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Volumn 47, Issue 3, 2012, Pages 509-516

Potential application of two thermostable lichenases from a newly isolated Bacillus licheniformis UEB CF: Purification and characterization

Author keywords

Bacillus licheniformis; Detergent activity; Lichenases; Surfactant stable; Thermostable

Indexed keywords

BACILLUS LICHENIFORMIS; DETERGENT INDUSTRY; ENDOGLUCANASES; LAMINARINS; LICHENASES; N-TERMINAL AMINO ACID SEQUENCE; OPTIMUM PH; OPTIMUM TEMPERATURE; OXIDIZING AGENTS; POTENTIAL APPLICATIONS; SDS-PAGE; SURFACTANT-STABLE; THERMOSTABLE;

EID: 84856217238     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.12.010     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0022842368 scopus 로고
    • The sequence statistics and solution conformation of a barley (1,3-1,4)-β-d-glucan
    • G.S. Buliga, D.A. Brant, and G.B. Fincher The sequence statistics and solution conformation of a barley (1,3-1,4)-β-d-glucan Carbohydr Res 57 1986 139 156
    • (1986) Carbohydr Res , vol.57 , pp. 139-156
    • Buliga, G.S.1    Brant, D.A.2    Fincher, G.B.3
  • 2
    • 33947606382 scopus 로고    scopus 로고
    • Improved quantitative analysis of oligosaccharides from lichenasehydrolyzed water-soluble barley β-glucans by high-performance anion-exchange chromatography
    • D.H. Yoo, B.H. Lee, P.S. Chang, H.G. Lee, and S.H. Yoo Improved quantitative analysis of oligosaccharides from lichenasehydrolyzed water-soluble barley β-glucans by high-performance anion-exchange chromatography J Agric Food Chem 55 2007 1656 1662
    • (2007) J Agric Food Chem , vol.55 , pp. 1656-1662
    • Yoo, D.H.1    Lee, B.H.2    Chang, P.S.3    Lee, H.G.4    Yoo, S.H.5
  • 3
    • 0242383940 scopus 로고    scopus 로고
    • Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1,4- and β-1,3;1,4-linked glucans
    • DOI 10.1016/S0141-8130(03)00080-1
    • T. McCarthy, O. Hanniffy, A. Savage, and M.G. Tuohy Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1,4-and β-1,3,1,4-linked glucans Int J Biol Macromol 33 2003 141 148 (Pubitemid 37346369)
    • (2003) International Journal of Biological Macromolecules , vol.33 , Issue.1-3 , pp. 141-148
    • McCarthy, T.1    Hanniffy, O.2    Savage, A.V.3    Tuohy, M.G.4
  • 4
    • 34548295727 scopus 로고    scopus 로고
    • Production, purification and application relevant characterization of an endo-1,3(4)-β-glucanase from Rhizomucor miehei
    • A. Boyce, and G. Walsh Production, purification and application relevant characterization of an endo-1,3(4)-β-glucanase from Rhizomucor miehei Appl Microbiol Biotechnol 76 2007 835 841
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 835-841
    • Boyce, A.1    Walsh, G.2
  • 5
    • 47849101161 scopus 로고    scopus 로고
    • Biochemical characterization of a novel thermostable β-1,3-1,4- glucanase (Lichenase) from Paecilomyces thermophila
    • DOI 10.1021/jf800303b
    • S. Yang, Q. Yan, Z. Jiang, G. Fan, and L. Wang Biochemical characterization of a novel thermostable β-1,3-1,4-glucanase (lichenase) from Paecilomyces thermophila J Agric Food Chem 56 2008 5345 5351 (Pubitemid 352039145)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.13 , pp. 5345-5351
    • Yang, S.1    Qiaojuan, Y.2    Jiang, Z.3    Fan, G.4    Wang, L.5
  • 6
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for many families of glycosyl hydrolases
    • B. Henrissat, I. Callebaut, S. Fabrega, P. Lehn, J. Mornon, and G. Davies Conserved catalytic machinery and the prediction of a common fold for many families of glycosyl hydrolases Proc Natl Acad Sci USA 92 1995 7090 7094
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.5    Davies, G.6
  • 7
    • 0016611070 scopus 로고
    • A new substrate for investigating the specificity of beta-glucan hydrolases
    • M.A. Anderson, and B.A. Stone A new substrate for investigating the specificity of beta-glucan hydrolases FEBS Lett 52 1975 202 207
    • (1975) FEBS Lett , vol.52 , pp. 202-207
    • Anderson, M.A.1    Stone, B.A.2
  • 8
    • 33845688815 scopus 로고    scopus 로고
    • Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry
    • K.R.S. Celestino, R.B. Cunha, and C.R. Felix Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry BMC Biochem 7 2006 23
    • (2006) BMC Biochem , vol.7 , pp. 23
    • Celestino, K.R.S.1    Cunha, R.B.2    Felix, C.R.3
  • 9
    • 0347700479 scopus 로고    scopus 로고
    • Effects of xylanase and β-glucanase addition on performance, nutrient digestibility, and physico-chemical conditions in the small intestine contents and caecal microflora of broiler chickens fed a wheat and barley-based diet
    • N. Mathlouthi, M. Serge, S. Luc, Q. Bernard, and L. Michel Effects of xylanase and β-glucanase addition on performance, nutrient digestibility, and physico-chemical conditions in the small intestine contents and faecal microflora of broiler chickens fed a wheat and barley-based diet Anim Res 51 2002 395 406 (Pubitemid 135712125)
    • (2002) Animal Research , vol.51 , Issue.5 , pp. 395-406
    • Mathlouthi, N.1    Mallet, S.2    Saulnier, L.3    Ouemener, B.4    Larbier, M.5
  • 10
    • 33745172830 scopus 로고    scopus 로고
    • Isolation and identification of mixed linked β-glucan degrading bacteria in the intestine of broiler chickens and partial characterization of respective 1,3-1,4-β-glucanase activities
    • DOI 10.1002/jobm.200510107
    • L. Beckmann, O. Simon, and W. Vahjen Isolation and identification of mixed linked β-glucan degrading bacteria in the intestine of broiler chickens and partial characterization of respective 1,3-1,4-β-glucanase activities J Basic Microbiol 46 2006 175 185 (Pubitemid 43893581)
    • (2006) Journal of Basic Microbiology , vol.46 , Issue.3 , pp. 175-185
    • Beckmann, L.1    Simon, O.2    Vahjen, W.3
  • 12
    • 0030765668 scopus 로고    scopus 로고
    • Isolation and overexpression of a gene encoding an extracellular β- (1,3-l,4)-glucanase from Streptococcus bovis JB1
    • M.S. Ekinci, S.I. McCrae, and H.J. Flint Isolation and overexpression of a gene encoding an extracellular β-(1,3-1,4)-glucanase from Streptococcus bovis JB1 Appl Environ Microbiol 63 1997 3752 3756 (Pubitemid 27411323)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.10 , pp. 3752-3756
    • Ekinci, M.S.1    Mccrae, S.I.2    Flint, H.J.3
  • 13
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4-β-glucanases: Structure, function and protein engineering
    • A. Planas Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering Biochem Biophys Acta 1543 2000 361 382
    • (2000) Biochem Biophys Acta , vol.1543 , pp. 361-382
    • Planas, A.1
  • 14
    • 33749009721 scopus 로고    scopus 로고
    • Cloning of β-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039 (CGMCC 0635) and its expression in Escherichia coli BL21 (DE3)
    • DOI 10.1007/s00253-006-0329-2
    • D. Teng, J. Wang, Y. Fan, Y. Yang, Z. Tian, and J. Luo Cloning of β-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039 (CGMCC 0635) and its expression in Escherichia coli BL21 (DE3) Appl Microbiol Biotechnol 72 2006 705 712 (Pubitemid 44454930)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.4 , pp. 705-712
    • Teng, D.1    Wang, J.-H.2    Fan, Y.3    Yang, Y.-L.4    Tian, Z.-G.5    Luo, J.6    Yang, G.-P.7    Zhang, F.8
  • 15
    • 38349108789 scopus 로고    scopus 로고
    • High-level expression of a truncated 1,3-1,4-β-d-glucanase from Fibrobacter succinogenes in Pichia pastoris by optimization of codons and fermentation
    • H.Q. Huang, P.L. Yang, H.Y. Luo, H.G. Tang, N. Shao, and T.Z. Yuan High-level expression of a truncated 1,3-1,4-β-d-glucanase from Fibrobacter succinogenes in Pichia pastoris by optimization of codons and fermentation Appl Microbiol Biotechnol 78 2008 95 103
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 95-103
    • Huang, H.Q.1    Yang, P.L.2    Luo, H.Y.3    Tang, H.G.4    Shao, N.5    Yuan, T.Z.6
  • 16
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Cold Spring Harbor, NY
    • J.H. Miller Experiments in molecular genetics 1972 Cold Spring Harbor Laboratory Cold Spring Harbor, NY p. 466
    • (1972) Experiments in Molecular Genetics , pp. 466
    • Miller, J.H.1
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • G.L. Miller Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal Chem 31 1959 426 428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors
    • DOI 10.1006/abio.1993.1457
    • F.L. Garcia-Carreno, L.F. Dimes, and N.F. Haard Substrate-gel electrophoresis for composition and molecular weight of proteinase or proteinaceous proteinase inhibitors Anal Biochem 214 1993 65 69 (Pubitemid 23300354)
    • (1993) Analytical Biochemistry , vol.214 , Issue.1 , pp. 65-69
    • Garcia-Carreno, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 21
    • 63449085549 scopus 로고    scopus 로고
    • Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: Purification, characterization and potential application as a laundry detergent additive
    • A. Haddar, R. Agrebi, A. Bougatef, N. Hmidet, A. Sellami-Kamoun, and M. Nasri Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: purification, characterization and potential application as a laundry detergent additive Bioresour Technol 100 2009 3366 3373
    • (2009) Bioresour Technol , vol.100 , pp. 3366-3373
    • Haddar, A.1    Agrebi, R.2    Bougatef, A.3    Hmidet, N.4    Sellami-Kamoun, A.5    Nasri, M.6
  • 22
    • 1642446551 scopus 로고    scopus 로고
    • Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF-1A5 using response surface methodology
    • X.J. Tang, G.Q. He, Q.H. Chen, X.Y. Zhang, and A.M. Ali Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF-1A5 using response surface methodology Bioresour Technol 93 2004 175 181
    • (2004) Bioresour Technol , vol.93 , pp. 175-181
    • Tang, X.J.1    He, G.Q.2    Chen, Q.H.3    Zhang, X.Y.4    Ali, A.M.5
  • 23
    • 0027524789 scopus 로고
    • Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • J. Stulke, R. Hanschke, and M. Hecker Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool J Gen Microbiol 139 1993 2041 2045 (Pubitemid 23284972)
    • (1993) Journal of General Microbiology , vol.139 , Issue.9 , pp. 2041-2045
    • Stulke, J.1    Hanschke, R.2    Hecker, M.3
  • 24
    • 50049110704 scopus 로고    scopus 로고
    • Purification and biochemical characterization of extracellular beta-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis
    • F. Bhiri, S. Ellouz Chaabouni, F. Limam, R. Ghrir, and N. Marzouki Purification and biochemical characterization of extracellular beta-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis Appl Biochem Biotechnol 149 2 2008 169 182
    • (2008) Appl Biochem Biotechnol , vol.149 , Issue.2 , pp. 169-182
    • Bhiri, F.1    Ellouz Chaabouni, S.2    Limam, F.3    Ghrir, R.4    Marzouki, N.5
  • 25
    • 0032507712 scopus 로고    scopus 로고
    • 2-terminal sequencing of an endo- (1 → 3,1 → 4)-β-glucanase from rice (Oryza sativa L.) bran
    • DOI 10.1016/S0168-9452(98)00032-6, PII S0168945298000326
    • 2-terminal sequencing of an endo-(1-3,1-4)-β-glucanase from rice (Oryza sativa L.) bran Plant Sci 134 1998 3 10 (Pubitemid 28303383)
    • (1998) Plant Science , vol.134 , Issue.1 , pp. 3-10
    • Akiyama, T.1    Kaku, H.2    Shibuya, N.3
  • 26
    • 0035811982 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
    • DOI 10.1016/S0141-0229(01)00354-4, PII S0141022901003544
    • P.G. Murray, A. Grassick, C.D. Laffey, M.M. Cuffe, T. Higgins, and A.V. Savage Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-d-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70 Enzyme Microb Technol 29 2001 90 98 (Pubitemid 32566389)
    • (2001) Enzyme and Microbial Technology , vol.29 , Issue.1 , pp. 90-98
    • Murray, P.G.1    Grassick, A.2    Laffey, C.D.3    Cuffe, M.M.4    Higgins, T.5    Savage, A.V.6    Planas, A.7    Tuohy, M.G.8
  • 27
    • 0002687206 scopus 로고
    • Purification and characterization of endo-p-l, 3-1,4-d-glucanase activity from Bacillus licheniformis
    • J. Lloberas, E. Querol, and J. Bernués Purification and characterization of endo-p-l, 3-1,4-d-glucanase activity from Bacillus licheniformis Appl Microbiol Biotechnol 29 1988 32 38
    • (1988) Appl Microbiol Biotechnol , vol.29 , pp. 32-38
    • Lloberas, J.1    Querol, E.2    Bernués, J.3
  • 28
    • 0025772933 scopus 로고
    • Properties of a thermoactive β-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli
    • S. Schimming, W.H. Schwarz, and W.L. Staudenbauer Properties of a thermoactive β-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli Biochem Biophys Res Commun 177 1991 447 452
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 447-452
    • Schimming, S.1    Schwarz, W.H.2    Staudenbauer, W.L.3
  • 29
    • 52049115933 scopus 로고    scopus 로고
    • Grass degrading β-1,3-1,4-d-glucanases from Bacillus subtilis GN156: Purification and characterization of glucanase J1 and pJ2 possessing extremely acidic pI
    • J. Apiraksakorn, S. Nitisinprasert, and R.E. Levin Grass degrading β-1,3-1,4-d-glucanases from Bacillus subtilis GN156: purification and characterization of glucanase J1 and pJ2 possessing extremely acidic pI Appl Biochem Biotechnol 149 2008 53 66
    • (2008) Appl Biochem Biotechnol , vol.149 , pp. 53-66
    • Apiraksakorn, J.1    Nitisinprasert, S.2    Levin, R.E.3
  • 30
    • 0032126046 scopus 로고    scopus 로고
    • Characterization of endoglucanases from the brown rot fungi Gloeophyllum sepiarium and Gloeophyllum trabeum
    • DOI 10.1016/S0141-0229(98)00033-7, PII S0141022998000337
    • S.D. Mansfield, J.N. Saddler, and G.M. Gubitz Characterisation of endoglucanases from the brown rot fungi Gloeophyllum sepiarium and Gloeophyllum traberum Enzyme Microbiol Technol 23 1998 133 140 (Pubitemid 28379072)
    • (1998) Enzyme and Microbial Technology , vol.23 , Issue.1-2 , pp. 133-140
    • Mansfield, S.D.1    Saddler, J.N.2    Gubitz, G.M.3
  • 31
    • 0028962474 scopus 로고
    • Structural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase CelD
    • S. Chauvaux, H. Souchon, P.M. Alzari, P. Chariot, and P. Beguin Structural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase CelD J Biol Chem 270 17 1995 9757 9762
    • (1995) J Biol Chem , vol.270 , Issue.17 , pp. 9757-9762
    • Chauvaux, S.1    Souchon, H.2    Alzari, P.M.3    Chariot, P.4    Beguin, P.5
  • 32
    • 70849094923 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable β-1,3-1,4- glucanase from Laetiporus sulphureus var. miniatus
    • M.R. Hong, K. Yeong-Su, J. Ah-Reum, L. Jung-Kul, K. Yeong-Suk, and O. Deok-Kun Purification and characterization of a thermostable β-1,3-1,4-glucanase from Laetiporus sulphureus var. miniatus J Microbiol Biotechnol 19 8 2009 818 822
    • (2009) J Microbiol Biotechnol , vol.19 , Issue.8 , pp. 818-822
    • Hong, M.R.1    Yeong-Su, K.2    Ah-Reum, J.3    Jung-Kul, L.4    Yeong-Suk, K.5    Deok-Kun, O.6
  • 33
    • 34447249051 scopus 로고    scopus 로고
    • Purification and characterization of thermostable beta-1,3-1,4 glucanase from Bacillus sp. A8-8
    • Y.J. Jung, J.S. Yoo, Y.S. Lee, I.H. Park, S.H. Kim, and S.C. Lee Purification and characterization of thermostable beta-1,3-1,4 glucanase from Bacillus sp. A8-8 Biotechnol Bioprocess Eng 12 2007 265 270
    • (2007) Biotechnol Bioprocess Eng , vol.12 , pp. 265-270
    • Jung, Y.J.1    Yoo, J.S.2    Lee, Y.S.3    Park, I.H.4    Kim, S.H.5    Lee, S.C.6
  • 34
    • 0001680804 scopus 로고
    • Selective enzymolysis of poly-β-d glucan and the structure of the polymers
    • F.W. Parrish, A.S. Perlin, and E.T. Reese Selective enzymolysis of poly-β-d glucan and the structure of the polymers Can J Chem 38 1960 2094 2104
    • (1960) Can J Chem , vol.38 , pp. 2094-2104
    • Parrish, F.W.1    Perlin, A.S.2    Reese, E.T.3
  • 35
    • 0028962948 scopus 로고
    • Genes encoding xylan and β-glucan hydrolyzing enzymes in Bacillus subtilis: Characterization, mapping and construction of strains deficient in lichenase, cellulase and xylanase
    • M. Wolf, A. Geczi, O. Simon, and R. Borriss Genes encoding xylan and β-glucan hydrolyzing enzymes in Bacillus subtilis: characterization, mapping and construction of strains deficient in lichenase, cellulase and xylanase Microbiology 4 1995 281 290
    • (1995) Microbiology , vol.4 , pp. 281-290
    • Wolf, M.1    Geczi, A.2    Simon, O.3    Borriss, R.4
  • 36
    • 0025994102 scopus 로고
    • Microbial β-glucanase different from cellulases
    • S. Bielecki, and E. Galas Microbial β-glucanase different from cellulases Crit Rev Biotechnol 10 1991 275 305
    • (1991) Crit Rev Biotechnol , vol.10 , pp. 275-305
    • Bielecki, S.1    Galas, E.2
  • 37
    • 20444448807 scopus 로고    scopus 로고
    • A novel β-glucanase gene from Bacillus halodurans C-125
    • DOI 10.1016/j.femsle.2005.05.009, PII S0378109705002910
    • M. Akita, K. Kaytama, Y. Hatada, S. Ito, and K. Horikoshi A novel β-glucanase gene from Bacillus halodurans C-125 FEMS Microbiol Lett 248 2005 9 15 (Pubitemid 40828309)
    • (2005) FEMS Microbiology Letters , vol.248 , Issue.1 , pp. 9-15
    • Akita, M.1    Kayatama, K.2    Hatada, Y.3    Ito, S.4    Horikoshi, K.5
  • 38
    • 0017083431 scopus 로고
    • Degradation of barley glucan and lichenan by Bacillus pumilus enzyme
    • H. Suzuki, and T. Kaneko Degradation of barley glucan and lichenan by Bacillus pumilus enzyme Agric Biol Chem 40 1976 577 586
    • (1976) Agric Biol Chem , vol.40 , pp. 577-586
    • Suzuki, H.1    Kaneko, T.2
  • 39
    • 29944444016 scopus 로고    scopus 로고
    • A lichenase-like family 12 endo-(1→4)-β-glucanase from Aspergillus japonicus: Study of the substrate specificity and mode of action on β-glucans in comparison with other glycoside hydrolases
    • DOI 10.1016/j.carres.2005.11.011, PII S0008621505005112
    • S.G. Grishutin, A.V. Gusakov, E.I. Dzedzyulya, and A.P. Sinitsyn A lichenase-like family 12 endo-(1,4)-β-glucanase from Aspergillus japonicus: study of the substrate specificity and mode of action on β-glucans in comparison with other glycoside hydrolases Carbohydr Res 341 2006 218 229 (Pubitemid 43042605)
    • (2006) Carbohydrate Research , vol.341 , Issue.2 , pp. 218-229
    • Grishutin, S.G.1    Gusakov, A.V.2    Dzedzyulya, E.I.3    Sinitsyn, A.P.4
  • 40
    • 0023684974 scopus 로고
    • Purification and properties of a 1,3-1,4-β-glucanase (lichenase, 1,3-1,4-β-D-glucan 4-glucanohydrolase, EC 3.2.1.73) from Bacteroides succinogenes cloned in Escherichia coli
    • J.D. Erfle, R.M. Teather, P.J. Wood, and J.E. Irvin Purification and properties of a 1,3-1,4-β-d-glucanase (lichenase, 1,3-1,4-β-d-glucan 4-glucanohydrolase, EC 3.2.1.73) from Bacteroides succinogenes cloned in Escherichia coli Biochem J 255 1988 833 841 (Pubitemid 18263948)
    • (1988) Biochemical Journal , vol.255 , Issue.3 , pp. 833-841
    • Erfle, J.D.1    Teather, R.M.2    Wood, P.J.3    Irvin, J.E.4
  • 41
    • 0000853597 scopus 로고    scopus 로고
    • Fractionation of oat (1→3), (1→4)-β-d-glucans and characterisation of the fractions 1
    • M.S. Izydorczyk, G.G. Biliaderis, L.J. Macri, and A.W. MacGregor Fractionation of oat (1 → 3)(1 → 4)-β-d-glucans and characterization of the fractions J Cereal Sci 27 1998 321 325 (Pubitemid 128373640)
    • (1998) Journal of Cereal Science , vol.27 , Issue.3 , pp. 321-325
    • Izydorczyk, M.S.1    Biliaderis, C.G.2    Macri, L.J.3    Macgregor, A.W.4
  • 42
    • 3042543053 scopus 로고    scopus 로고
    • A comparative study on structure-function relations of mixedlinkage linear β-glucans
    • A. Lazaridou, C.G. Biliaderis, M. Micha-Screttas, and B.R. Steele A comparative study on structure-function relations of mixedlinkage linear β-glucans Food Hydrocolloid 18 2004 837 855
    • (2004) Food Hydrocolloid , vol.18 , pp. 837-855
    • Lazaridou, A.1    Biliaderis, C.G.2    Micha-Screttas, M.3    Steele, B.R.4
  • 43
    • 0001000529 scopus 로고
    • Structural studies of (1 → 3), (1 → 4)-β-d-glucans by 13C-NMR and by rapid analysis of cellulose-like regions using high-performance anion-exchange chromatography of oligosaccharides released by lichenase
    • P.J. Wood, J. Weisz, and B.A. Blackwell Structural studies of (1 → 3), (1 → 4)-β-d-glucans by 13C-NMR and by rapid analysis of cellulose-like regions using high-performance anion-exchange chromatography of oligosaccharides released by lichenase Cereal Chem 71 1994 301 307
    • (1994) Cereal Chem , vol.71 , pp. 301-307
    • Wood, P.J.1    Weisz, J.2    Blackwell, B.A.3
  • 44
    • 0012345289 scopus 로고
    • Synthesis of an N-acetylchito oligosaccharide-carrying styrene-type macromer and its high-molecular-weight homopolymer
    • K. Kobayashi, K. Aoki, H. Sumitomo, and T. Akaike Synthesis of an N-acetylchito oligosaccharide-carrying styrene-type macromer and its high-molecular-weight homopolymer Die Makromol Chem 11 1990 577 582
    • (1990) Die Makromol Chem , vol.11 , pp. 577-582
    • Kobayashi, K.1    Aoki, K.2    Sumitomo, H.3    Akaike, T.4
  • 45
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: From a bioindustrial viewpoint
    • DOI 10.1016/S0734-9750(99)00027-0, PII S0734975099000270
    • C.G. Kumar, and H. Takagi Microbial alkaline proteases: from a bioindustrial viewpoint Biotechnol Adv 17 1999 561 594 (Pubitemid 30086544)
    • (1999) Biotechnology Advances , vol.17 , Issue.7 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2


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