메뉴 건너뛰기




Volumn 28, Issue 2, 2011, Pages 118-124

Penicillium oxalicum SAEM-51: A mutagenised strain for enhanced production of chitin deacetylase for bioconversion to chitosan

Author keywords

[No Author keywords available]

Indexed keywords

CHITIN DEACETYLASE; COLLOIDAL CHITIN; ENZYME PRODUCTION; ETHIDIUM BROMIDE; FOOD PROCESSING INDUSTRY; MORPHOLOGICAL FEATURES; MUTANT STRAIN; OPTIMUM TEMPERATURE; PH OPTIMA; RESIDUAL MATERIALS; SCANNING ELECTRON MICROGRAPHS; SUBMERGED FERMENTATION; WILD-TYPE STRAIN;

EID: 79551470817     PISSN: 18716784     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbt.2010.09.009     Document Type: Article
Times cited : (29)

References (32)
  • 1
    • 0001491030 scopus 로고
    • La chitine dans le regne animal
    • Jeuniaux C. La chitine dans le regne animal. Bull. Soc. Zool. Fr. 1982, 107:363-386.
    • (1982) Bull. Soc. Zool. Fr. , vol.107 , pp. 363-386
    • Jeuniaux, C.1
  • 2
    • 0001881554 scopus 로고
    • The distribution and quantitative importance of chitin in fungi
    • Massachusetts Institute of Technology, R.A.A. Muzzarelli, E.R. Pariser (Eds.)
    • Ruiz-Herrera J. The distribution and quantitative importance of chitin in fungi. Proceedings of the Ist International Conference on Chitin and Chitosan 1978, 11-21. Massachusetts Institute of Technology. R.A.A. Muzzarelli, E.R. Pariser (Eds.).
    • (1978) Proceedings of the Ist International Conference on Chitin and Chitosan , pp. 11-21
    • Ruiz-Herrera, J.1
  • 3
    • 0034237306 scopus 로고    scopus 로고
    • Chitin deacetyalases: new, versatile tools in biotechnology
    • Tsigos I., et al. Chitin deacetyalases: new, versatile tools in biotechnology. Trends Biotechnol. 2000, 18:305-312.
    • (2000) Trends Biotechnol. , vol.18 , pp. 305-312
    • Tsigos, I.1
  • 4
    • 0030731058 scopus 로고    scopus 로고
    • Heterogeneous N-deacetylation of chitin in alkaline solution
    • Chang H. Heterogeneous N-deacetylation of chitin in alkaline solution. Carbohydr. Res. 1997, 303:327-332.
    • (1997) Carbohydr. Res. , vol.303 , pp. 327-332
    • Chang, H.1
  • 5
    • 0015979175 scopus 로고
    • A pathway of chitosan formation in Mucor rouxii: enzymatic deacetylation of chitin
    • Araki Y., Ito E. A pathway of chitosan formation in Mucor rouxii: enzymatic deacetylation of chitin. Biochem. Biophys. Res. Commun. 1975, 56:669-675.
    • (1975) Biochem. Biophys. Res. Commun. , vol.56 , pp. 669-675
    • Araki, Y.1    Ito, E.2
  • 6
    • 0028819719 scopus 로고
    • Purification and characterization of chitin deacetylase from Colletotrichum lindemuthianum
    • Tsigos I., Bouriotis V. Purification and characterization of chitin deacetylase from Colletotrichum lindemuthianum. J. Biol. Chem. 1995, 270:26286-26291.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26286-26291
    • Tsigos, I.1    Bouriotis, V.2
  • 7
    • 0037045870 scopus 로고    scopus 로고
    • Selection of Gongronella butleri strains for enhanced chitosan yield with UV mutagenesis
    • Maw T., et al. Selection of Gongronella butleri strains for enhanced chitosan yield with UV mutagenesis. J. Biotechnol. 2002, 95:189-193.
    • (2002) J. Biotechnol. , vol.95 , pp. 189-193
    • Maw, T.1
  • 8
    • 16444382409 scopus 로고    scopus 로고
    • The extracellular constitutive production of chitin deacetylase in Metarhizium anisopliae: possible edge to entomopathogenic fungi in the biological control of the insect pests
    • Nahar P., et al. The extracellular constitutive production of chitin deacetylase in Metarhizium anisopliae: possible edge to entomopathogenic fungi in the biological control of the insect pests. J. Invertebr. Pathol. 2004, 85:80-88.
    • (2004) J. Invertebr. Pathol. , vol.85 , pp. 80-88
    • Nahar, P.1
  • 9
    • 33746289630 scopus 로고    scopus 로고
    • Purification and characterization of chitin deacetylase from Scopulariopsis brevicaulis
    • Cai J., et al. Purification and characterization of chitin deacetylase from Scopulariopsis brevicaulis. Carbohydr. Pol. 2006, 65:211-217.
    • (2006) Carbohydr. Pol. , vol.65 , pp. 211-217
    • Cai, J.1
  • 10
    • 48649105376 scopus 로고    scopus 로고
    • Enzymatic deacetylation of chitin by extracellular chitin deacetylase from a newly screened Mortierella sp DY-52
    • Kim, et al. Enzymatic deacetylation of chitin by extracellular chitin deacetylase from a newly screened Mortierella sp DY-52. J. Microbiol. Biotechnol. 2008, 18:759-766.
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 759-766
    • Kim1
  • 11
    • 2542592570 scopus 로고    scopus 로고
    • Chitinolytic enzymes from Clostridium aminovalericum: activity screening and purification
    • Simunek J., et al. Chitinolytic enzymes from Clostridium aminovalericum: activity screening and purification. Folia Microbiol. 2004, 49:194-198.
    • (2004) Folia Microbiol. , vol.49 , pp. 194-198
    • Simunek, J.1
  • 12
    • 34249864385 scopus 로고    scopus 로고
    • Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin
    • Kadokura K., et al. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 2007, 75:357-365.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 357-365
    • Kadokura, K.1
  • 13
    • 61549136877 scopus 로고    scopus 로고
    • Novel mutation method for increased cellulase production
    • Chand P., et al. Novel mutation method for increased cellulase production. J. Appl. Microbiol. 2005, 28:606-610.
    • (2005) J. Appl. Microbiol. , vol.28 , pp. 606-610
    • Chand, P.1
  • 14
    • 35348855877 scopus 로고    scopus 로고
    • Comparison of three induced mutation methods for Acidothiobacillus caldus in processing sphalerite
    • Xia L., et al. Comparison of three induced mutation methods for Acidothiobacillus caldus in processing sphalerite. Miner. Eng. 2007, 20:1323-1326.
    • (2007) Miner. Eng. , vol.20 , pp. 1323-1326
    • Xia, L.1
  • 16
    • 0040425922 scopus 로고
    • Chitin deacetylase from Colletotrichum lindemuthianum
    • Academic Press, W.A. Woods, S.T. Kellogg (Eds.)
    • Kauss H., Bausch B. Chitin deacetylase from Colletotrichum lindemuthianum. Methods in Enzymology 1988, 518-523. Academic Press. W.A. Woods, S.T. Kellogg (Eds.).
    • (1988) Methods in Enzymology , pp. 518-523
    • Kauss, H.1    Bausch, B.2
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 19
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O.H., et al. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193:265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1
  • 20
    • 29944442946 scopus 로고    scopus 로고
    • Production of xylanase and protease by Penicillium janthinellum CRC 87M-115 from different agricultural wastes
    • Oliveira L.A., et al. Production of xylanase and protease by Penicillium janthinellum CRC 87M-115 from different agricultural wastes. Bioresour. Technol. 2006, 97:862-867.
    • (2006) Bioresour. Technol. , vol.97 , pp. 862-867
    • Oliveira, L.A.1
  • 21
    • 0004271860 scopus 로고
    • World Scientific Publishing Co. Pvt. Ltd./Utopia Press
    • Doelle H.W. Microbial Process Development 1994, World Scientific Publishing Co. Pvt. Ltd./Utopia Press.
    • (1994) Microbial Process Development
    • Doelle, H.W.1
  • 22
    • 1642487699 scopus 로고    scopus 로고
    • Citric acid production by selected mutants of Aspergillus niger from cane molasses
    • Ikram-ul H., et al. Citric acid production by selected mutants of Aspergillus niger from cane molasses. Bioresour. Technol. 2004, 93:125-130.
    • (2004) Bioresour. Technol. , vol.93 , pp. 125-130
    • Ikram-ul, H.1
  • 23
    • 29944444021 scopus 로고    scopus 로고
    • Strain improvement for tannase production from co-culture of Aspergillus foetidus and Rhizopus oryzae
    • Purohit J.S., et al. Strain improvement for tannase production from co-culture of Aspergillus foetidus and Rhizopus oryzae. Bioresour. Technol. 2006, 97:795-801.
    • (2006) Bioresour. Technol. , vol.97 , pp. 795-801
    • Purohit, J.S.1
  • 24
    • 33845754107 scopus 로고    scopus 로고
    • Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulase production
    • Adsul M.G., et al. Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulase production. Bioresour. Technol. 2007, 98:1467-1473.
    • (2007) Bioresour. Technol. , vol.98 , pp. 1467-1473
    • Adsul, M.G.1
  • 25
    • 70349582716 scopus 로고    scopus 로고
    • Overproduction of glucoamylase by a deregulated mutant of a thermophilic mould Thermomucor indicae-seudaticae
    • Kumar P., Satyanarayana T. Overproduction of glucoamylase by a deregulated mutant of a thermophilic mould Thermomucor indicae-seudaticae. Appl. Biochem. Biotechnol. 2009, 158:113-125.
    • (2009) Appl. Biochem. Biotechnol. , vol.158 , pp. 113-125
    • Kumar, P.1    Satyanarayana, T.2
  • 26
    • 70350635955 scopus 로고    scopus 로고
    • Enhanced production of an extracellular β-d-fructofuranosidase fructohydrolase from a 2-deoxy-d-glucose stabilized mutant of Candida utilis
    • Ali S., Ashiq M. Enhanced production of an extracellular β-d-fructofuranosidase fructohydrolase from a 2-deoxy-d-glucose stabilized mutant of Candida utilis. Appl. Biochem. Biotechnol. 2009, 159:453-463.
    • (2009) Appl. Biochem. Biotechnol. , vol.159 , pp. 453-463
    • Ali, S.1    Ashiq, M.2
  • 27
    • 0019480673 scopus 로고
    • Chitinase-overproducing mutant of Serratia marcescens
    • Reid J.D., Ogrydziak D.M. Chitinase-overproducing mutant of Serratia marcescens. Appl. Environ. Microbiol. 1981, 41:664-669.
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 664-669
    • Reid, J.D.1    Ogrydziak, D.M.2
  • 28
    • 0031148966 scopus 로고    scopus 로고
    • Properties of the chitinase of the antifungal biocontrol agent Streptomyces lydicus WYEC108
    • Mahadevan B., Crawford D.L. Properties of the chitinase of the antifungal biocontrol agent Streptomyces lydicus WYEC108. Enzyme Microb. Technol. 1997, 20:489-493.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 489-493
    • Mahadevan, B.1    Crawford, D.L.2
  • 29
    • 23844435977 scopus 로고    scopus 로고
    • Effect of different carbon sources on endochitinase production by Colletotrichum gloeosporioides
    • Souza R.F., et al. Effect of different carbon sources on endochitinase production by Colletotrichum gloeosporioides. Curr. Microbiol. 2005, 51:16-21.
    • (2005) Curr. Microbiol. , vol.51 , pp. 16-21
    • Souza, R.F.1
  • 30
    • 0033119843 scopus 로고    scopus 로고
    • Impact of process parameters on chitinase production by an alkalophilic marine Beauveria bassiana in solid state fermentation
    • Suresh P.V., Chandrasekaran M. Impact of process parameters on chitinase production by an alkalophilic marine Beauveria bassiana in solid state fermentation. Process Biochem. 1999, 34:257-267.
    • (1999) Process Biochem. , vol.34 , pp. 257-267
    • Suresh, P.V.1    Chandrasekaran, M.2
  • 31
    • 22544434369 scopus 로고    scopus 로고
    • Optimization of process parameters for chitinase production by soil isolates of Penicillium chrysogenum under solid substrate fermentation
    • Patidar P., et al. Optimization of process parameters for chitinase production by soil isolates of Penicillium chrysogenum under solid substrate fermentation. Process Biochem. 2005, 40:2962-2967.
    • (2005) Process Biochem. , vol.40 , pp. 2962-2967
    • Patidar, P.1
  • 32
    • 0000038470 scopus 로고
    • Solid state fermentation for production of alpha amylase by Bacillus megaterium 16 M
    • Ramesh M.V., Lonsane B.K. Solid state fermentation for production of alpha amylase by Bacillus megaterium 16 M. Biotechnol. Lett. 1987, 9:323-328.
    • (1987) Biotechnol. Lett. , vol.9 , pp. 323-328
    • Ramesh, M.V.1    Lonsane, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.