ChemCatChem

Cover image for Vol. 2 Issue 8

Special Issue: Biocatalysis

August 9, 2010

Volume 2, Issue 8

Pages 877–1015

  1. Cover Picture

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. Cover Picture: Regioselective Hydroformylation of Styrene Using Rhodium-Substituted Carbonic Anhydrase (ChemCatChem 8/2010) (page 877)

      Qing Jing and Romas J. Kazlauskas

      Article first published online: 30 JUL 2010 | DOI: 10.1002/cctc.201090032

      Thumbnail image of graphical abstract

      The cover picture shows rhodium-substituted carbonic anhydrase. In their Communication on page 953 ff., Jing and Kazlauskas demonstrate how, by replacing the zinc center in carbonic anhydrase with rhodium, an enzyme is created that catalyzes the hydroformylation of styrene. The active-site-bound rhodium favors formation of the linear hydroformylation product, whereas the unbound rhodium favors the branched product. This is just one example of the great recent strides made in biocatalysis, as highlighted in this Special Issue.

  2. Editorial

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. You have free access to this content
      Highlights in Biocatalysis (pages 879–880)

      Garabed Antranikian, Uwe T. Bornscheuer and Andreas Liese

      Article first published online: 22 JUL 2010 | DOI: 10.1002/cctc.201000228

  3. Graphical Abstract

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. Graphical Abstract: ChemCatChem 8/2010 (pages 881–885)

      Article first published online: 30 JUL 2010 | DOI: 10.1002/cctc.201090033

  4. News

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
  5. Reviews

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. Biocatalytic Reductions and Chemical Versatility of the Old Yellow Enzyme Family of Flavoprotein Oxidoreductases (pages 892–914)

      Helen S. Toogood, John M. Gardiner and Nigel S. Scrutton

      Article first published online: 28 JUN 2010 | DOI: 10.1002/cctc.201000094

      Thumbnail image of graphical abstract

      Flavo flav: We describe an overview of the biocatalytic potential of the old yellow family of flavoprotein oxidoreductases and illustrate the value of combining mechanistic and structural studies of biocatalysts to guide future exploitation of these enzymes in industrial biocatalysis.

    2. Artificial Metalloenzymes (pages 916–927)

      Fiora Rosati and Gerard Roelfes

      Article first published online: 8 APR 2010 | DOI: 10.1002/cctc.201000011

      Thumbnail image of graphical abstract

      The best of both worlds: Artificial metalloenzymes have emerged as a promising approach to merge the attractive properties of homogeneous and biocatalysis. In this Review, the design and optimization strategies and the catalytic scope of artificial metalloenzymes are discussed, with a particular focus on the role of the second coordination sphere.

  6. Minireview

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. Biocatalytic Production of Coenzyme A Analogues (pages 929–937)

      Erick Strauss, Marianne de Villiers and Ilse Rootman

      Article first published online: 21 JUL 2010 | DOI: 10.1002/cctc.201000139

      Thumbnail image of graphical abstract

      Enzymes and CoA: Coenzyme A (CoA) analogues have found widespread application in chemical biology, where their uses include the inhibition and study of CoA-dependent enzymes and the labeling of proteins, especially carrier protein modules. This Minireview provides an analysis of the CoA biosynthetic enzymes, an overview of their application in the production of CoA analogues, and a description of analogues that can be accessed by such methods.

  7. Highlight

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. Expanding the Application Range of Aldolases: Novel Asymmetric Syntheses of α-Methylated β-Hydroxy α-Amino Acids and β-Amino Alcohols (pages 939–942)

      Katrin Baer, Nina Dückers, Werner Hummel and Harald Gröger

      Article first published online: 16 JUN 2010 | DOI: 10.1002/cctc.201000007

      Thumbnail image of graphical abstract

      Broadened horizons: The application range of the long-known enzymatic enantio- and diastereoselective synthesis of β-hydroxy α-amino acids, a structural motif widely found in drug molecules and their intermediates, by means of an aldol reaction has recently been successfully expanded towards the asymmetric synthesis of α,α-disubstituted β-hydroxy α-amino acids and β-amino alcohols.

  8. Communications

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. Chemoenzymatic Combination of Glucose Oxidase with Titanium Silicalite-1 (pages 943–945)

      Peter N. R. Vennestrøm, Esben Taarning, Claus H. Christensen, Sven Pedersen, Jan-Dierk Grunwaldt and John M. Woodley

      Article first published online: 21 JUL 2010 | DOI: 10.1002/cctc.201000120

      Thumbnail image of graphical abstract

      Zeozymes: A proof-of-concept is presented for the chemoenzymatic combination of titanium silicalite-1 zeolite with glucose oxidase. In this combination, glucose is oxidized to gluconic acid and the H2O2 byproduct formed in situ is used for the simultaneous oxidation of chemical substrates. Both a soluble glucose oxidase and a truly integrated heterogeneous combination whereby the oxidase enzyme is anchored onto the zeolite surface are reported.

    2. Oxidoreductases Working Together: Concurrent Obtaining of Valuable Derivatives by Employing the PIKAT Method (pages 946–949)

      Fabricio R. Bisogno, Ana Rioz-Martínez, Cristina Rodríguez, Iván Lavandera, Gonzalo de Gonzalo, Daniel E. Torres Pazmiño, Marco W. Fraaije and Vicente Gotor

      Article first published online: 28 JUN 2010 | DOI: 10.1002/cctc.201000115

      Thumbnail image of graphical abstract

      Flying PIKATs: The stereoselective oxidation of several sulfides linked to the enantioselective oxidation of different sec-alcohols are combined in a parallel interconnected kinetic asymmetric transformation (PIKAT) fashion. Furthermore, the cofactor concentration employed in these processes is investigated, demonstrating a high capacity of performance, even at micromolar concentrations of the mediator.

    3. One-Step Lactosylation of Hydrophobic Alcohols by Nonaqueous Biocatalysis (pages 950–952)

      Yuri Okutani, Shizuka Egusa, Yukiko Ogawa, Takuya Kitaoka, Masahiro Goto and Hiroyuki Wariishi

      Article first published online: 29 APR 2010 | DOI: 10.1002/cctc.201000051

      Thumbnail image of graphical abstract

      SEE delights: Alkyllactosides are successfully synthesized in a one-step enzymatic reaction from lactose in its original form and hydrophobic alcohols, by using a surfactant-enveloped enzyme (SEE) in nonaqueous 1,3-dimethyl-2-imidazolizinone, which can dissolve both donor sugars and acceptors. Nonaqueous biocatalysis is highly advantageous for efficient enzymatic glycosylation by SEE-mediated dehydration reaction.

    4. Regioselective Hydroformylation of Styrene Using Rhodium-Substituted Carbonic Anhydrase (pages 953–957)

      Qing Jing and Romas J. Kazlauskas

      Article first published online: 15 JUL 2010 | DOI: 10.1002/cctc.201000159

      Thumbnail image of graphical abstract

      CA confidential: Replacing the active-site zinc in carbonic anhydrase (CA) by rhodium forms a new enzymatic catalyst for cofactor-free hydroformylation of styrene with syn gas. Unlike free rhodium, this rhodium–protein hybrid, [Rh]–CA, is regioselective (8.4:1) for linear over branched aldehyde product, which is a 40-fold change in regioselectivity compared to free rhodium.

    5. Directed Evolution of Enantioconvergency: The Case of an Epoxide Hydrolase-Catalyzed Reaction of a Racemic Epoxide (pages 958–961)

      Huabao Zheng, Daniel Kahakeaw, Juan Pablo Acevedo and Manfred T. Reetz

      Article first published online: 15 JUL 2010 | DOI: 10.1002/cctc.201000122

      Thumbnail image of graphical abstract

      Highly evolved: The Aspergillus niger epoxide hydrolase (ANEH) has been subjected to laboratory evolution with the creation of mutants that transform the racemic epoxide to a single stereoisomer with greater than 90 % conversion and 99 % enantiomeric excess.

    6. Rational Protein Design of Paenibacillus barcinonensis Esterase EstA for Kinetic Resolution of Tertiary Alcohols (pages 962–967)

      Arnau Bassegoda, Giang-Son Nguyen, Marlen Schmidt, Robert Kourist, Pilar Diaz and Uwe T. Bornscheuer

      Article first published online: 28 JUN 2010 | DOI: 10.1002/cctc.201000053

      Thumbnail image of graphical abstract

      Designs are all there: Structural alignment-based protein engineering yields esterase variants that enable high conversion and exhibit excellent enantioselectivity in the kinetic resolution of tertiary alcohol esters. Whereas the wild-type esterase EstA from Paenibacillus barcinonensis shows low activity and selectivity, several mutants show a significantly increased enantioselectivity.

  9. Full Papers

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. A pH-Based High-Throughput Screening of Sucrose-Utilizing Transglucosidases for the Development of Enzymatic Glucosylation Tools (pages 969–975)

      Elise Champion, Claire Moulis, Sandrine Morel, Laurence A. Mulard, Pierre Monsan, Magali Remaud-Siméon and Isabelle André

      Article first published online: 22 JUL 2010 | DOI: 10.1002/cctc.201000111

      Thumbnail image of graphical abstract

      Screen if you want to go faster: A high-throughput screening protocol relying on a pH-based assay has been developed to identify glucansucrase variants that retain their ability to utilize sucrose as a substrate. By using this procedure, 17 improved mutants for the glucosylation of a nonnatural acceptor (D-GlcpNAc) are identified from a library of 8000 amylosucrase variants.

    2. Reversed Enantiopreference of an ω-Transaminase by a Single-Point Mutation (pages 976–980)

      Maria Svedendahl, Cecilia Branneby, Lina Lindberg and Per Berglund

      Article first published online: 22 JUL 2010 | DOI: 10.1002/cctc.201000107

      Thumbnail image of graphical abstract

      Rational design of an (S)-selective ω-transaminase from Arthrobacter citreus variant CNB05-01 increased the enantioselectivity for 4-fluorophenylacetone. Additionally, a single-point mutation, V328A, reversed the enzyme enantiopreference for 4-fluorophenylacetone, which was found to be substrate dependent. The shift in enantiopreference was confirmed by molecular docking simulations.

    3. Asymmetric Retro-Henry Reaction Catalyzed by Hydroxynitrile Lyase from Hevea brasiliensis (pages 981–986)

      Ruslan Yuryev, Sebastian Briechle, Mandana Gruber-Khadjawi, Herfried Griengl and Andreas Liese

      Article first published online: 21 JUL 2010 | DOI: 10.1002/cctc.201000147

      Thumbnail image of graphical abstract

      Oh Henry! Hydroxynitrile lyase from Hevea brasiliensis is a promiscuous biocatalyst that catalyzes the asymmetric Henry reaction yielding (S)-β-nitroalcohols as well as its reverse reaction, leading to the production of (R)- enantiomers by means of resolution of racemic β-nitroalcohols. The biocatalytic retro-Henry reaction is studied using the cleavage of 2-nitro-1-phenylethanol as a model system.

    4. Ampicillin Synthesis Using a Two-Enzyme Cascade with Both α-Amino Ester Hydrolase and Penicillin G Acylase (pages 987–991)

      Janna K. Blum, Andria L. Deaguero, Carolina V. Perez and Andreas S. Bommarius

      Article first published online: 28 JUL 2010 | DOI: 10.1002/cctc.201000135

      Thumbnail image of graphical abstract

      Two enzymes in a cascade: α-Amino ester hydrolase (EC 3.1.1.43) and penicillin G acylase (EC 3.5.1.11) are employed together to perform a purely aqueous one-pot production of ampicillin directly from penicillin G resulting in a maximum of 47 % conversion to ampicillin. This works explores batch and staggered configurations for enzyme addition and variations in enzyme loadings.

    5. Plasma-Modified Polypropylene as Carrier for the Immobilization of Candida antarctica Lipase B and Pyrobaculum calidifontis Esterase (pages 992–996)

      Torge Vorhaben, Dominique Böttcher, Dagmar Jasinski, Ulf Menyes, Volker Brüser, Karsten Schröder and Uwe T. Bornscheuer

      Article first published online: 19 JUL 2010 | DOI: 10.1002/cctc.201000130

      Thumbnail image of graphical abstract

      Carrier opportunities: Treatment of the polypropylene-based carrier Accurel by an oxygen plasma turns this hydrophobic material into a carrier suitable for enzyme immobilization, which leads not only to higher immobilization yields and enhanced stability in recycling experiments, but also allows the use of the hydrolases in a nonaqueous reaction system.

    6. Thermostability Enhancement of Clostridium thermocellum Cellulosomal Endoglucanase Cel8A by a Single Glycine Substitution (pages 997–1003)

      Michael Anbar, Raphael Lamed and Edward A. Bayer

      Article first published online: 14 JUL 2010 | DOI: 10.1002/cctc.201000112

      Thumbnail image of graphical abstract

      Thermostable mutant enzymes: The X-ray crystal structure of the Clostridium thermocellum Cel8A cellulase depicts the amino acid substitutions which enable the protein to withstand elevated temperatures while maintaining wild-type levels of activity. The mutant enzyme may be used in combination with other selected glycoside hydrolases to efficiently degrade lignocellulosic materials used in the biofuel industry.

    7. Entrapping Flavin-Containing Monooxygenase on Corrugated Silica Nanospheres and their Recyclable Biocatalytic Activities (pages 1004–1010)

      Archana A. Biradar, Ankush V. Biradar and Tewodros Asefa

      Article first published online: 24 MAR 2010 | DOI: 10.1002/cctc.200900253

      Thumbnail image of graphical abstract

      Synthetic methods and biocatalytic activities of new classes of heterogeneous biocatalysts by immobilizing flavin-containing monooxygenase on corrugated and nanoporous silica nanospheres are reported. By using the structures of the etched silica nanospheres, effective immobilization of flavin-containing monooxygenase 1 (FMO1) is demonstrated. The FMO1 immobilized etched silica nanospheres have shown efficient and recyclable biocatalytic activity for nicotine oxidation.

  10. Preview

    1. Top of page
    2. Cover Picture
    3. Editorial
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireview
    8. Highlight
    9. Communications
    10. Full Papers
    11. Preview
    1. You have free access to this content
      Preview: ChemCatChem 9/2010 (page 1015)

      Article first published online: 30 JUL 2010 | DOI: 10.1002/cctc.201090031

SEARCH

SEARCH BY CITATION