메뉴 건너뛰기




Volumn 73, Issue 6, 2008, Pages

A thermostable chitinase with chitin-binding activity from Phaseolus limensis

Author keywords

Antifungal; Chitin binding; Chitinase; Large lima bean; Thermostable

Indexed keywords

ATHELIA ROLFSII; FUSARIUM SOLANI; PHASEOLUS LUNATUS; PYTHIUM; PYTHIUM APHANIDERMATUM;

EID: 48749090476     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2008.00800.x     Document Type: Article
Times cited : (19)

References (32)
  • 2
    • 0027215763 scopus 로고
    • Antifungal effect of bean endochitinase on Rhizoctonia solani: Ultrastructural changes and cytochemical aspect of chitin breakdown
    • Benhamou N, Broglie K, Broglie R, Chet I. 1993. Antifungal effect of bean endochitinase on Rhizoctonia solani: ultrastructural changes and cytochemical aspect of chitin breakdown. Can J Microbiol 39 : 318 28.
    • (1993) Can J Microbiol , vol.39 , pp. 318-328
    • Benhamou, N.1    Broglie, K.2    Broglie, R.3    Chet, I.4
  • 3
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene, purification, properties, and possible function
    • Boller T, Gehri A, Mauch F, Vogeli U. 1983. Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta 157 : 22 31.
    • (1983) Planta , vol.157 , pp. 22-31
    • Boller, T.1    Gehri, A.2    Mauch, F.3    Vogeli, U.4
  • 5
    • 0034893473 scopus 로고    scopus 로고
    • Induced expression of the class II chitinase gene during cold acclimation and dehydration of bermudagrass (Cynodon sp.)
    • De Los Reyes BG, Taliaferro CM, Anderson MP, Melcher U, McMaugh S. 2001. Induced expression of the class II chitinase gene during cold acclimation and dehydration of bermudagrass (Cynodon sp.). Theor Appl Genet 103 : 297 306.
    • (2001) Theor Appl Genet , vol.103 , pp. 297-306
    • De Los Reyes, B.G.1    Taliaferro, C.M.2    Anderson, M.P.3    Melcher, U.4    McMaugh, S.5
  • 7
    • 0032100935 scopus 로고    scopus 로고
    • Srchi13, a novel early nodulin from Sesbania rostrata, is related to acidic class III chitinases
    • Goormachtig S, Lievens S, van de Velde W, van Montagu M, Holsters M. 1998. Srchi13, a novel early nodulin from Sesbania rostrata, is related to acidic class III chitinases. Plant Cell 10 : 905 15.
    • (1998) Plant Cell , vol.10 , pp. 905-915
    • Goormachtig, S.1    Lievens, S.2    Van De Velde, W.3    Van Montagu, M.4    Holsters, M.5
  • 8
    • 0034127684 scopus 로고    scopus 로고
    • Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12
    • Hashimoto M, Ikegami T, Seino S, Ohuchi N, Fukada H, Sugiyama J, Shirakawa M, Watanabe T. 2000. Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J Bacteriol 182 (11 3045 54.
    • (2000) J Bacteriol , vol.182 , Issue.11 , pp. 3045-3054
    • Hashimoto, M.1    Ikegami, T.2    Seino, S.3    Ohuchi, N.4    Fukada, H.5    Sugiyama, J.6    Shirakawa, M.7    Watanabe, T.8
  • 9
    • 31444440508 scopus 로고    scopus 로고
    • Purification and characterization of a novel isozyme of chitinase from Bombyx mori
    • Kabir KE, Hirowatari D, Watanabe K, Koga D. 2006. Purification and characterization of a novel isozyme of chitinase from Bombyx mori. Biosci Biotechnol Biochem 70 (1 252 62.
    • (2006) Biosci Biotechnol Biochem , vol.70 , Issue.1 , pp. 252-262
    • Kabir, K.E.1    Hirowatari, D.2    Watanabe, K.3    Koga, D.4
  • 10
    • 33745886849 scopus 로고    scopus 로고
    • Purification and characterization of chitinases from Clostridium sp. E-16 isolated from the intestinal tract of the South American sea lion (Otaria flavescens)
    • Konagaya Y, Tsuchiya C, Sugita H. 2006. Purification and characterization of chitinases from Clostridium sp. E-16 isolated from the intestinal tract of the South American sea lion (Otaria flavescens). Lett Appl Microbiol 43 : 187 93.
    • (2006) Lett Appl Microbiol , vol.43 , pp. 187-193
    • Konagaya, Y.1    Tsuchiya, C.2    Sugita, H.3
  • 11
    • 0015853344 scopus 로고
    • Gel electrophoresis of proteins
    • Laemmli UK, Favre M. 1973. Gel electrophoresis of proteins. J Mol Biol 80 : 575 99.
    • (1973) J Mol Biol , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 13
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano J, Duran A, Cabib E. 1977. A rapid and sensitive assay for chitinase using tritiated chitin. Anal Biochem 83 (2 648 56.
    • (1977) Anal Biochem , vol.83 , Issue.2 , pp. 648-656
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 14
    • 0036444826 scopus 로고    scopus 로고
    • Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2
    • Nawani NN, Kapadnis BP, Das AD, Rao AS, Mahajan SK. 2002. Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2. J Appl Microbiol 93 : 965 75.
    • (2002) J Appl Microbiol , vol.93 , pp. 965-975
    • Nawani, N.N.1    Kapadnis, B.P.2    Das, A.D.3    Rao, A.S.4    Mahajan, S.K.5
  • 15
    • 0344994629 scopus 로고    scopus 로고
    • Chitinolytic activity of Pseudomonas fluorescens isolates from barley and sugar beet rhizosphere
    • Nielsen MN, Sdpresen J. 1999. Chitinolytic activity of Pseudomonas fluorescens isolates from barley and sugar beet rhizosphere. FEMS Microbiol Ecol 30 : 217 27.
    • (1999) FEMS Microbiol Ecol , vol.30 , pp. 217-227
    • Nielsen, M.N.1    Sdpresen, J.2
  • 16
    • 0036802220 scopus 로고    scopus 로고
    • The abundant class III chitinase homolog in young developing banana fruits behaves as a transient vegetative storage protein and most probably serves as an important supply of amino acids for the synthesis of ripening-associated proteins
    • Peumans WJ, Proost P, Swennen RL, van Damme EJ. 2002. The abundant class III chitinase homolog in young developing banana fruits behaves as a transient vegetative storage protein and most probably serves as an important supply of amino acids for the synthesis of ripening-associated proteins. Plant Physiol 130 : 1063 72.
    • (2002) Plant Physiol , vol.130 , pp. 1063-1072
    • Peumans, W.J.1    Proost, P.2    Swennen, R.L.3    Van Damme, E.J.4
  • 17
    • 0034502946 scopus 로고    scopus 로고
    • R. Velazhahan, 45-kDa chitinase purified from pearl millet (Pennisetum glaucum [l.] R. Br.) shows antifungal activity
    • Radhajeyalakshmi R, Meena B, Thangavelu R, Deborah SD, Vidhyasekaran P. 2000. R. Velazhahan, 45-kDa chitinase purified from pearl millet (Pennisetum glaucum [L.] R. Br.) shows antifungal activity. J Plant Dis Prot 107 : 605 16.
    • (2000) J Plant Dis Prot , vol.107 , pp. 605-616
    • Radhajeyalakshmi, R.1    Meena, B.2    Thangavelu, R.3    Deborah, S.D.4    Vidhyasekaran, P.5
  • 18
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: Their involvement in morphogenesis and host-parasite interaction
    • Sahai AS, Manocha MS. 1993. Chitinases of fungi and plants: their involvement in morphogenesis and host-parasite interaction. FEMS Microbiol 11 : 317 38.
    • (1993) FEMS Microbiol , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 19
    • 0001519173 scopus 로고
    • Plant chitinase are potent inhibitors of fungal growth
    • Schlumbaum A, Mauch F, Vogeli U. 1986. Plant chitinase are potent inhibitors of fungal growth. Nature 324 : 355 6.
    • (1986) Nature , vol.324 , pp. 355-356
    • Schlumbaum, A.1    Mauch, F.2    Vogeli, U.3
  • 20
    • 0035286420 scopus 로고    scopus 로고
    • Purification, characterization and molecular cloning of a chitinase from the seeds of Benincasa hispida
    • Shih CYT, Khan AA, Jia SF, Wu JL, Shih DS. 2001. Purification, characterization and molecular cloning of a chitinase from the seeds of Benincasa hispida. Biosci Biotechnol Biochem 65 (3 501 9.
    • (2001) Biosci Biotechnol Biochem , vol.65 , Issue.3 , pp. 501-509
    • Shih, C.Y.T.1    Khan, A.A.2    Jia, S.F.3    Wu, J.L.4    Shih, D.S.5
  • 21
    • 15244357854 scopus 로고    scopus 로고
    • Purification, characterization and antifungal activity of chitinases from pineapple (Ananas comosus) leaf
    • Taira T, Toma N, Ishihara M. 2005. Purification, characterization and antifungal activity of chitinases from pineapple (Ananas comosus) leaf. Biosci Biotechnol Biochem 69 (1 189 96.
    • (2005) Biosci Biotechnol Biochem , vol.69 , Issue.1 , pp. 189-196
    • Taira, T.1    Toma, N.2    Ishihara, M.3
  • 22
    • 0035028330 scopus 로고    scopus 로고
    • N-acetylglucosamine and glucosamine-containing arabinogalactan proteins control somatic embryogenesis
    • Van Hengel AJ, Tadesse Z, Immerzeel P, Schols H, Van Kammen A, De Vries SC. 2001. N-acetylglucosamine and glucosamine-containing arabinogalactan proteins control somatic embryogenesis. Plant Physiol 125 : 1880 90.
    • (2001) Plant Physiol , vol.125 , pp. 1880-1890
    • Van Hengel, A.J.1    Tadesse, Z.2    Immerzeel, P.3    Schols, H.4    Van Kammen, A.5    De Vries, S.C.6
  • 23
    • 0027350252 scopus 로고
    • Purification, characterization and differential hormonal regulation of a β-1, 3-glucanase and two chitinases from chickpea (Cicer arietinum L.)
    • Vogelsang R, Barz W. 1993. Purification, characterization and differential hormonal regulation of a β-1, 3-glucanase and two chitinases from chickpea (Cicer arietinum L.). Planta 189 : 60 9.
    • (1993) Planta , vol.189 , pp. 60-69
    • Vogelsang, R.1    Barz, W.2
  • 24
    • 37349123486 scopus 로고    scopus 로고
    • Hypotin, a novel antipathogenic and antiproliferative protein from peanuts with sequence similarity to those of chitinase precursors
    • Wang SY, Shao B, Rao PF, Lee YY, Ye XY. 2007. Hypotin, a novel antipathogenic and antiproliferative protein from peanuts with sequence similarity to those of chitinase precursors. J Agri Food Chem 55 : 9792 9.
    • (2007) J Agri Food Chem , vol.55 , pp. 9792-9799
    • Wang, S.Y.1    Shao, B.2    Rao, P.F.3    Lee, Y.Y.4    Ye, X.Y.5
  • 25
    • 38949200203 scopus 로고    scopus 로고
    • Purification and characterization of a chitinase from peanut (Arachis hypogaea L.)
    • Wang SY, Shao B, Ye XY, Rao PF. 2008. Purification and characterization of a chitinase from peanut (Arachis hypogaea L.). J Food Biochem 32 : 32 45.
    • (2008) J Food Biochem , vol.32 , pp. 32-45
    • Wang, S.Y.1    Shao, B.2    Ye, X.Y.3    Rao, P.F.4
  • 27
    • 14844327503 scopus 로고    scopus 로고
    • A study of the purification and properties of chitinase from bean seeds (Phaseolus vulgaris)
    • Yang HQ, Luo ZM. 1998. A study of the purification and properties of chitinase from bean seeds (Phaseolus vulgaris). J Human Agric Univ (China) 24 (3 194 8.
    • (1998) J Human Agric Univ (China) , vol.24 , Issue.3 , pp. 194-198
    • Yang, H.Q.1    Luo, Z.M.2
  • 28
    • 0036452040 scopus 로고    scopus 로고
    • Delandin, a chitinase-like protein with antifungal, HIV-1 reverse transcriptase inhibitory and mitogenic activities from the ricebean (Delandia umbellata
    • Ye XY, Ng TB. 2002. Delandin, a chitinase-like protein with antifungal, HIV-1 reverse transcriptase inhibitory and mitogenic activities from the ricebean (Delandia umbellata). Protein Expr Purif 24 : 524 9.
    • (2002) Protein Expr Purif , vol.24 , pp. 524-529
    • Ye, X.Y.1    Ng, T.B.2
  • 29
    • 0037328739 scopus 로고    scopus 로고
    • Isolation of vulgin, a new antifungal polypeptide with mitogenic activity from the pinto bean
    • Ye XY, Ng TB. 2003. Isolation of vulgin, a new antifungal polypeptide with mitogenic activity from the pinto bean. J Peptide Sci 9 : 114 9.
    • (2003) J Peptide Sci , vol.9 , pp. 114-119
    • Ye, X.Y.1    Ng, T.B.2
  • 30
    • 0034607116 scopus 로고    scopus 로고
    • Dolichin, a new chitinase-like antifungal protein isolated from field beans (Dolichos lablab)
    • Ye XY, Wang HX, Ng TB. 2000. Dolichin, a new chitinase-like antifungal protein isolated from field beans (Dolichos lablab). Biochem Biophys Res Commun 269 : 155 9.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 155-159
    • Ye, X.Y.1    Wang, H.X.2    Ng, T.B.3
  • 32
    • 0036007921 scopus 로고    scopus 로고
    • Mutation of a chitinase-like gene causes ectopic deposition of lignin, aberrant cell shapes, and overproduction of ethylene
    • Zhong R, Kays SJ, Schroeder BP, Ye ZH. 2002. Mutation of a chitinase-like gene causes ectopic deposition of lignin, aberrant cell shapes, and overproduction of ethylene. Plant Cell 14 : 165 79.
    • (2002) Plant Cell , vol.14 , pp. 165-179
    • Zhong, R.1    Kays, S.J.2    Schroeder, B.P.3    Ye, Z.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.