메뉴 건너뛰기




Volumn 16, Issue 1, 2011, Pages 114-119

Effects of various inhibitors on β-galactosidase purified from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. rittmannii isolated from Antarctica

Author keywords

Galactosidase; Galactose; Inhibition; Metal ion chelators; PMCB and PMSF

Indexed keywords

1 ,10-PHENANTHROLINE; 2-MERCAPTOETHANOL; ACTIVE SITE; ALICYCLOBACILLUS ACIDOCALDARIUS; ANTARCTICA; CYS RESIDUES; ENZYMATIC ACTIVITIES; GALACTOSE; GALACTOSIDASES; LACTOSE HYDROLYSIS; METALLOENZYMES; PHENYLMETHYLSULFONYL FLUORIDE; PLOT ANALYSIS; PMCB AND PMSF;

EID: 80052027571     PISSN: 12268372     EISSN: 19763816     Source Type: Journal    
DOI: 10.1007/s12257-010-0070-7     Document Type: Article
Times cited : (35)

References (22)
  • 1
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases [1]
    • Henrisat, B. and A. Bairoch (1996) Updating a sequencebased classification of glycosyl hydrolases. Biochem. J. 316:695-696. (Pubitemid 26182174)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 2
    • 0032135068 scopus 로고    scopus 로고
    • Thermostable β-Galactosidase from an Extreme Thermophile, Thermus sp. A4: Enzyme Purification and Characterization, and Gene Cloning and Sequencing
    • Ohtsu, N., H. Motoshima, K. Goto, F. Tsukasaki, and H. Matsuzawa (1998). Thermostable β-galactosidase from an extreme thermophile Thermus sp. A4: Enzyme purification and characterisation, Gene Cloning and Sequencing. Biosci. Biotechnol. Biochem. 62:1539-1545. (Pubitemid 128475080)
    • (1998) Bioscience, Biotechnology and Biochemistry , vol.62 , Issue.8 , pp. 1539-1545
    • Ohtsu, N.1    Motoshima, H.2    Goto, K.3    Tsukasaki, F.4    Matsuzawa, H.5
  • 3
    • 0034128505 scopus 로고    scopus 로고
    • Sequence and expression of a halobacterial β-galactosidase
    • Holmes, M. L and M. L. Dyall-Smith (2000) Sequence and expression of a halobacterial β-galactosidase. Gen. Mol. Microbiol. 36:114-122.
    • (2000) Gen. Mol. Microbiol. , vol.36 , pp. 114-122
    • Holmes, M.L.1    Dyall-Smith, M.L.2
  • 4
    • 0034080264 scopus 로고    scopus 로고
    • Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic antarctic Planococcus isolate
    • DOI 10.1128/AEM.66.6.2438-2444.2000
    • Sheridan, P. P. and J. E. Brenchley (2000) Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic antarctic Planococcus isolate. Appl. Environ. Microbiol. 66:2438-2444. (Pubitemid 30353949)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.6 , pp. 2438-2444
    • Sheridan, P.P.1    Brenchley, J.E.2
  • 5
    • 0036968554 scopus 로고    scopus 로고
    • Trimeric crystal structure of the glycoside hydrolase family 42 β-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose
    • DOI 10.1016/S0022-2836(02)00746-5
    • Hidaka, M., S. Fushinobu, N. Ohtsu, H. Motoshima, H. Matsuzawa, H. Shoun, and T. Wakagi (2002) Trimeric crystal structure of the glycoside hydrolase family 42 β-galactosidase from Thermus termophilus A4 and the structure of its complex with galactose. J. Mol. Biol. 322:79-91. (Pubitemid 36132672)
    • (2002) Journal of Molecular Biology , vol.322 , Issue.1 , pp. 79-91
    • Hidaka, M.1    Fushinobu, S.2    Ohtsu, N.3    Motoshima, H.4    Matsuzawa, H.5    Shoun, H.6    Wakagi, T.7
  • 6
    • 33947582209 scopus 로고    scopus 로고
    • Purification and some properties of a β-galactosidase from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. rittmannii isolated from Antarctica
    • DOI 10.1016/j.enzmictec.2006.11.006, PII S0141022906005485
    • Gul-Guven, R., K. Guven, A. Poli, and B. Nicolaus (2007) Purification and some properties of a β-galactosidase from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. rittmannii isolated from Antarctica. Enz. Microb. Technol. 40:1570-1577. (Pubitemid 46482645)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.6 , pp. 1570-1577
    • Gul-Guven, R.1    Guven, K.2    Poli, A.3    Nicolaus, B.4
  • 7
    • 38549105991 scopus 로고    scopus 로고
    • Isolation and characterization of a new family 42 β-galactosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius: Identification of the active site residues
    • Di Lauro, B., A. Strazzulli, G. Perugino, F. La Cara, E. Bedini, M. M. Corsaro, M. Rossi, and M. Moracci (2008) Isolation and characterization of a new family 42 β-galactosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius: Identification of the active site residues. Biochim. et Biophysica Acta 1784:292-301.
    • (2008) Biochim. et Biophysica Acta , vol.1784 , pp. 292-301
    • Di Lauro, B.1    Strazzulli, A.2    Perugino, G.3    La Cara, F.4    Bedini, E.5    Corsaro, M.M.6    Rossi, M.7    Moracci, M.8
  • 8
    • 76649083583 scopus 로고    scopus 로고
    • Effects of galactose and glucose on the hydrolysis reaction of a thermostable β-galactosidase from Caldicellulosiruptor saccharolyticus
    • Park, A. R. and D. K. Oh (2010) Effects of galactose and glucose on the hydrolysis reaction of a thermostable β-galactosidase from Caldicellulosiruptor saccharolyticus. Appl. Microbiol. Biotechnol. 85:1427-1435.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1427-1435
    • Park, A.R.1    Oh, D.K.2
  • 9
    • 34248581677 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile in Family 42 β-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis
    • DOI 10.1016/j.febslet.2007.04.053, PII S001457930700453X
    • Shaikh, F. A., J. Mullegger, S. He, and S. G. Withers (2007) Identification of the catalytic nucleophile in family 42 β-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis. FEBS Lett. 581:2441-2446. (Pubitemid 46764703)
    • (2007) FEBS Letters , vol.581 , Issue.13 , pp. 2441-2446
    • Shaikh, F.A.1    Mullegger, J.2    He, S.3    Withers, S.G.4
  • 10
    • 0032126799 scopus 로고    scopus 로고
    • Galactose competitive inhibition of β-galactosidase (Aspergillus oryzae) immobilized on chitosan and nylon supports
    • DOI 10.1016/S0141-0229(98)00018-0, PII S0141022998000180
    • Portaccio, M., S. Stellato, S. Rossi, U. Bencivenga, M. S. Mohy Eldin, F. S. Gaeta, and D. G. Mita (1998) Galactose competitive inhibition of β-galactosidase (Aspergillus oryzae) immobilized on chitosan and nylon supports. Enz. Microbial Technol. 23:101-106. (Pubitemid 28379067)
    • (1998) Enzyme and Microbial Technology , vol.23 , Issue.1-2 , pp. 101-106
    • Portaccio, M.1    Stellato, S.2    Rossi, S.3    Bencivenga, U.4    Mohy Eldin, M.S.5    Gaeta, F.S.6    Mita, D.G.7
  • 11
    • 0034693116 scopus 로고    scopus 로고
    • Purification and characterisation of a β-galactosidase from Aspergillus aculeatus with activity towards (modified) exopolysaccharides from Lactococcus lactis subsp. cremoris B39 and B891
    • van Casteren, W. H. M., M. Eimermann, L. A. M. van den Broek, J. P. Vincken, H. A. Schols, and A. G. J. Voragen (2000) Purification and characterisation of a β-galactosidase from Aspergillus aculeatus with activity towards (modified) exopolysaccharides from Lactococcus lactis subsp. cremoris B39 and B891. Carbohydrate Res. 329:75-85.
    • (2000) Carbohydrate Res. , vol.329 , pp. 75-85
    • Van Casteren, W.H.M.1    Eimermann, M.2    Van Den Broek, L.A.M.3    Vincken, J.P.4    Schols, H.A.5    Voragen, A.G.J.6
  • 12
    • 0034816937 scopus 로고    scopus 로고
    • A mechanistical mathematical model to predict lactose hydrolysis by β-galactosidase in a permeabilized cell mass of Kluyveromyces lactis: Validity and sensitivity analysis
    • DOI 10.1016/S0032-9592(01)00211-4, PII S0032959201002114
    • Fontes, E. A. F, F. M. L. Passos, and F. J. V. Passos (2001) A mechanistical mathematical model to predict lactose hydrolysis by β-galactosidase in a permeabilized cell mass of Kluyveromyceslactis: Validity and sensitivity analysis. Proc. Biochem. 37:267-274. (Pubitemid 32928925)
    • (2001) Process Biochemistry , vol.37 , Issue.3 , pp. 267-274
    • Fontes, E.A.F.1    Passos, F.M.L.2    Passos, F.J.V.3
  • 13
    • 37549063875 scopus 로고    scopus 로고
    • Heterologous expression of a gene encoding a thermostable β-galactosidase from Alicyclobacillus acidocaldarius
    • Yuan, T., P. Yang, Y. Wang, K. Meng, H. Luo, W. Zhang, N. Wu, Y. Fan, and B. Yao (2008) Heterologous expression of a gene encoding a thermostable β-galactosidase from Alicyclobacillus acidocaldarius. Biotechnol. Lett. 30:343-348.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 343-348
    • Yuan, T.1    Yang, P.2    Wang, Y.3    Meng, K.4    Luo, H.5    Zhang, W.6    Wu, N.7    Fan, Y.8    Yao, B.9
  • 14
    • 0031886814 scopus 로고    scopus 로고
    • Alicyclobacilli from an unexplored geothermal soil in Antarctica: Mount Rittmann
    • DOI 10.1007/s003000050224
    • Nicolaus, B., R. Importa, M. C. Manca, L. Lama, E. Esposito, and A. Gambacorta (1998) Alicyclobacillus from an unexplored geotermal soil in Antarctica: Mount Rittmann. Polar Biol. 19:133-141. (Pubitemid 28111286)
    • (1998) Polar Biology , vol.19 , Issue.2 , pp. 133-141
    • Nicolaus, B.1    Improta, R.2    Manca, M.C.3    Lama, L.4    Esposito, E.5    Gambacorta, A.6
  • 15
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden, A. (1974) A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem. J. 137:143-144.
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 16
    • 67249118564 scopus 로고    scopus 로고
    • Enzyme inhibition and activition: A general theory
    • Saboury, A. A. (2009) Enzyme inhibition and activition: A general theory. J. Iranian Chem. Soc. 6:219-229.
    • (2009) J. Iranian Chem. Soc. , vol.6 , pp. 219-229
    • Saboury, A.A.1
  • 19
    • 33947513910 scopus 로고    scopus 로고
    • Calcium alginate entrapped preparations of Aspergillus oryzae β galactosidase: Its stability and applications in the hydrolysis of lactose
    • DOI 10.1016/j.ijbiomac.2007.01.001, PII S0141813007000062
    • Haider, T. and O. Husain (2007) Calcium alginate entrapped preparations of Aspergillus oryzae β-galactosidase: Its stability and applications in the hydrolysis of lactose. Inter. J. Biol. Macromol. 41:72-80. (Pubitemid 46466930)
    • (2007) International Journal of Biological Macromolecules , vol.41 , Issue.1 , pp. 72-80
    • Haider, T.1    Husain, Q.2
  • 20
    • 0021506933 scopus 로고
    • Some properties of a β-galactosidase from an extremely thermophilic bacterium
    • Cowan, D. A., R. M. Daniel, A. M. Martin, and H. W. Morgan (1984) Some properties of a β-galactosidase from an extremely thermophilic bacterium. Biotechnol. Bioeng. 26:1141-1145. (Pubitemid 14016406)
    • (1984) Biotechnology and Bioengineering , vol.26 , Issue.10 , pp. 1141-1145
    • Cowan, D.A.1    Daniel, R.M.2    Martin, A.M.3    Morgan, H.W.4
  • 21
    • 0026176947 scopus 로고
    • Specificity, inhibitory studies, and oligosaccharide formation by β-galactosidase from psychrotrophic Bacillus subtilis
    • Rahim, K. A. A. and B. Lee (1991) Specificity, inhibitory studies, and oligosaccharide formation by β-galactosidase from psychrotrophic Bacillus subtilis. KL88. J. Dairy Sci. 74:1773-1778.
    • (1991) KL88. J. Dairy Sci. , vol.74 , pp. 1773-1778
    • Rahim, K.A.A.1    Lee, B.2
  • 22
    • 0025904881 scopus 로고
    • A highly reactive β-Galactosidase (Escherichia coli) resulting from a substitution of an aspartic acid for Gly-794
    • Martinez-Bilbao, M., R. E. Holdsworth, L. A. Edwards, and R. E. Huber (1991) A highly reactive β-galactosidase (Escherichia coli) resulting from a substitution of an aspartic acid for Gly-794. J. Biol. Chem. 266:4979-4986. (Pubitemid 21909451)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.8 , pp. 4979-4986
    • Martinez-Bilbao, M.1    Holdsworth, R.E.2    Edwards, L.A.3    Huber, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.