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Volumn 12, Issue , 2013, Pages 528-540

Production, purification and characterization of novel beta glucosidase from newly isolated Penicillium simplicissimum H-11 in submerged fermentation

Author keywords

glucosidase; Characterization; Penicillium simplicissimum; Purification

Indexed keywords

AMMONIUM SULFATE; BETA GLUCOSIDASE; COBALT; COPPER ION; FERRIC ION; SALICIN;

EID: 84879037841     PISSN: None     EISSN: 16112156     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (55)

References (37)
  • 1
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • Banker J. Amide modes and protein conformation. Biochim Biophys Acta 1992;1120: 123-43.
    • (1992) Biochim Biophys Acta , vol.1120 , pp. 123-143
    • Banker, J.1
  • 3
    • 84878636780 scopus 로고    scopus 로고
    • Purification and characterization of intracellular cellulase from Aspergillus oryzae ITCC-4857.01
    • Begum MF, Absar N. Purification and characterization of intracellular cellulase from Aspergillus oryzae ITCC-4857.01. Mycobiology 2009;37:121-7.
    • (2009) Mycobiology , vol.37 , pp. 121-127
    • Begum, M.F.1    Absar, N.2
  • 4
    • 0034253208 scopus 로고    scopus 로고
    • Cellulases and related enzymes in biotechnology
    • Bhat MK. Cellulases and related enzymes in biotechnology. Biotechnol Adv 2000; 18:355-83.
    • (2000) Biotechnol Adv , vol.18 , pp. 355-383
    • Bhat, M.K.1
  • 5
    • 0036448608 scopus 로고    scopus 로고
    • Microbial β-glucosidases: Cloning, properties, and applications
    • Bhatia Y, Mishra S, Bisaria VS. Microbial β-glucosidases: cloning, properties, and applications. Crit Rev Biotechnol 2002;22: 375-407.
    • (2002) Crit Rev Biotechnol , vol.22 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 6
    • 84873045391 scopus 로고    scopus 로고
    • Production and characterization of a novel β-glucosidase from Fusarium solani
    • Bhatti HN, Batool S, Afzal N. Production and characterization of a novel β-glucosidase from Fusarium solani. Int J Agric Biol 2013;15:140-4.
    • (2013) Int J Agric Biol , vol.15 , pp. 140-144
    • Bhatti, H.N.1    Batool, S.2    Afzal, N.3
  • 7
    • 50049110704 scopus 로고    scopus 로고
    • Purification and biochemical characterization of extracellular beta-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis
    • Bhiri F, Chaabouni SE, Limam F, Ghrir R, Marzouki N. Purification and biochemical characterization of extracellular beta-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis. Appl Biochem Biotechnol 2008;149:169-82.
    • (2008) Appl Biochem Biotechnol , vol.149 , pp. 169-182
    • Bhiri, F.1    Chaabouni, S.E.2    Limam, F.3    Ghrir, R.4    Marzouki, N.5
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt Biochem 1976;72:248.
    • (1976) Analyt Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 9
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler DM, Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymer 1986;25:469-87.
    • (1986) Biopolymer , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 11
    • 84862239638 scopus 로고    scopus 로고
    • A highly efficient β-glucosidase from the buffalo rumen fungus Neocallimastix patriciarum W5
    • Chen H, Chen Y, Lu MJ, Chang J, Wang HC, Ke H et al. A highly efficient β-glucosidase from the buffalo rumen fungus Neocallimastix patriciarum W5. Biotechnol Biofuels 2012;5:24.
    • (2012) Biotechnol Biofuels , vol.5 , pp. 24
    • Chen, H.1    Chen, Y.2    Lu, M.J.3    Chang, J.4    Wang, H.C.5    Ke, H.6
  • 12
    • 0026794451 scopus 로고
    • Secondary structure of the pentraxin female protein in water determined by infrared spectroscopy: Effects of calcium and phosphorylcholine
    • Dong A, Caughey B, Caughey WS, Bhat KS, Coe JE. Secondary structure of the pentraxin female protein in water determined by infrared spectroscopy: Effects of calcium and phosphorylcholine. Biochemistry 1992;31:9364-70.
    • (1992) Biochemistry , vol.31 , pp. 9364-9370
    • Dong, A.1    Caughey, B.2    Caughey, W.S.3    Bhat, K.S.4    Coe, J.E.5
  • 13
    • 0001256511 scopus 로고
    • Structure of synthetic polypeptides
    • Elliott A, Ambrose EJ. Structure of synthetic polypeptides. Nature 1950;165: 921-2.
    • (1950) Nature , vol.165 , pp. 921-922
    • Elliott, A.1    Ambrose, E.J.2
  • 14
    • 84855808115 scopus 로고    scopus 로고
    • Purification and some kinetic properties of β-glucosidase from Aspergillus terreus NRRL 265
    • Elshafei AM, Hassan MM, Morsi NM, Elghonamy DH. Purification and some kinetic properties of β-glucosidase from Aspergillus terreus NRRL 265. Afr J Biotechnol 2011;10:19556-69.
    • (2011) Afr J Biotechnol , vol.10 , pp. 19556-19569
    • Elshafei, A.M.1    Hassan, M.M.2    Morsi, N.M.3    Elghonamy, D.H.4
  • 17
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B, Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem J 1996;316:695-6.
    • (1996) Biochem J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 18
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence based classification of glycosyl hydrolases
    • Henrissat B, Davies GJ. Structural and sequence based classification of glycosyl hydrolases. Curr Opin Struc Biol 1997;7:637-44.
    • (1997) Curr Opin Struc Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.J.2
  • 19
    • 84855611427 scopus 로고    scopus 로고
    • FTIR and SEM analysis of thermo-chemical fractionated of Sugarcane Bagasse
    • Irfan M, Syed Q, Abbas S, GulSher M, Baig S, Nadeem M. FTIR and SEM analysis of thermo-chemical fractionated of Sugarcane Bagasse. Turk J Biochem 2011;36: 322-8.
    • (2011) Turk J Biochem , vol.36 , pp. 322-328
    • Irfan, M.1    Syed, Q.2    Abbas, S.3    Gulsher, M.4    Baig, S.5    Nadeem, M.6
  • 20
  • 21
    • 80051855655 scopus 로고    scopus 로고
    • Characterization of selected cellulolytic activities of multi-enzymatic complex system from Penicillium funiculosum
    • Karboune S, Geraert PA, Kermasha S. Characterization of selected cellulolytic activities of multi-enzymatic complex system from Penicillium funiculosum. J Agric Food Chem 2008;56:903-9.
    • (2008) J Agric Food Chem , vol.56 , pp. 903-909
    • Karboune, S.1    Geraert, P.A.2    Kermasha, S.3
  • 22
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong J, Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin 2007;39:549-59.
    • (2007) Acta Biochim Biophys Sin , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 23
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S, Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Protein Chem 1986;38:181-364.
    • (1986) Adv Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriaophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriaophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0027519943 scopus 로고
    • Protein glycosylation
    • Lis H, Sharon N. Protein glycosylation. Europ J Biochem 1993:218:1-27.
    • (1993) Europ J Biochem , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 27
    • 84856984996 scopus 로고    scopus 로고
    • Characterization of a thermostable b-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33
    • Liu D, Zhang R, Yang X, Zhang Z, Song S, Miao Y et al. Characterization of a thermostable b-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33. Microb Cell Fact 2012; 11:25.
    • (2012) Microb Cell Fact , vol.11 , pp. 25
    • Liu, D.1    Zhang, R.2    Yang, X.3    Zhang, Z.4    Song, S.5    Miao, Y.6
  • 28
    • 84862966812 scopus 로고    scopus 로고
    • Purification and characterization of β- 1,4-glucosidase from Aspergillus glaucus
    • Ma S, Leng B, Xu X, Zhu X, Shi Y, Tao Y, et al. Purification and characterization of β- 1,4-glucosidase from Aspergillus glaucus. Afr J Biotechnol 2011;10:19607-14.
    • (2011) Afr J Biotechnol , vol.10 , pp. 19607-19614
    • Ma, S.1    Leng, B.2    Xu, X.3    Zhu, X.4    Shi, Y.5    Tao, Y.6
  • 29
    • 0000320288 scopus 로고
    • Characteristic infrared bands of monosubstituted amides
    • Miyazawa T, Shimanouchi T, Mizushima S. Characteristic infrared bands of monosubstituted amides. J Chem Phys 1956;24: 408.
    • (1956) J Chem Phys , vol.24 , pp. 408
    • Miyazawa, T.1    Shimanouchi, T.2    Mizushima, S.3
  • 30
    • 84873923895 scopus 로고    scopus 로고
    • Hydrolysis of lignocellulosic feedstock by Rumniococcus albus in production of biofuel ethanol
    • Mutalik S, Kumar CSV, Swamy S, Manjappa S. Hydrolysis of lignocellulosic feedstock by Rumniococcus albus in production of biofuel ethanol. Ind J Biotechnol 2012; 11:453-7.
    • (2012) Ind J Biotechnol , vol.11 , pp. 453-457
    • Mutalik, S.1    Kumar, C.S.V.2    Swamy, S.3    Manjappa, S.4
  • 32
    • 84866348014 scopus 로고    scopus 로고
    • Production, purification, and characterization of a β-glucosidase of Penicillium funiculosum NCL1
    • Ramani G, Meera B, Vanitha C, Rao M, Gunasekaran P. Production, purification, and characterization of a β-glucosidase of Penicillium funiculosum NCL1. Appl Biochem Biotechnol 2012;167:959-72.
    • (2012) Appl Biochem Biotechnol , vol.167 , pp. 959-972
    • Ramani, G.1    Meera, B.2    Vanitha, C.3    Rao, M.4    Gunasekaran, P.5
  • 33
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae
    • Riou C, Salmon JM, Vallier MJ, Gunata Z, Barre P. Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae. Appl Environ Microbiol 1998; 64:3607-14.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.M.2    Vallier, M.J.3    Gunata, Z.4    Barre, P.5
  • 34
    • 0022463740 scopus 로고
    • Resolution-enhanced fourier transform infrared spectroscopy of enzymes
    • Susi H, Byler DM. Resolution-enhanced fourier transform infrared spectroscopy of enzymes. Methods Enzymol 1986;130: 290-311.
    • (1986) Methods Enzymol , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 35
    • 0036266523 scopus 로고    scopus 로고
    • Hydrophobic interaction, chromatography of trichoderma reesei cellulase on polypropylene glycol-sepharose
    • Tomaz T, Roche A. Hydrophobic interaction, chromatography of trichoderma reesei cellulase on polypropylene glycol-sepharose. Sep Sci Technol 2002;37:1-11.
    • (2002) Sep Sci Technol , vol.37 , pp. 1-11
    • Tomaz, T.1    Roche, A.2
  • 36
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley beta- D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese JN, Hrmova M, Fincher GB. Three-dimensional structure of a barley beta- D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 1997;7:179-90.
    • (1997) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.