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Volumn 58, Issue 5, 2010, Pages 3184-3190

An acidophilic and acid-stable β-mannanase from Phialophora sp. P13 with high mannan hydrolysis activity under simulated gastric conditions

Author keywords

mannanase; Acidophilic and acid stable enzyme; Phialophora sp; Pichia pastoris

Indexed keywords

BETA MANNOSIDASE; MANNAN; PRIMER DNA;

EID: 77949350981     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf904367r     Document Type: Article
Times cited : (53)

References (30)
  • 1
    • 0032533450 scopus 로고    scopus 로고
    • High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5
    • Hilge, M.; Gloor, S. M.; Rypniewski, W.; Sauer, O.; Heightman, T. D.; Zimmermann, W.; Winterhalter, K.; Piontek, K. High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5. Structure 1998, 6, 1433-1444.
    • (1998) Structure , vol.6 , pp. 1433-1444
    • Hilge, M.1    Gloor, S.M.2    Rypniewski, W.3    Sauer, O.4    Heightman, T.D.5    Zimmermann, W.6    Winterhalter, K.7    Piontek, K.8
  • 2
    • 25444475386 scopus 로고    scopus 로고
    • Enzymology of endo-β-l,4-mannanase
    • Whitaker, J. R, Voragen, A. J. G, Wong, D. W. S, Eds, Marcel Dekker: New York
    • Stålbrand, H. Enzymology of endo-β-l,4-mannanase. In Handbook of Food Enzymology; Whitaker, J. R., Voragen, A. J. G, Wong, D. W. S., Eds.; Marcel Dekker: New York, 2003; pp 961-969.
    • (2003) Handbook of Food Enzymology , pp. 961-969
    • Stålbrand, H.1
  • 4
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991, 250, 309-316.
    • (1991) Biochem. J , vol.250 , pp. 309-316
    • Henrissat, B.1
  • 5
    • 57649138447 scopus 로고    scopus 로고
    • Biochemical and structural characterization of the intracellular mannanase AaManA of Alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan GH-A
    • Zhang, Y.; Ju, J.; Peng, H.; Gao, F.; Zhou, C.; Zeng, Y.; Xue, Y.; Li, Y.; Henrissat, B.; Gao, G. F.; Ma, Y. Biochemical and structural characterization of the intracellular mannanase AaManA of Alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan GH-A. J. Biol. Chem. 2008, 283, 31551-31558.
    • (2008) J. Biol. Chem , vol.283 , pp. 31551-31558
    • Zhang, Y.1    Ju, J.2    Peng, H.3    Gao, F.4    Zhou, C.5    Zeng, Y.6    Xue, Y.7    Li, Y.8    Henrissat, B.9    Gao, G.F.10    Ma, Y.11
  • 6
    • 25444475768 scopus 로고    scopus 로고
    • The structure and characterization of a modular endo-beta-1,4mannanase from Cellulomonas fimi
    • Nours, J. L.; Anderson, L.; Stoll, D.; Stålbrand, H.; Leggio, L. L. The structure and characterization of a modular endo-beta-1,4mannanase from Cellulomonas fimi. Biochemistry 2005, 44, 12700-12708.
    • (2005) Biochemistry , vol.44 , pp. 12700-12708
    • Nours, J.L.1    Anderson, L.2    Stoll, D.3    Stålbrand, H.4    Leggio, L.L.5
  • 8
    • 42649129680 scopus 로고    scopus 로고
    • An overview of mannan structure and mannan-degrading enzyme systems
    • Moreira, L. R.; Filho, E. X. F. An overview of mannan structure and mannan-degrading enzyme systems. Appl. Microbiol. Biotechnol. 2008, 79, 165-178.
    • (2008) Appl. Microbiol. Biotechnol , vol.79 , pp. 165-178
    • Moreira, L.R.1    Filho, E.X.F.2
  • 9
    • 60549106842 scopus 로고    scopus 로고
    • A novel highly acidic β-mannanase from the acidophilic fungus Bispora sp. MEY-I: Gene cloning and overexpression in Pichia pastoris
    • Luo, H.; Wang, Y.; Wang, H.; Yang, J.; Yang, Y.; Huang, H.; Yang, P.; Bai, Y.; Shi, P.; Fan, Y.; Yao, B. A novel highly acidic β-mannanase from the acidophilic fungus Bispora sp. MEY-I: gene cloning and overexpression in Pichia pastoris. Appl. Microbiol. Biotechnol. 2009, 82, 453-461.
    • (2009) Appl. Microbiol. Biotechnol , vol.82 , pp. 453-461
    • Luo, H.1    Wang, Y.2    Wang, H.3    Yang, J.4    Yang, Y.5    Huang, H.6    Yang, P.7    Bai, Y.8    Shi, P.9    Fan, Y.10    Yao, B.11
  • 10
    • 3142741043 scopus 로고    scopus 로고
    • Purification and characterization of a β-mannanase from Trichoderma harzianum strain T4
    • Ferreira, H. M.; Filho, E. X. F. Purification and characterization of a β-mannanase from Trichoderma harzianum strain T4. Carbohydr. Polym. 2004, 57, 23-29.
    • (2004) Carbohydr. Polym , vol.57 , pp. 23-29
    • Ferreira, H.M.1    Filho, E.X.F.2
  • 11
    • 33846392320 scopus 로고    scopus 로고
    • Cloning, functional expression and characterization of Aspergillus sulphureus β-mannanase in Pichia pastoris
    • Chen, X.; Cao, Y.; Ding, Y; Lu, W.; Li, D. Cloning, functional expression and characterization of Aspergillus sulphureus β-mannanase in Pichia pastoris. J. Biotechnol. 2007, 128, 452-461.
    • (2007) J. Biotechnol , vol.128 , pp. 452-461
    • Chen, X.1    Cao, Y.2    Ding, Y.3    Lu, W.4    Li, D.5
  • 12
    • 29244437175 scopus 로고    scopus 로고
    • Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme
    • Hatada, Y.; Takeda, N.; Hirasawa, K.; Ohta, Y.; Usami, R.; Yoshida, Y.; Grant, W. D.; Ito, S.; Horikoshi, K. Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme. Extremophiles 2005, 9, 497-500.
    • (2005) Extremophiles , vol.9 , pp. 497-500
    • Hatada, Y.1    Takeda, N.2    Hirasawa, K.3    Ohta, Y.4    Usami, R.5    Yoshida, Y.6    Grant, W.D.7    Ito, S.8    Horikoshi, K.9
  • 13
    • 12544256289 scopus 로고    scopus 로고
    • Characterization and gene cloning of a novel β-mannanase from alkaliphilic Bacillus sp. N16-5
    • Ma, Y.; Xue, Y.; Dou, Y.; Xu, Z; Tao, W.; Zhou, P. Characterization and gene cloning of a novel β-mannanase from alkaliphilic Bacillus sp. N16-5. Extremophiles 2004, 8, 447-454.
    • (2004) Extremophiles , vol.8 , pp. 447-454
    • Ma, Y.1    Xue, Y.2    Dou, Y.3    Xu, Z.4    Tao, W.5    Zhou, P.6
  • 14
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from Pl and YAC clones for chromosome walking
    • Liu, Y.; Whittier, R. F. Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from Pl and YAC clones for chromosome walking. Genomics 1995, 25, 674-681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.1    Whittier, R.F.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 33747333106 scopus 로고    scopus 로고
    • Miller, G. L. Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar. Anal. Chem. 1959, 31, 426-428.
    • Miller, G. L. Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar. Anal. Chem. 1959, 31, 426-428.
  • 19
    • 33751330608 scopus 로고    scopus 로고
    • Lineweaver, H.; Burk, D. The Determination of Enzyme Dissociation Constants. J. Am. Chem. Soc. 1934, 56, 658-666.
    • Lineweaver, H.; Burk, D. The Determination of Enzyme Dissociation Constants. J. Am. Chem. Soc. 1934, 56, 658-666.
  • 20
    • 33846860196 scopus 로고    scopus 로고
    • Cloning and overexpression of a Paenibacillus β-glucanase in Pichia pastoris: Purification and characterization of the recombinant enzyme
    • Yang, P.; Shi, P.; Wang, Y.; Bai, Y.; Meng, K.; Luo, H.; Yuan, T.; Yao, B. Cloning and overexpression of a Paenibacillus β-glucanase in Pichia pastoris: purification and characterization of the recombinant enzyme. J. Microbiol. Biotechnol. 2007, 17, 58-66.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 58-66
    • Yang, P.1    Shi, P.2    Wang, Y.3    Bai, Y.4    Meng, K.5    Luo, H.6    Yuan, T.7    Yao, B.8
  • 21
    • 67649236365 scopus 로고    scopus 로고
    • An Acidophilic β-Galactosidase from Bispora sp. MEY-1 with High Lactose Hydrolytic Activity under Simulated Gastric Conditions
    • Wang, H.; Luo, H.; Bai, Y.; Wang, Y.; Yang, P.; Shi, P.; Zhang, W.; Fan, Y.; Yao, B. An Acidophilic β-Galactosidase from Bispora sp. MEY-1 with High Lactose Hydrolytic Activity under Simulated Gastric Conditions. J. Agric. Food Chem. 2009, 57, 5535-5541.
    • (2009) J. Agric. Food Chem , vol.57 , pp. 5535-5541
    • Wang, H.1    Luo, H.2    Bai, Y.3    Wang, Y.4    Yang, P.5    Shi, P.6    Zhang, W.7    Fan, Y.8    Yao, B.9
  • 22
    • 50249156831 scopus 로고    scopus 로고
    • A novel phytase from Yersinia rohdei with high phytate hydrolysis activity under low pH and strong pepsin conditions
    • Huang, H.; Luo, H.; Wang, Y.; Fu, D.; Shao, N.; Wang, G.; Yang, P.; Yao, B. A novel phytase from Yersinia rohdei with high phytate hydrolysis activity under low pH and strong pepsin conditions. Appl. Microbiol. Biotechnol. 2008, 80, 417-426.
    • (2008) Appl. Microbiol. Biotechnol , vol.80 , pp. 417-426
    • Huang, H.1    Luo, H.2    Wang, Y.3    Fu, D.4    Shao, N.5    Wang, G.6    Yang, P.7    Yao, B.8
  • 23
    • 77949383280 scopus 로고    scopus 로고
    • Minekus, M; Marteau, P; Havenaar, R; Huis in't Veld, J. H. J. A multicompartmental dynamic computer-controlled model simulating the stomach and small intestine. Altern. Lab. Anim. 1995, 23, 197-209.
    • Minekus, M; Marteau, P; Havenaar, R; Huis in't Veld, J. H. J. A multicompartmental dynamic computer-controlled model simulating the stomach and small intestine. Altern. Lab. Anim. 1995, 23, 197-209.
  • 25
    • 0030004496 scopus 로고    scopus 로고
    • Purification of alkaline proteases from a Bacillus strain and their possible interrelationship
    • Kobayashi, T.; Hakamada, Y.; Hitomi, J.; Koike, K.; Ito, S. Purification of alkaline proteases from a Bacillus strain and their possible interrelationship. Appl. Microbiol. Biotechnol. 1996, 45, 63-71.
    • (1996) Appl. Microbiol. Biotechnol , vol.45 , pp. 63-71
    • Kobayashi, T.1    Hakamada, Y.2    Hitomi, J.3    Koike, K.4    Ito, S.5
  • 26
    • 10144234125 scopus 로고    scopus 로고
    • Characterization of extremely thermostable enzymatic breakers (alpha-1,6-galactosidase and beta-1,4-mannanase) from the hyperthermophilic bacterium Thermotoga neapolitana 5068 for hydrolysis of guar gum
    • McCutchen, C. M.; Duffaud, G. D.; Leduc, P.; Petersen, A. R. H.; Tayal, A.; Khan, S. A.; Kelly, R. M. Characterization of extremely thermostable enzymatic breakers (alpha-1,6-galactosidase and beta-1,4-mannanase) from the hyperthermophilic bacterium Thermotoga neapolitana 5068 for hydrolysis of guar gum. Biotechnol. Bioeng. 1996, 52, 332-339.
    • (1996) Biotechnol. Bioeng , vol.52 , pp. 332-339
    • McCutchen, C.M.1    Duffaud, G.D.2    Leduc, P.3    Petersen, A.R.H.4    Tayal, A.5    Khan, S.A.6    Kelly, R.M.7
  • 27
    • 0029666454 scopus 로고    scopus 로고
    • The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: A C-NMR study of Bacillus circulons xylanase
    • McIntosh, L. P.; Hand, G.; Johnson, P. E.; Joshi, M. D.; Körner, M.; Plesniak, L. A.; Ziser, L.; Wakarchuk, W. W.; Withers, S. G. The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a C-NMR study of Bacillus circulons xylanase. Biochemistry 1996, 35, 9958-9966.
    • (1996) Biochemistry , vol.35 , pp. 9958-9966
    • McIntosh, L.P.1    Hand, G.2    Johnson, P.E.3    Joshi, M.D.4    Körner, M.5    Plesniak, L.A.6    Ziser, L.7    Wakarchuk, W.W.8    Withers, S.G.9
  • 28
    • 12944280876 scopus 로고    scopus 로고
    • A highly acid-stable and thermostable endo-beta-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • Huang, Y.; Krauss, G.; Cottaz, S.; Driguez, H.; Lipps, G. A highly acid-stable and thermostable endo-beta-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus. Biochem. J. 2005, 385, 581-588.
    • (2005) Biochem. J , vol.385 , pp. 581-588
    • Huang, Y.1    Krauss, G.2    Cottaz, S.3    Driguez, H.4    Lipps, G.5
  • 29
    • 0032407988 scopus 로고    scopus 로고
    • Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: Biased distribution of acidic residues and importance of Asp37 for catalysis at low pH
    • Fushinobu, S.; Ito, K.; Konno, M.; Wakagi, T.; Matsuzawa, H. Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH. Protein Eng. 1998, 11, 1121-1128.
    • (1998) Protein Eng , vol.11 , pp. 1121-1128
    • Fushinobu, S.1    Ito, K.2    Konno, M.3    Wakagi, T.4    Matsuzawa, H.5
  • 30
    • 67650673628 scopus 로고    scopus 로고
    • A novel protease-resistant α-galactosidase with high hydrolytic activity from Gibberella sp. F75: Gene cloning, expression, and enzymatic characterization
    • Cao, Y.; Wang, Y.; Meng, K.; Bai, Y.; Shi, P.; Luo, H.; Yang, P.; Zhou, Z.; Zhang, Z.; Yao, B. A novel protease-resistant α-galactosidase with high hydrolytic activity from Gibberella sp. F75: gene cloning, expression, and enzymatic characterization. Appl. Microbiol. Biotechnol. 2009, 83, 875-884.
    • (2009) Appl. Microbiol. Biotechnol , vol.83 , pp. 875-884
    • Cao, Y.1    Wang, Y.2    Meng, K.3    Bai, Y.4    Shi, P.5    Luo, H.6    Yang, P.7    Zhou, Z.8    Zhang, Z.9    Yao, B.10


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