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1
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4243961395
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Novozymes emerges
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McCoy M. Novozymes emerges. Chem Eng News. 19:2000;23-25.
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(2000)
Chem Eng News
, vol.19
, pp. 23-25
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McCoy, M.1
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2
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0035575497
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In vitro enzyme evolution: The screening challenge of isolating the one in a million
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Cohen N., Abramov S., Dror Y., Freeman A. In vitro enzyme evolution: the screening challenge of isolating the one in a million. Trends Biotechnol. 19:2001;507-510.
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(2001)
Trends Biotechnol
, vol.19
, pp. 507-510
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Cohen, N.1
Abramov, S.2
Dror, Y.3
Freeman, A.4
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3
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0036902361
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Substrate arrays as enzyme fingerprinting tools
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An elegant review utilizing substrate arrays for enzyme fingerprinting. The authors assayed a series of enzymes and substrates and describe the potential of arrays for enzyme discovery and quality control applications.
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Reymond J.L., Wahler D. Substrate arrays as enzyme fingerprinting tools. Chembiochem. 3:2002;701-708 An elegant review utilizing substrate arrays for enzyme fingerprinting. The authors assayed a series of enzymes and substrates and describe the potential of arrays for enzyme discovery and quality control applications.
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(2002)
Chembiochem
, vol.3
, pp. 701-708
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Reymond, J.L.1
Wahler, D.2
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4
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0036669678
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Industrial enzyme applications
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An overview of the recent developments of industrial enzymes.
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Kirk O., Borchert T.V., Fuglsang C.C. Industrial enzyme applications. Curr Opin Biotechnol. 13:2002;345-351 An overview of the recent developments of industrial enzymes.
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(2002)
Curr Opin Biotechnol
, vol.13
, pp. 345-351
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Kirk, O.1
Borchert, T.V.2
Fuglsang, C.C.3
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5
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0036669414
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Enzyme technology: An overview
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A useful review on the effects of new enzyme technologies.
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van Beilen J.B., Li Z. Enzyme technology: an overview. Curr Opin Biotechnol. 13:2002;338-344 A useful review on the effects of new enzyme technologies.
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(2002)
Curr Opin Biotechnol
, vol.13
, pp. 338-344
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Van Beilen, J.B.1
Li, Z.2
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6
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0037436563
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Dispelling the myths - Biocatalysis in industrial synthesis
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Schoemaker H.E., Mink D., Wubbolts M.G. Dispelling the myths - biocatalysis in industrial synthesis. Science. 299:2003;1694-1697.
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(2003)
Science
, vol.299
, pp. 1694-1697
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Schoemaker, H.E.1
Mink, D.2
Wubbolts, M.G.3
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7
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0036536478
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Directed evolution of enzymes and pathways for industrial biocatalysis
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Zhao H., Chockalingam K., Chen Z. Directed evolution of enzymes and pathways for industrial biocatalysis. Curr Opin Biotechnol. 13:2002;104-110.
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(2002)
Curr Opin Biotechnol
, vol.13
, pp. 104-110
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Zhao, H.1
Chockalingam, K.2
Chen, Z.3
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8
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0036773518
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Optimizing lipases and related enzymes for efficient application
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In a very thorough review the authors present three design approaches for optimization of lipases and related enzymes for effective applications. These approaches include: physicochemical approaches, reaction engineering and molecular biology methods.
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Bornscheuer U.T., Bessler C., Srinivas R., Krishna S.H. Optimizing lipases and related enzymes for efficient application. Trends Biotechnol. 20:2002;433-437 In a very thorough review the authors present three design approaches for optimization of lipases and related enzymes for effective applications. These approaches include: physicochemical approaches, reaction engineering and molecular biology methods.
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(2002)
Trends Biotechnol
, vol.20
, pp. 433-437
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Bornscheuer, U.T.1
Bessler, C.2
Srinivas, R.3
Krishna, S.H.4
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10
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0036897839
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Milestones in directed enzyme evolution
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Tao H., Cornish V.W. Milestones in directed enzyme evolution. Curr Opin Chem Biol. 6:2002;858-864.
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(2002)
Curr Opin Chem Biol
, vol.6
, pp. 858-864
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Tao, H.1
Cornish, V.W.2
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11
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85031080365
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Novozymes A/S: Annual Report 2002. Edited by Bagsvaerd, Denmark; 2002. URL:
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Novozymes A/S: Annual Report 2002. Edited by Bagsvaerd, Denmark; 2002. URL: http://www.novozymes.com/cgi-bin/bvisapi.dll/ar2002/welcome.jsp?lang=en.
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12
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0036323668
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Bacterial alkaline proteases: Molecular approaches and industrial applications
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Gupta R., Beg Q.K., Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol. 59:2002;15-32.
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(2002)
Appl Microbiol Biotechnol
, vol.59
, pp. 15-32
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Gupta, R.1
Beg, Q.K.2
Lorenz, P.3
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13
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0035745539
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Enhanced production and characterization of a highly thermostable alkaline protease from Bacillus sp. P-2
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Kaur S., Vohra R.M., Kapoor M., Beg Q.K., Hoondaldal G.S. Enhanced production and characterization of a highly thermostable alkaline protease from Bacillus sp. P-2. World J Microbiol Biotechnol. 17:2001;125-129.
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(2001)
World J Microbiol Biotechnol
, vol.17
, pp. 125-129
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Kaur, S.1
Vohra, R.M.2
Kapoor, M.3
Beg, Q.K.4
Hoondaldal, G.S.5
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14
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0001735819
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Novel enzymes from unknown microbes - Direct cloning of the metagenome
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Lorenz P., Liebeton K., Niehaus F., Eck J., Zinke H. Novel enzymes from unknown microbes - direct cloning of the metagenome. Int Symp Bicatal Biotransform. 5:2001;379.
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(2001)
Int Symp Bicatal Biotransform
, vol.5
, pp. 379
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Lorenz, P.1
Liebeton, K.2
Niehaus, F.3
Eck, J.4
Zinke, H.5
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15
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0036901312
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Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently
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The authors describe an elegant way to shuffle DNA sequences that do not necessarily arise from a physical gene. This technique provides another option for DNA shuffling for use in directed evolution.
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Ness J.E., Kim S., Gottman A., Pak R., Krebber A., Borchert T.V., Govindarajan S., Mundorff E.C., Minshull J. Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently. Nat Biotechnol. 20:2002;1251-1255 The authors describe an elegant way to shuffle DNA sequences that do not necessarily arise from a physical gene. This technique provides another option for DNA shuffling for use in directed evolution.
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(2002)
Nat Biotechnol
, vol.20
, pp. 1251-1255
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Ness, J.E.1
Kim, S.2
Gottman, A.3
Pak, R.4
Krebber, A.5
Borchert, T.V.6
Govindarajan, S.7
Mundorff, E.C.8
Minshull, J.9
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16
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0037424370
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Activity-stability relationships in extremophilic enzymes
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Outstanding work demonstrating the value of coupling analysis of thermodynamic parameters with enzyme performance. Analyzing properties of an extremophilic α-amylase, the authors propose a rational basis for stability-activity relationships in such thermophilic enzymes.
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D'Amico S., Marx J.C., Gerday C., Feller G. Activity-stability relationships in extremophilic enzymes. J Biol Chem. 278:2003;7891-7896 Outstanding work demonstrating the value of coupling analysis of thermodynamic parameters with enzyme performance. Analyzing properties of an extremophilic α-amylase, the authors propose a rational basis for stability-activity relationships in such thermophilic enzymes.
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(2003)
J Biol Chem
, vol.278
, pp. 7891-7896
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D'Amico, S.1
Marx, J.C.2
Gerday, C.3
Feller, G.4
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17
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0037837789
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Kinetic stabilization of Bacillus licheniformis α-amylase through introduction of hydrophobic residues at the surface
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This paper demonstrates the surprising result of stabilization of a solvent by adding a hydrophobic sidechain to the exposed surface of an α-amylase.
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Machius M., Declerck N., Huber R., Wiegand G. Kinetic stabilization of Bacillus licheniformis α-amylase through introduction of hydrophobic residues at the surface. J Biol Chem. 278:2003;11546-11553 This paper demonstrates the surprising result of stabilization of a solvent by adding a hydrophobic sidechain to the exposed surface of an α-amylase.
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(2003)
J Biol Chem
, vol.278
, pp. 11546-11553
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Machius, M.1
Declerck, N.2
Huber, R.3
Wiegand, G.4
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18
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0037135614
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A novel, high performance enzyme for starch liquefaction. Discovery and optimization of a low pH, thermostable α-amylase
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Richardson T.H., Tan X., Frey G., Callen W., Cabell M., Lam D., Macomber J., Short J.M., Robertson D.E., Miller C. A novel, high performance enzyme for starch liquefaction. Discovery and optimization of a low pH, thermostable α-amylase. J Biol Chem. 277:2002;26501-26507.
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(2002)
J Biol Chem
, vol.277
, pp. 26501-26507
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Richardson, T.H.1
Tan, X.2
Frey, G.3
Callen, W.4
Cabell, M.5
Lam, D.6
Macomber, J.7
Short, J.M.8
Robertson, D.E.9
Miller, C.10
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19
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0037425010
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Diversa promises products, profits
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Thayer A.M. Diversa promises products, profits. Chem Eng News. 81:2003;15-17.
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(2003)
Chem Eng News
, vol.81
, pp. 15-17
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Thayer, A.M.1
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20
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0038521353
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Replacement of methionine 208 in a truncated Bacillus sp. TS-23 α-amylase with oxidation-resistant leucine enhances its resistance to hydrogen peroxide
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Lin L.L., Lo H.F., Chiang W.Y., Hu H.Y., Hsu W.H., Chang C.T. Replacement of methionine 208 in a truncated Bacillus sp. TS-23 α-amylase with oxidation-resistant leucine enhances its resistance to hydrogen peroxide. Curr Microbiol. 46:2003;211-216.
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(2003)
Curr Microbiol
, vol.46
, pp. 211-216
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Lin, L.L.1
Lo, H.F.2
Chiang, W.Y.3
Hu, H.Y.4
Hsu, W.H.5
Chang, C.T.6
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21
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0037247952
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Phytases: Microbial sources, production, purification, and potential biotechnological applications
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Vohra A., Satyanarayana T. Phytases: microbial sources, production, purification, and potential biotechnological applications. Crit Rev Biotechnol. 23:2003;29-60.
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(2003)
Crit Rev Biotechnol
, vol.23
, pp. 29-60
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Vohra, A.1
Satyanarayana, T.2
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22
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0036271498
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The consensus concept for thermostability engineering of proteins: Further proof of concept
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Lehmann M., Loch C., Middendorf A., Studer D., Lassen S.F., Pasamontes L., van Loon A.P., Wyss M. The consensus concept for thermostability engineering of proteins: further proof of concept. Protein Eng. 15:2002;403-411.
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(2002)
Protein Eng
, vol.15
, pp. 403-411
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Lehmann, M.1
Loch, C.2
Middendorf, A.3
Studer, D.4
Lassen, S.F.5
Pasamontes, L.6
Van Loon, A.P.7
Wyss, M.8
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23
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0036033349
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Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0
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Utilizing a rational protein design approach, one single amino acid substitution in A. niger phytase produced an enzyme with 56% increased catalysis at the important physiological conditions of pH 4.0 and 37°C.
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Mullaney E.J., Daly C.B., Kim T., Porres J.M., Lei X.G., Sethumadhavan K., Ullah A.H. Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0. Biochem Biophys Res Commun. 297:2002;1016-1020 Utilizing a rational protein design approach, one single amino acid substitution in A. niger phytase produced an enzyme with 56% increased catalysis at the important physiological conditions of pH 4.0 and 37°C.
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(2002)
Biochem Biophys Res Commun
, vol.297
, pp. 1016-1020
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Mullaney, E.J.1
Daly, C.B.2
Kim, T.3
Porres, J.M.4
Lei, X.G.5
Sethumadhavan, K.6
Ullah, A.H.7
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24
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0036204592
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Engineering of phytase for improved activity at low pH
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The authors improved the pH profiles of Aspergillus fumigatus and consensus phytases by site-directed mutagenesis based on rational protein design.
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Tomschy A., Brugger R., Lehmann M., Svendsen A., Vogel K., Kostrewa D., Lassen S.F., Burger D., Kronenberger A., van Loon A.P.et al. Engineering of phytase for improved activity at low pH. Appl Environ Microbiol. 68:2002;1907-1913 The authors improved the pH profiles of Aspergillus fumigatus and consensus phytases by site-directed mutagenesis based on rational protein design.
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(2002)
Appl Environ Microbiol
, vol.68
, pp. 1907-1913
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Tomschy, A.1
Brugger, R.2
Lehmann, M.3
Svendsen, A.4
Vogel, K.5
Kostrewa, D.6
Lassen, S.F.7
Burger, D.8
Kronenberger, A.9
Van Loon, A.P.10
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25
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0036295882
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Cloned and expressed fungal phyA gene in alfalfa produces a stable phytase
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This work describes the successful stable expression of a fungal phytase in alfafa.
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Ullah A.H., Sethumadhavan K., Mullaney E.J., Ziegelhoffer T., Austin-Phillips S. Cloned and expressed fungal phyA gene in alfalfa produces a stable phytase. Biochem Biophys Res Commun. 290:2002;1343-1348 This work describes the successful stable expression of a fungal phytase in alfafa.
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(2002)
Biochem Biophys Res Commun
, vol.290
, pp. 1343-1348
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Ullah, A.H.1
Sethumadhavan, K.2
Mullaney, E.J.3
Ziegelhoffer, T.4
Austin-Phillips, S.5
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26
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0037322616
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Functional expression of a fungal laccase in Saccharomyces cerevisiae by directed evolution
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Bulter T., Alcalde M., Sieber V., Meinhold P., Schlachtbauer C., Arnold F.H. Functional expression of a fungal laccase in Saccharomyces cerevisiae by directed evolution. Appl Environ Microbiol. 69:2003;987-995.
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(2003)
Appl Environ Microbiol
, vol.69
, pp. 987-995
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Bulter, T.1
Alcalde, M.2
Sieber, V.3
Meinhold, P.4
Schlachtbauer, C.5
Arnold, F.H.6
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27
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0038143259
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Enguita FJ, Martins LO, Henriques AO, Carrondo MA: Crystal structure of a bacterial endospore coat component: A Laccase with enchanced thermostability properties. J Biol Chem 2003: in press.
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Enguita FJ, Martins LO, Henriques AO, Carrondo MA: Crystal structure of a bacterial endospore coat component: A Laccase with enchanced thermostability properties. J Biol Chem 2003: in press.
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28
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0037379158
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Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability
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Sandgren M., Gualfetti P.J., Shaw A., Gross L.S., Saldajeno M., Day A.G., Jones T.A., Mitchinson C. Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability. Protein Sci. 12:2003;848-860.
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(2003)
Protein Sci
, vol.12
, pp. 848-860
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Sandgren, M.1
Gualfetti, P.J.2
Shaw, A.3
Gross, L.S.4
Saldajeno, M.5
Day, A.G.6
Jones, T.A.7
Mitchinson, C.8
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29
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0036901551
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DNA family shuffling of hyperthermostable β-glycosidases
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This paper shows for the first time that hyperthermostable enzymes can be used in a directed evolution approach to generate hybrid enyzmes with improved catalytic characteristics.
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Kaper T., Brouns S.J., Geerling A.C., De Vos W.M., Van der Oost J. DNA family shuffling of hyperthermostable β-glycosidases. Biochem J. 368:2002;461-470 This paper shows for the first time that hyperthermostable enzymes can be used in a directed evolution approach to generate hybrid enyzmes with improved catalytic characteristics.
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(2002)
Biochem J
, vol.368
, pp. 461-470
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Kaper, T.1
Brouns, S.J.2
Geerling, A.C.3
De Vos, W.M.4
Van der Oost, J.5
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30
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0037335665
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The relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A
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The relationship between thermostability and alkaline acitivity in cellobiohydrolases from glycosyl hydrolase family 7 (Cel7) were elegantly analyzed in this paper. The authors showed that the five amino acid substitutions responsible for the improved activity effectively narrowed the useful pH optima.
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Boer H., Koivula A. The relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A. Eur J Biochem. 270:2003;841-848 The relationship between thermostability and alkaline acitivity in cellobiohydrolases from glycosyl hydrolase family 7 (Cel7) were elegantly analyzed in this paper. The authors showed that the five amino acid substitutions responsible for the improved activity effectively narrowed the useful pH optima.
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(2003)
Eur J Biochem
, vol.270
, pp. 841-848
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Boer, H.1
Koivula, A.2
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31
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0035854021
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Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling
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The paper describes an elegant approach to shuffle distant genes. Analyses of the chimeric genes obtained demonstrated the potential of the method to generate shuffled libraries.
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Gibbs M.D., Nevalainen K.M., Bergquist P.L. Degenerate oligonucleotide gene shuffling (DOGS): a method for enhancing the frequency of recombination with family shuffling. Gene. 271:2001;13-20 The paper describes an elegant approach to shuffle distant genes. Analyses of the chimeric genes obtained demonstrated the potential of the method to generate shuffled libraries.
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(2001)
Gene
, vol.271
, pp. 13-20
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Gibbs, M.D.1
Nevalainen, K.M.2
Bergquist, P.L.3
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32
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0036372478
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Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD
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This paper describes the successful thermostabilization of an endoglucanase. With only one round of a two-step screening, the authors isolated an endoglucanase variant with higher thermostability than the wild-type parental enzymes.
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Murashima K., Kosugi A., Doi R.H. Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD. Mol Microbiol. 45:2002;617-626 This paper describes the successful thermostabilization of an endoglucanase. With only one round of a two-step screening, the authors isolated an endoglucanase variant with higher thermostability than the wild-type parental enzymes.
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(2002)
Mol Microbiol
, vol.45
, pp. 617-626
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Murashima, K.1
Kosugi, A.2
Doi, R.H.3
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34
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85031078274
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Brugger R, Simoes Nunes C, Hug D, Vogel K, Guggenbuhl P, Mascarello F, Augem S, Wyss M, Van Loon AP, Pasamontes L: Characteristics of fungal phytases from Aspergillus fumigatus and Sartorya fumigata. Appl Microbiol Biotechnol 2003: in press.
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Brugger R, Simoes Nunes C, Hug D, Vogel K, Guggenbuhl P, Mascarello F, Augem S, Wyss M, Van Loon AP, Pasamontes L: Characteristics of fungal phytases from Aspergillus fumigatus and Sartorya fumigata. Appl Microbiol Biotechnol 2003: in press.
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35
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0038034712
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Combined sequence and structure analysis of the fungal laccase family
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Kumar S.V., Phale P.S., Durani S., Wangikar P.P. Combined sequence and structure analysis of the fungal laccase family. Biotechnol Bioeng. 83:2003;386-394.
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(2003)
Biotechnol Bioeng
, vol.83
, pp. 386-394
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Kumar, S.V.1
Phale, P.S.2
Durani, S.3
Wangikar, P.P.4
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