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Volumn 61, Issue 3, 2011, Pages 453-461

Chitinolytic enzyme production and genetic improvement of a new isolate belonging to Streptomyces anulatus

Author keywords

16S rDNA; Chitin; Chitinase; Molecular weight; Protoplast fusion; Streptomyces

Indexed keywords

BACTERIA (MICROORGANISMS); DECAPODA (CRUSTACEA); STREPTOMYCES; STREPTOMYCES ANULATUS; STREPTOMYCES COELICOLOR;

EID: 80755172264     PISSN: 15904261     EISSN: 18692044     Source Type: Journal    
DOI: 10.1007/s13213-010-0158-5     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 76049088124 scopus 로고    scopus 로고
    • Isolation and characterization of two Streptomyces species produced non polyenic antifungal agents
    • Agwa A, Aly MM, Bonaly R (2000) Isolation and characterization of two Streptomyces species produced non polyenic antifungal agents. J Union Arab Biol 7 B: 62-84
    • (2000) J Union Arab Biol , vol.7 B , pp. 62-84
    • Agwa, A.1    Aly, M.M.2    Bonaly, R.3
  • 2
    • 0025238624 scopus 로고
    • Optimum conditions for efficient transformation of Streptomyces venezuelae protoplasts
    • Anné J, Van Melleart L, Eyssen H (1990) Optimal conditions for efficient transformation of Streptomyces venezuelae protoplasts. Appl Microbiol Biotechnol 32:431-435 (Pubitemid 20095296)
    • (1990) Applied Microbiology and Biotechnology , vol.32 , Issue.4 , pp. 431-435
    • Anne, J.1    Van Mellaert, L.2    Eyssen, H.3
  • 3
    • 23844494456 scopus 로고    scopus 로고
    • Isolation and identification of Streptomyces fradiae SU-1 from Thailand and protoplast transformation with the chitinase B gene from Nocardiopsis prasina OPC-131
    • DOI 10.1007/s00284-005-4402-3
    • Apichaisataienchote B, Altenbuchner J, Buchenauer H (2005) Isolation and identification of Streptomyces fradiae SU-1 from Thailand and protoplast transformation with the chitinase B gene from OPC-131. Curr Microbiol 51:116-121 (Pubitemid 41160026)
    • (2005) Current Microbiology , vol.51 , Issue.2 , pp. 116-121
    • Apichaisataienchote, B.1    Altenbuchner, J.2    Buchenauer, H.3
  • 4
    • 0019832103 scopus 로고
    • Protoplast fusion in Streptomyces: Conditions for efficient genetic recombination and cell regeneration
    • Baltz RH, Matsushima P (1981) Protoplast fusion in Streptomyces: conditions for efficient genetic recombination and cell regeneration. J Gen Microbiol 127:137-146 (Pubitemid 12169881)
    • (1981) Journal of General Microbiology , vol.127 , Issue.1 , pp. 137-146
    • Baltz, R.H.1    Matsushima, P.2
  • 5
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding
    • Bradford MM (1976) A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0020584674 scopus 로고
    • Rapid method for the determination of fatty acid profiles from fats and oils using trimethylsulphonium hydroxide for transesterification
    • Butte W (1983) Rapid method for the determination of fatty acid profiles from fats and oils using trimethylsulphonium hydroxide for transesterification. J Chromatogr 261:142-145 (Pubitemid 13071468)
    • (1983) Journal of Chromatography , vol.261 , Issue.1 , pp. 142-145
    • Butte, W.1
  • 8
    • 33746671918 scopus 로고    scopus 로고
    • Biotechnological aspects of chitinolytic enzymes: A review
    • DOI 10.1007/s00253-005-0183-7
    • Dahiya N, Tewari R, Hoondal GH (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71:773-782 (Pubitemid 44162510)
    • (2006) Applied Microbiology and Biotechnology , vol.71 , Issue.6 , pp. 773-782
    • Dahiya, N.1    Tewari, R.2    Hoondal, G.S.3
  • 11
    • 0032444536 scopus 로고    scopus 로고
    • Chitinolytic enzyme activity of Penicillium janthinellum P9 in bench- top bioreactor
    • DOI 10.1016/S0922-338X(99)80020-8
    • Fenice M, Leuba JL, Federici F (1998) Chitinolytic enzymes activity of Penicillium janthinellum P9 in bench top bioreactor. J Ferment Bioeng 86:620-623 (Pubitemid 29048964)
    • (1998) Journal of Fermentation and Bioengineering , vol.86 , Issue.6 , pp. 620-623
    • Fenice, M.1    Leuba, J.-L.2    Federici, F.3
  • 12
    • 0000759564 scopus 로고
    • Physiology of microbial degradation of chitin and chitosan
    • Gooday GW (1990) Physiology of microbial degradation of chitin and chitosan. Biodegradation 1:177-190
    • (1990) Biodegradation , vol.1 , pp. 177-190
    • Gooday, G.W.1
  • 14
    • 0030974363 scopus 로고    scopus 로고
    • Lipid and fatty acid composition of cytoplasmic membranes from Streptomyces hygroscopicus and its stable protoplast-type L form
    • Hoischen C, Gura K, Luge C, Gumpert J (1997) Lipid and fatty acid composition of cytoplasmic membranes from Streptomyces hygroscopicus and Its stable protoplast-type L form. J Bacteriol 179(11):3430-3436 (Pubitemid 27232977)
    • (1997) Journal of Bacteriology , vol.179 , Issue.11 , pp. 3430-3436
    • Hoischen, C.1    Gura, K.2    Luge, C.3    Gumpert, J.4
  • 15
    • 0029903641 scopus 로고    scopus 로고
    • Production of chitinolytic enzymes from a novel species of Aeromonas
    • Huang JH, Chen CJ, Su YC (1996) Production of chitinolytic enzymes from a novel species of Aeromonas. J Ind Microbiol Biotechnol 17:89-95
    • (1996) J Ind Microbiol Biotechnol , vol.17 , pp. 89-95
    • Huang, J.H.1    Chen, C.J.2    Su, Y.C.3
  • 16
    • 0034693322 scopus 로고    scopus 로고
    • Chitin catabolism in the marine bacterium Vibrio furnissii. Identification and molecular cloning of a chitoporin
    • Keyhani NO, Li XB, Roseman S (2000) Chitin catabolism in the marine bacterium Vibrio furnissii. Identification and molecular cloning of a chitoporin. J Biol Chem 275:33068-33088
    • (2000) J Biol Chem , vol.275 , pp. 33068-33088
    • Keyhani, N.O.1    Li, X.B.2    Roseman, S.3
  • 17
    • 80755127684 scopus 로고    scopus 로고
    • Indole-3-acetic acid production by Streptomyces sp. isolated from some Thai medicinal plant rhizosphere
    • Khamna S, Yokota A, Peberdy JF, Lumyong S (2010) Indole-3-acetic acid production by Streptomyces sp. isolated from some Thai medicinal plant rhizosphere. Green Chem 12:35-38
    • (2010) Green Chem , vol.12 , pp. 35-38
    • Khamna, S.1    Yokota, A.2    Peberdy, J.F.3    Lumyong, S.4
  • 18
    • 12144267986 scopus 로고    scopus 로고
    • Purification and characterization of chitinase from Streptomyces sp. M-20
    • Kim KJ, Yang YJ, Kim JG (2003) Purification and characterization of chitinase from Streptomyces sp. M-20. J Biochem Mol Biol 36(2):185-189
    • (2003) J Biochem Mol Biol , vol.36 , Issue.2 , pp. 185-189
    • Kim, K.J.1    Yang, Y.J.2    Kim, J.G.3
  • 19
    • 26244468501 scopus 로고    scopus 로고
    • Biological control of late leaf spot of peanut (Arachis hypogaea) with chitinolytic bacteria
    • DOI 10.1094/PHYTO-95-1157
    • Kishore GK, Pande S, Podile AR (2005) Biological control of late leaf spot of peanut (Arachis hypogaea) with chinitolytic bacteria. Phytopathology 95:1157-1165 (Pubitemid 41417114)
    • (2005) Phytopathology , vol.95 , Issue.10 , pp. 1157-1165
    • Kishore, G.K.1    Pande, S.2    Podile, A.R.3
  • 20
    • 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)
    • DOI 10.1111/j.1472-765X.2006.01926.x
    • Konagaya Y, Tsuchiya C, Sugita H (2006) Purification and characterization of chitinases from Clostridium sp. E16 isolated from the intestinal tract of the South American sea lion (Otraia flavescens). Lett Appl Microbiol 43(2):187-193 (Pubitemid 44050634)
    • (2006) Letters in Applied Microbiology , vol.43 , Issue.2 , pp. 187-193
    • Konagaya, Y.1    Tsuchiya, C.2    Sugita, H.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 80755127686 scopus 로고    scopus 로고
    • Industrial microbiology
    • Madigan MT, Martinko JM eds, 11th edn. Pearson Prentice Hall, Upper Saddle River, NJ
    • Madigan MT, Martinko JM (2006) Industrial microbiology. In: Madigan MT, Martinko JM (eds) Biology of microorganisms, 11th edn. Pearson Prentice Hall, Upper Saddle River, NJ
    • (2006) Biology of Microorganisms
    • Madigan, M.T.1    Martinko, J.M.2
  • 23
    • 0031148966 scopus 로고    scopus 로고
    • Properties of the chitinase of the antifungal biocontrol agent Streptomyces lydicus WYEC108
    • DOI 10.1016/S0141-0229(96)00175-5, PII S0141022996001755
    • Mahadevan B, Crawford DL (1997) Properties of the chitinase of the antifungal biocontrol agent Streptomyces lydicus WYEC 108. Enzyme Microb Technol 20:489-493 (Pubitemid 27207878)
    • (1997) Enzyme and Microbial Technology , vol.20 , Issue.7 , pp. 489-493
    • Mahadevan, B.1    Crawford, D.L.2
  • 24
    • 0006507671 scopus 로고
    • Protoplast fusion
    • Demain AL, Solomon NA eds, American Society of Microbiology, Washington DC
    • Matsushima P, Baltz RH (1986) Protoplast fusion. In: Demain AL, Solomon NA (eds) Manual of industrial microbiology and biotechnology. American Society of Microbiology, Washington DC, pp 170-183
    • (1986) Manual of Industrial Microbiology and Biotechnology , pp. 170-183
    • Matsushima, P.1    Baltz, R.H.2
  • 25
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-429
    • (1959) Anal Chem , vol.31 , pp. 426-429
    • Miller, G.L.1
  • 26
    • 70350144778 scopus 로고    scopus 로고
    • Chitinase production by Streptomyces sp. ANU 6277
    • Narayana K J P, Vijayalakshmi M (2009) Chitinase production by Streptomyces sp. ANU 6277. Braz J Microbiol 40(10):725-733
    • (2009) Braz J Microbiol , vol.40 , Issue.10 , pp. 725-733
    • Narayana, K.J.P.1    Vijayalakshmi, M.2
  • 27
    • 4544334839 scopus 로고    scopus 로고
    • Production dynamics and characterization of chitinolytic system of Streptomyces sp. NK1057, a well equipped chitin degrader
    • DOI 10.1023/B:WIBI.0000040400.68310.7c
    • Nawani NN, Kapadnis BP (2004) Production dynamics and characterization of chitinolytic system of Streptomyces sp. NK 1057, a well equipped chitin degrader. World J Microbiol Biotechnol 20:487-494 (Pubitemid 39211251)
    • (2004) World Journal of Microbiology and Biotechnology , vol.20 , Issue.5 , pp. 487-494
    • Nawani, N.N.1    Kapadnis, B.P.2
  • 28
    • 0036444826 scopus 로고    scopus 로고
    • Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2
    • DOI 10.1046/j.1365-2672.2002.01766.x
    • Nawani NN, Kapadinis BP, Das AD, Rao AS, Mahajan SK (2002) Purification and characterization of a thermophilic and acidophilic chitinase from Micromonospora sp. V2. J Appl Microbiol 93(6):965-975 (Pubitemid 35408571)
    • (2002) Journal of Applied Microbiology , vol.93 , Issue.6 , pp. 965-975
    • Nawani, N.N.1    Kapadnis, B.P.2    Das, A.D.3    Rao, A.S.4    Mahajan, S.K.5
  • 30
    • 0019911619 scopus 로고
    • Protoplast fusion permits high-frequency transfer of a Streptomyces determinant which mediates actinomycin synthesis
    • Ochi K (1982) Protoplast fusion permits high-frequency transfer of a Streptomyces determinant which mediates actinomycin synthesis. J Bacteriol 150(2):592-597 (Pubitemid 12011232)
    • (1982) Journal of Bacteriology , vol.150 , Issue.2 , pp. 592-597
    • Ochi, K.1
  • 31
    • 0030917623 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae
    • Pinto A D S, Barreto CC, Schrank A, Ulho A C J, Vainstein MH (1997) Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae. Can J Microbiol 43:322-327 (Pubitemid 27252435)
    • (1997) Canadian Journal of Microbiology , vol.43 , Issue.4 , pp. 322-327
    • De Pinto, A.S.1    Barreto, C.C.2    Schrank, A.3    Marilene, H.V.4
  • 32
    • 0001023407 scopus 로고
    • Methods for characterization of Streptomyces species
    • Shirling EB, Gottlieb D (1966) Methods for characterization of Streptomyces species. Int J Syst Bacteriol 16:313-340
    • (1966) Int J Syst Bacteriol , vol.16 , pp. 313-340
    • Shirling, E.B.1    Gottlieb, D.2
  • 34
    • 80052563968 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a new local keratinase producing Pseudomomanas sp., MS21
    • Tork S, Aly MM, Nawar L (2010) Biochemical and molecular characterization of a new local keratinase producing Pseudomomanas sp., MS21. Asian J Biotechnol 2(1):1-13
    • (2010) Asian J Biotechnol , vol.2 , Issue.1 , pp. 1-13
    • Tork, S.1    Aly, M.M.2    Nawar, L.3
  • 36
    • 0025880428 scopus 로고
    • Regulation of chitinase synthesis in Trichoderma harzianum
    • Ulhoa CJ, Peberdy JF (1991) Regulation of chitinase synthesis in Trichoderma harzianum. J Gen Microbiol 14:2163-2169
    • (1991) J Gen Microbiol , vol.14 , pp. 2163-2169
    • Ulhoa, C.J.1    Peberdy, J.F.2
  • 37
    • 0033769336 scopus 로고    scopus 로고
    • Isolation of a chitinase overproducing mutant of Streptomyces peucetius defective in daunorubicin biosynthesis
    • Vetrivel KS, Dharmalingam K (2000) Isolation of a chitinase overproducing mutant of Streptomyces peucetius defective in daunorubicin biosynthesis. Can J Microbiol 46(10):956-960
    • (2000) Can J Microbiol , vol.46 , Issue.10 , pp. 956-960
    • Vetrivel, K.S.1    Dharmalingam, K.2
  • 38


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.