메뉴 건너뛰기




Volumn 40, Issue 3, 2009, Pages 623-630

Production, purification and application of extracellular chitinase from Cellulosimicrobium cellulans 191;Produção, purificação e aplicação da quitinase extracelular de cellulosimicrobium cellulans 191

Author keywords

Cellulosimicrobium cellulans; Chitinase; Fungal lysis; Protoplasts

Indexed keywords

CELLULOSIMICROBIUM CELLULANS; FUNGI;

EID: 70349507282     PISSN: 15178382     EISSN: 16784405     Source Type: Journal    
DOI: 10.1590/S1517-83822009000300026     Document Type: Article
Times cited : (31)

References (31)
  • 2
    • 17844381320 scopus 로고    scopus 로고
    • Production and purification of extracellular chitinases from Penicillium aculeatum NRRL 2129 under solid-state fermentation
    • Binod, P.; Pusztahelyi, T.; Nagy, V.; Sandhya, C.; Szakács, G.; Pócsi, I.; Pandey, A. (2005). Production and purification of extracellular chitinases from Penicillium aculeatum NRRL 2129 under solid-state fermentation. Enzyme Microbial Technol. 36, 880-887.
    • (2005) Enzyme Microbial Technol , vol.36 , pp. 880-887
    • Binod, P.1    Pusztahelyi, T.2    Nagy, V.3    Sandhya, C.4    Szakács, G.5    Pócsi, I.6    Pandey, A.7
  • 3
    • 0030917623 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae
    • De Siqueira Pinto, A.; Barreto C.C.; Schrank, A.; Ulhoa, C.J.; Henning Vainstein, M. (1997). Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae. Can. J. Microbiol. 43, 322-327.
    • (1997) Can. J. Microbiol. , vol.43 , pp. 322-327
    • de Siqueira Pinto, A.1    Barreto, C.C.2    Schrank, A.3    Ulhoa, C.J.4    Henning Vainstein, M.5
  • 4
    • 0032478045 scopus 로고    scopus 로고
    • The purification and characterization of Trichoderma harzianum exochitinase
    • Deane, E.E.; Whipps, J.M.; Lynch, J.M.; Peberdy, J.F. (1998). The purification and characterization of Trichoderma harzianum exochitinase. Biochim. Biophys. Acta. 1383, 101-110.
    • (1998) Biochim. Biophys. Acta. , vol.1383 , pp. 101-110
    • Deane, E.E.1    Whipps, J.M.2    Lynch, J.M.3    Peberdy, J.F.4
  • 5
    • 70349545237 scopus 로고    scopus 로고
    • Produção de β-1,3 glucanases, proteases líticas e quitinases por microrganismos e aplicação na lise de leveduras
    • Campinas, (M. Sc. Dissertation. Faculdade de Engenharia de Alimentos. Unicamp)
    • Fleuri, L.F. (2003). Produção de β-1,3 glucanases, proteases líticas e quitinases por microrganismos e aplicação na lise de leveduras. Campinas, 141 p. (M. Sc. Dissertation. Faculdade de Engenharia de Alimentos. Unicamp).
    • (2003) , pp. 141
    • Fleuri, L.F.1
  • 6
    • 30744472614 scopus 로고    scopus 로고
    • Produção, purificação, clonagem e aplicação de enzimas líticas
    • Fleuri, L.F; Sato, H.H. (2005). Produção, purificação, clonagem e aplicação de enzimas líticas. Quim. Nova. 28, 871-879.
    • (2005) Quim. Nova. , vol.28 , pp. 871-879
    • Fleuri, L.F.1    Sato, H.H.2
  • 7
    • 70349529260 scopus 로고    scopus 로고
    • Estudo da influência de diferentes parâmetros na produção de enzimas líticas
    • Fleuri, L.F; Sato, H.H. (2008). Estudo da influência de diferentes parâmetros na produção de enzimas líticas. Ciênc. Tecnol. Aliment. 28, 1-12.
    • (2008) Ciênc. Tecnol. Aliment. , vol.28 , pp. 1-12
    • Fleuri, L.F.1    Sato, H.H.2
  • 8
    • 70349548208 scopus 로고    scopus 로고
    • β-1,3 glucanases e quitinases: Aplicação na lise de leveduras e inibição de fungos
    • Fleuri, L.F; Sato, H.H. (2008). β-1,3 glucanases e quitinases: aplicação na lise de leveduras e inibição de fungos. Ciênc. Agrotec. 32, 1224-1231.
    • (2008) Ciênc. Agrotec , vol.32 , pp. 1224-1231
    • Fleuri, L.F.1    Sato, H.H.2
  • 9
    • 7544224118 scopus 로고    scopus 로고
    • Purification and characterization of extracellular chitinase from Aeromonas schubertii
    • Guo, S.H.; Chen, J.K.; Lee, W.C. (2004). Purification and characterization of extracellular chitinase from Aeromonas schubertii. Enzyme Microbial Technol. 35, 550-556.
    • (2004) Enzyme Microbial Technol , vol.35 , pp. 550-556
    • Guo, S.H.1    Chen, J.K.2    Lee, W.C.3
  • 10
    • 33947388372 scopus 로고    scopus 로고
    • Effects of shear stress and mass transfer on chitinase production by Paenibacillus sp. CHE-N1
    • Kao, P.M.; Chen, C.I.; Huang, S.C.; Chang, Y.C.; Tsai, P.J.; Liu, Y.C. (2007). Effects of shear stress and mass transfer on chitinase production by Paenibacillus sp. CHE-N1. Biochem. Eng. J. 34, 172-178.
    • (2007) Biochem. Eng. J. , vol.34 , pp. 172-178
    • Kao, P.M.1    Chen, C.I.2    Huang, S.C.3    Chang, Y.C.4    Tsai, P.J.5    Liu, Y.C.6
  • 11
    • 33947211770 scopus 로고    scopus 로고
    • Development of continuous chitinase production process in a membrane bioreactor by Paenibacillus sp. CHE-N1
    • Kao, P.M.; Chen, C.I.; Huang, S.C.; Chang, Y.C.; Tsai, P.J.; Liu, Y.C. (2007). Development of continuous chitinase production process in a membrane bioreactor by Paenibacillus sp. CHE-N1. Process Biochem. 42, 606-611.
    • (2007) Process Biochem. , vol.42 , pp. 606-611
    • Kao, P.M.1    Chen, C.I.2    Huang, S.C.3    Chang, Y.C.4    Tsai, P.J.5    Liu, Y.C.6
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0042431707 scopus 로고    scopus 로고
    • Production of chitinase from Verticillium lecanii F091 using submerged fermentation
    • Liu, B.L.; Kao, P.M.; Tzeng, Y.M.; Feng, K.C. (2003). Production of chitinase from Verticillium lecanii F091 using submerged fermentation. Enzyme Microbial Technol., 33, 410-415.
    • (2003) Enzyme Microbial Technol. , vol.33 , pp. 410-415
    • Liu, B.L.1    Kao, P.M.2    Tzeng, Y.M.3    Feng, K.C.4
  • 15
    • 0009365216 scopus 로고    scopus 로고
    • A review of chitin and chitosan applications. Reactive Func
    • Majeti, N.V.; Kumar, R. (2000). A review of chitin and chitosan applications. Reactive Func. Polymers. 46, 1-27.
    • (2000) Polymers. , vol.46 , pp. 1-27
    • Majeti, N.V.1    Kumar, R.2
  • 16
    • 3042808753 scopus 로고    scopus 로고
    • Process optimization for antifungal chitinase production by Trichoderma harzianum
    • Nampoothiri, K.M.; Baiju, T.V.; Sandhya, C.; Sabu, A.; Szakacs, G.; Pandey, A. (2004). Process optimization for antifungal chitinase production by Trichoderma harzianum. Process Biochem. 39, 1583-1590.
    • (2004) Process Biochem , vol.39 , pp. 1583-1590
    • Nampoothiri, K.M.1    Baiju, T.V.2    Sandhya, C.3    Sabu, A.4    Szakacs, G.5    Pandey, A.6
  • 17
    • 4544334839 scopus 로고    scopus 로고
    • Production dynamics and characterization of chitinolytic system of Streptomyces sp NK1057, a well equipped chitin degrader. World J
    • Nawani, N.N.; Kapadnis, B.P. (2004). Production dynamics and characterization of chitinolytic system of Streptomyces sp NK1057, a well equipped chitin degrader. World J. Microbiol. Biotech. 20, 487-494.
    • (2004) Microbiol. Biotech. , vol.20 , pp. 487-494
    • Nawani, N.N.1    Kapadnis, B.P.2
  • 19
    • 0025216038 scopus 로고
    • Trichoderma protoplast fusion; a tool for improving biocontrol agents
    • Pe'er, S.; Chet, I. (1990). Trichoderma protoplast fusion; a tool for improving biocontrol agents. Can. J. Microbiol. 36, 6-9.
    • (1990) Can. J. Microbiol. , vol.36 , pp. 6-9
    • Pe'er, S.1    Chet, I.2
  • 20
    • 33746227334 scopus 로고    scopus 로고
    • Self-fusion of protoplasts enhances chitinase production and biocontrol activity in Trichoderma harzianum
    • Prabavathy, V.R.; Mathivanan, N.; Sagadevan, E.; Murugesan, K.; Lalithakumari, D. (2006). Self-fusion of protoplasts enhances chitinase production and biocontrol activity in Trichoderma harzianum. Bioresource Technol. 97, 2330-2334.
    • (2006) Bioresource Technol , vol.97 , pp. 2330-2334
    • Prabavathy, V.R.1    Mathivanan, N.2    Sagadevan, E.3    Murugesan, K.4    Lalithakumari, D.5
  • 21
    • 33645224774 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of chitin in the production of oligosaccharides using Lecanicillium fungicola chitinases
    • Ramírez-Coutiño, L.; Marín-Cervantes, M.C.; Huerta, S.; Revah, S.; Shirai, K. (2006). Enzymatic hydrolysis of chitin in the production of oligosaccharides using Lecanicillium fungicola chitinases. Process Biochem. 41, 1106-1110.
    • (2006) Process Biochem , vol.41 , pp. 1106-1110
    • Ramírez-Coutiño, L.1    Marín-Cervantes, M.C.2    Huerta, S.3    Revah, S.4    Shirai, K.5
  • 22
    • 34447251503 scopus 로고    scopus 로고
    • Purification of Aspergillus sp. S1-13 chitinases and their role in saccharification of chitin in mash of solid-state culture with shellfish waste
    • Rattanakit, N.; Yano, S.; Plikomol, A.; Wakayama, M.; Tachiki, T. (2007). Purification of Aspergillus sp. S1-13 chitinases and their role in saccharification of chitin in mash of solid-state culture with shellfish waste. J. Biosc. Bioeng. 103, 535-541.
    • (2007) J. Biosc. Bioeng. , vol.103 , pp. 535-541
    • Rattanakit, N.1    Yano, S.2    Plikomol, A.3    Wakayama, M.4    Tachiki, T.5
  • 23
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugar
    • Réissig, J.L.; Strominger, J.L.; Leloir, L.F. (1955). A modified colorimetric method for the estimation of N-acetylamino sugar. J. Biol. Chem. 217, 959-699.
    • (1955) J. Biol. Chem. , vol.217 , pp. 959-699
    • Réissig, J.L.1    Strominger, J.L.2    Leloir, L.F.3
  • 24
    • 0004169627 scopus 로고
    • Macmillan Press, London
    • Roberts, G.A.F. (1992). Chitin chemistry. Macmillan Press, London, pp. 55-58.
    • (1992) Chitin chemistry , pp. 55-58
    • Roberts, G.A.F.1
  • 25
    • 0027297246 scopus 로고
    • Chitinase of fungi and plants: Their involvement in morphogenesis and host-parasite interactions
    • Sahai, A.S.; Manocha, M.S. (1993). Chitinase of fungi and plants: their involvement in morphogenesis and host-parasite interactions. Microbiol. Rev., 11:317-338.
    • (1993) Microbiol. Rev. , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 26
    • 0031663817 scopus 로고    scopus 로고
    • Purification and characterization of three thermostable endochitinases of a novel Bacillus strain, MH-1, isolated from chitin-containing compost
    • Sakai, K.; Yokota, A.; Kurokawa, H.; Wakayama, M.; Moriguchi, M. (1998). Purification and characterization of three thermostable endochitinases of a novel Bacillus strain, MH-1, isolated from chitin-containing compost. Appl. Environ. Microbiol. 64, 3397.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3397
    • Sakai, K.1    Yokota, A.2    Kurokawa, H.3    Wakayama, M.4    Moriguchi, M.5
  • 27
    • 0024597212 scopus 로고
    • Use of lytic enzymes for protoplast production in Trichoderma reesei QM9414
    • Sandhu, D.K.; Wadhwa, V.; Bagga, P.S. (1989). Use of lytic enzymes for protoplast production in Trichoderma reesei QM9414. Enzyme Microbial Technol. 11, 21-25.
    • (1989) Enzyme Microbial Technol , vol.11 , pp. 21-25
    • Sandhu, D.K.1    Wadhwa, V.2    Bagga, P.S.3
  • 28
    • 0028186313 scopus 로고
    • Optimization of formation and regeneration of protoplasts from biocontrol agents of Trichoderma sp
    • Tschen, J.S.M.; Li, I.F. (1994). Optimization of formation and regeneration of protoplasts from biocontrol agents of Trichoderma sp. Mycoscience. 35, 257-263.
    • (1994) Mycoscience , vol.35 , pp. 257-263
    • Tschen, J.S.M.1    Li, I.F.2
  • 29
    • 33748885083 scopus 로고    scopus 로고
    • Bioconversion of shellfish chitin wastes for the production of Bacillus subtilis W-118 chitinase
    • Wang, S.L.; Lin, T.Y.; Yen, Y.H.; Liao, H.F.; Chen, Y.J. (2006). Bioconversion of shellfish chitin wastes for the production of Bacillus subtilis W-118 chitinase. Carboh. Res. 341, 2507-2515.
    • (2006) Carboh. Res. , vol.341 , pp. 2507-2515
    • Wang, S.L.1    Lin, T.Y.2    Yen, Y.H.3    Liao, H.F.4    Chen, Y.J.5
  • 30
    • 47649115843 scopus 로고    scopus 로고
    • Seleção, produção e caracterização da enzima quitinase. Campinas
    • (PhD. Thesis. Faculdade de Engenharia de Alimentos. Unicamp)
    • Yamaguchi, M.M. (2003). Seleção, produção e caracterização da enzima quitinase. Campinas, 83 p. (PhD. Thesis. Faculdade de Engenharia de Alimentos. Unicamp).
    • (2003) , pp. 83
    • Yamaguchi, M.M.1
  • 31
    • 3142634524 scopus 로고    scopus 로고
    • Characteristics of thermostable chitinase enzymes from the Indonesian Bacillus sp 13.26
    • Yuli, P.E.; Suhartono, M.T.; Rukayadi, Y.; Hwang, J.K.; Pyun, Y.R. (2004). Characteristics of thermostable chitinase enzymes from the Indonesian Bacillus sp 13.26. Enzyme Microbial Technol. 35, 147-153.
    • (2004) Enzyme Microbial Technol , vol.35 , pp. 147-153
    • Yuli, P.E.1    Suhartono, M.T.2    Rukayadi, Y.3    Hwang, J.K.4    Pyun, Y.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.