    Sasaki, C.2    Schelp, E.3    Bortone, K.4    Robertus, J.D.5
  • 6
    • 33646130841 scopus 로고    scopus 로고
    • Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from Streptomyces coelicolor A3(2)
    • Kawase T., Yokokawa S., Saito A., Fujii T., Nikaidou N., Miyashita K., Watanabe T. Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from Streptomyces coelicolor A3(2). Biosci. Biotechnol. Biochem. 2006, 70:988-998.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 988-998
    • Kawase, T.1    Yokokawa, S.2    Saito, A.3    Fujii, T.4    Nikaidou, N.5    Miyashita, K.6    Watanabe, T.7
  • 7
    • 84856572622 scopus 로고    scopus 로고
    • Novel modular endo-β-1,4-xylanase with transglycosylation activity from Cellulosimicrobium sp. strain HY-13 that is homologous to inverting GH family 6 enzymes
    • Kim D.Y., Ham S.-J., Kim J.-H., Kim J., Lee M.-H., Cho H.-Y., Shin D.-H., Rhee Y.H., Son K.-H., Park H.-Y. Novel modular endo-β-1,4-xylanase with transglycosylation activity from Cellulosimicrobium sp. strain HY-13 that is homologous to inverting GH family 6 enzymes. Bioresour. Technol. 2012, 107:25-32.
    • (2012) Bioresour. Technol. , vol.107 , pp. 25-32
    • Kim, D.Y.1    Ham, S.-J.2    Kim, J.-H.3    Kim, J.4    Lee, M.-H.5    Cho, H.-Y.6    Shin, D.-H.7    Rhee, Y.H.8    Son, K.-H.9    Park, H.-Y.10
  • 8
    • 26244468501 scopus 로고    scopus 로고
    • Biological control of late leaf spot of groundnut (Arachis hypogaea L.,) with chitinolytic bacteria
    • Kishore G.K., Pande S., Podile A.R. Biological control of late leaf spot of groundnut (Arachis hypogaea L.,) with chitinolytic bacteria. Phytopathology 2005, 95:1157-1165.
    • (2005) Phytopathology , vol.95 , pp. 1157-1165
    • Kishore, G.K.1    Pande, S.2    Podile, A.R.3
  • 9
    • 0036195363 scopus 로고    scopus 로고
    • Characterization of a chitinase gene from Stenotrophomonas maltophilia strain 34S1 and its involvement in biological control
    • Kobayashi D.Y., Reedy R.M., Bick J., Oudemans P.V. Characterization of a chitinase gene from Stenotrophomonas maltophilia strain 34S1 and its involvement in biological control. Appl. Environ. Microbiol. 2002, 68:1047-1054.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1047-1054
    • Kobayashi, D.Y.1    Reedy, R.M.2    Bick, J.3    Oudemans, P.V.4
  • 10
    • 0030452755 scopus 로고    scopus 로고
    • Synthesis of artificial chitin: irreversible catalytic behavior of a glycosyl hydrolase through a transition state analogue substrate
    • Kobayashi S., Kiyosada T., Shoda S. Synthesis of artificial chitin: irreversible catalytic behavior of a glycosyl hydrolase through a transition state analogue substrate. J. Am. Chem. Soc. 1996, 118:13113.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 13113
    • Kobayashi, S.1    Kiyosada, T.2    Shoda, S.3
  • 11
  • 12
    • 84855609532 scopus 로고    scopus 로고
    • Purification and characterization of a novel chitinase gene from Paecilomyces thermophila expressed in Escherichia coli
    • Kopparapu N.K., Zhou P., Zhang S., Yan Q., Liu Z., Jiang Z. Purification and characterization of a novel chitinase gene from Paecilomyces thermophila expressed in Escherichia coli. Carbohydr. Res. 2011, 347:155-160.
    • (2011) Carbohydr. Res. , vol.347 , pp. 155-160
    • Kopparapu, N.K.1    Zhou, P.2    Zhang, S.3    Yan, Q.4    Liu, Z.5    Jiang, Z.6
  • 13
    • 0036226811 scopus 로고    scopus 로고
    • Degradation characteristics of toluene, benzene, ethylbenzene, and xylene by Stenotrophomonas maltophilia T3-c
    • Lee E.Y., Jun Y.S., Cho K.S., Ryu H.W. Degradation characteristics of toluene, benzene, ethylbenzene, and xylene by Stenotrophomonas maltophilia T3-c. J. Air Waste Manag. Assoc. 2002, 52:400-406.
    • (2002) J. Air Waste Manag. Assoc. , vol.52 , pp. 400-406
    • Lee, E.Y.1    Jun, Y.S.2    Cho, K.S.3    Ryu, H.W.4
  • 14
    • 61749102862 scopus 로고    scopus 로고
    • Purification and properties of a chitinase from Penicillium sp. LYG 0704
    • Lee Y.G., Chung K.C., Wi S.G., Lee J.C., Bae H.J. Purification and properties of a chitinase from Penicillium sp. LYG 0704. Protein Express. Purif. 2009, 65:244-250.
    • (2009) Protein Express. Purif. , vol.65 , pp. 244-250
    • Lee, Y.G.1    Chung, K.C.2    Wi, S.G.3    Lee, J.C.4    Bae, H.J.5
  • 15
    • 84871737296 scopus 로고    scopus 로고
    • Transglycosylation by chitinase D from Serratia proteamaculans improved through altered substrate interactions
    • Madhuprakash J., Tanneeru K., Purushotham P., Guruprasad L., Podile A.R. Transglycosylation by chitinase D from Serratia proteamaculans improved through altered substrate interactions. J. Biol. Chem. 2012, 287:44619-44627.
    • (2012) J. Biol. Chem. , vol.287 , pp. 44619-44627
    • Madhuprakash, J.1    Tanneeru, K.2    Purushotham, P.3    Guruprasad, L.4    Podile, A.R.5
  • 16
    • 11144340288 scopus 로고    scopus 로고
    • Whole cells of Bacillus subtilis AF 1 proved more effective than cell-free and chitinase-based formulations in biological control of citrus fruit rot and groundnut rust
    • Manjula K., Kishore G.K., Podile A.R. Whole cells of Bacillus subtilis AF 1 proved more effective than cell-free and chitinase-based formulations in biological control of citrus fruit rot and groundnut rust. Can. J. Microbiol. 2004, 50:737-744.
    • (2004) Can. J. Microbiol. , vol.50 , pp. 737-744
    • Manjula, K.1    Kishore, G.K.2    Podile, A.R.3
  • 18
    • 0030726362 scopus 로고    scopus 로고
    • Cloning, sequencing and expresión of the gene encoding Clostridium paraputrificum chitinase ChiB and análisis of the functions of novel cadherin-like domains and a chitin binding domain
    • Morimoto K., Karita S., Kimura T., Sakka K., Ohmita K. Cloning, sequencing and expresión of the gene encoding Clostridium paraputrificum chitinase ChiB and análisis of the functions of novel cadherin-like domains and a chitin binding domain. J. Bacteriol. 1997, 179:7306-7314.
    • (1997) J. Bacteriol. , vol.179 , pp. 7306-7314
    • Morimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmita, K.5
  • 19
    • 76049087800 scopus 로고    scopus 로고
    • Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13
    • Neeraja C., Moerschbacher B., Podile A.R. Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13. Bioresour. Technol. 2010, 101:3635-3641.
    • (2010) Bioresour. Technol. , vol.101 , pp. 3635-3641
    • Neeraja, C.1    Moerschbacher, B.2    Podile, A.R.3
  • 21
    • 24044553899 scopus 로고    scopus 로고
    • Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7
    • Orikoshi H., Nakayama S., Hanato C., Miyamoto K., Tsujibo H. Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7. J. Appl. Microbiol. 2005, 99:551-557.
    • (2005) J. Appl. Microbiol. , vol.99 , pp. 551-557
    • Orikoshi, H.1    Nakayama, S.2    Hanato, C.3    Miyamoto, K.4    Tsujibo, H.5
  • 22
    • 0030770243 scopus 로고    scopus 로고
    • Chitinolytic activity of an endophytic strain of Bacillus cereus
    • Pleban S., Chernin L., Chet I. Chitinolytic activity of an endophytic strain of Bacillus cereus. Lett. Appl. Microbiol. 1997, 25:284-288.
    • (1997) Lett. Appl. Microbiol. , vol.25 , pp. 284-288
    • Pleban, S.1    Chernin, L.2    Chet, I.3
  • 23
    • 84866334862 scopus 로고    scopus 로고
    • Synthesis of higher chain chitooligosaccharides by a hyper transglycosylating processive endo-chitinase of Serratia proteamaculans 568
    • Purushotham P., Podile A.R. Synthesis of higher chain chitooligosaccharides by a hyper transglycosylating processive endo-chitinase of Serratia proteamaculans 568. J. Bacteriol. 2012, 194:4260-4271.
    • (2012) J. Bacteriol. , vol.194 , pp. 4260-4271
    • Purushotham, P.1    Podile, A.R.2
  • 24
    • 84859218754 scopus 로고    scopus 로고
    • Multiple chitinases of an endophytic Serratia proteamaculans 568 generate chitin oligomers
    • Purushotham P., Sarma P.V.S.R.N., Podile A.R. Multiple chitinases of an endophytic Serratia proteamaculans 568 generate chitin oligomers. Bioresour. Technol. 2012, 112:261-269.
    • (2012) Bioresour. Technol. , vol.112 , pp. 261-269
    • Purushotham, P.1    Sarma, P.V.S.R.N.2    Podile, A.R.3
  • 25
    • 0031663817 scopus 로고    scopus 로고
    • Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost
    • Sakai K., Yokota A., Kurokawa H., Wakayama M., Moriguchi M. Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost. Appl. Environ. Microbiol. 1998, 64:3397-3402.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3397-3402
    • Sakai, K.1    Yokota, A.2    Kurokawa, H.3    Wakayama, M.4    Moriguchi, M.5
  • 26
    • 0036232796 scopus 로고    scopus 로고
    • Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes
    • Sasaki C., Yokoyama A., Itoh Y., Hashimoto M., Watanabe T., Fukamizo T. Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes. J. Biochem. 2002, 131:557-564.
    • (2002) J. Biochem. , vol.131 , pp. 557-564
    • Sasaki, C.1    Yokoyama, A.2    Itoh, Y.3    Hashimoto, M.4    Watanabe, T.5    Fukamizo, T.6
  • 27
    • 76749113742 scopus 로고    scopus 로고
    • Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste
    • Songsiriritthigul C., Lapboonrueng S., Pechsrichuang P., Pesatcha P., Yamabhai M. Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste. Bioresour. Technol. 2010, 101:4096-4103.
    • (2010) Bioresour. Technol. , vol.101 , pp. 4096-4103
    • Songsiriritthigul, C.1    Lapboonrueng, S.2    Pechsrichuang, P.3    Pesatcha, P.4    Yamabhai, M.5
  • 28
    • 22144480668 scopus 로고    scopus 로고
    • Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS
    • Suginta W., Vongsuwan A., Songsiriritthigul C., Svasti J., Prinz H. Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS. FEBS J. 2005, 272:3376-3386.
    • (2005) FEBS J. , vol.272 , pp. 3376-3386
    • Suginta, W.1    Vongsuwan, A.2    Songsiriritthigul, C.3    Svasti, J.4    Prinz, H.5
  • 29
    • 0031782072 scopus 로고    scopus 로고
    • A chitin-binding domain in a marine bacterial chitinase and other microbial chitinases: implications for the ecology and evolution of 1, 4-β-glycanases
    • Svitel A.L., Kirchman D.L. A chitin-binding domain in a marine bacterial chitinase and other microbial chitinases: implications for the ecology and evolution of 1, 4-β-glycanases. Microbiol. 1998, 144:1299-1308.
    • (1998) Microbiol. , vol.144 , pp. 1299-1308
    • Svitel, A.L.1    Kirchman, D.L.2
  • 30
    • 0345411954 scopus 로고    scopus 로고
    • The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis
    • Wang F.P., Li Q., Zhou Y., Li M.G., Xiao X. The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis. Proteins 2003, 53:908-916.
    • (2003) Proteins , vol.53 , pp. 908-916
    • Wang, F.P.1    Li, Q.2    Zhou, Y.3    Li, M.G.4    Xiao, X.5
  • 31
    • 0028145771 scopus 로고
    • The roles of C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe T., Ito Y., Yamada T., Hashimoto M., Sekine S., Tanaka H. The roles of C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 1994, 176:4465-4472.
    • (1994) J. Bacteriol. , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 32
    • 0034022195 scopus 로고    scopus 로고
    • The role of chitinase production by Stenotrophomonas maltophilia strain C3 in biological control of Bipolaris sorokiniana
    • Zhang Z., Yuen G.Y. The role of chitinase production by Stenotrophomonas maltophilia strain C3 in biological control of Bipolaris sorokiniana. Phytopathology 2000, 90:384-389.
    • (2000) Phytopathology , vol.90 , pp. 384-389
    • Zhang, Z.1    Yuen, G.Y.2


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