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Stability and Stabilization of Biocatalysts - 1st Edition - ISBN: 9780444829702, 9780080541655

Stability and Stabilization of Biocatalysts, Volume 15

1st Edition

Authors: F.J. Plou J.L. Iborra P.J. Halling
Editor: A. Ballesteros
Hardcover ISBN: 9780444829702
eBook ISBN: 9780080541655
Imprint: Elsevier Science
Published Date: 10th November 1998
Page Count: 756
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Table of Contents

Preface. Acknowledgements. Inactivation Mechanisms and Reactors. Diagnosing the inactivating process of enzymes (O. Misset, A. van Dijk). Stability and stabilization of glucose-fructose oxidoreductase from Zymomonas mobilis against irreversible inactivation during substrate turnover in biochemical reactors (B. Nidetzky et al.). Reactor performance under thermal inactivation and temperature optimization with chitin-immobilized lactase (A. Illanes et al.). Fast in-situ-characterization of biocatalysts long-term stability (M. Boy et al.). Chemical and thermal stability of ferulic acid (feruloyl) esterases from Aspergillus (C.B. Faulds et al.). Stability properties of calf intestinal alkaline phosphatase (U. McKeon et al.). Stabilization of ß-glucanase and its effect on the substrate hydrolysis pattern (I. Markovic et al.). Some factors affecting the behavior of anhydrous &agr;-chymotrypsin at high temperature (D. Pirozzi, G. Greco Jr.). Horseradish peroxidase stability in the course of phenols oxidation (A.M. Egorov et al.). The effect of impurities of crude olive residue oil on the operational stability of the Candida rugosa lipase immobilized in polyurethane foams (A.C. Correia, S. Ferreira-Dias). Approaches for improved identification of mechanisms of enzyme inactivation (M. Polakovic et al.). Stability and stabilization of &agr;-1-4-D-glucan phosphorylases (R. Grießler et al.). Oxidation by hydrogen peroxide of D-amino acid oxidase from Rhodotorula gracilis (V. Obregón et al.). Cosolvent effect on the synthesis of ampicillin and cephalexin with penicillin acylase (C. Aguirre et al.). Conversion and stability studies on enzyme-membrane reactor with lipase immobilized by different methods (T. Venyige et al.). Study of the deactivation process of the glucose oxidase-catalase enzymatic system by means of simulation (L.E. Romero, D. Cantero). Stabilization by Chemical Modification. Stabilization of hydrolases by chemical modification with fatty acids or polyethylene glycol (F.J. Plou et al.). Modification of the carbohydrate moiety in ribonuclease B and its influence on the protein stability probed by limited proteolysis (U. Arnold, R. Ulbrich-Hofmann). Comparative studies on selective modification of &eegr;-amino groups in lipases and phospholipase A2 (B.C. Koops et al.). Analysis of the thermal deactivation kinetics of &agr;-chymotrypsin modified by chemoenzymatic glycosilation (M.A. Longo, D. Combes). Increasing the operational stability of flavoproteins by covalent cofactor binding (W.J.H. van Berkel et al.). Properties of PEG-modified microbial proteases. Activity and stability studies (T.M. Fatum et al.). The effect of crosslinking on thermal inactivation of cellulases (J. Bilen, U. Bakir). Studies of the stability of acid phosphatase (A. niger) by cross-linking with glutaraldehyde and soil humates (N. Ortega et al.). Non-Covalent Processes in Solution. Folding and association versus misfolding and aggregation proteins (R. Jaenicke). Activity of monoclonal antibodies in prevention of in vitro aggregation of their antigens (B. Solomon et al.). Stability of monodeamidated forms of ribonuclease A (F. Catanzano et al.). Pressure effects of protein oligomeric dissociation (C. Balny). Effect of high hydrostatic pressure on enzyme stability (D. Combes, V. Athès). Thermodynamic stability of a monomeric derivative of bovine seminal ribonuclease (G. Barone et al.). Thermodynamic stability of ribonuclease P2 sulfolobus solfataricus and some mutants (G. Graziano et al.). Stabilization of &agr;-chymotrypsin by DMSO (E. Flaschel, L. Ebmeier). Thermal stabilization by its ligands of NADP+-isocitrate dehydrogenase from the thermophilic cyanobacterium Phormidium laminosum (M.A. Pardo et al.). The characterization of protein stability from hydrogen exchange: maximum entropy analysis of co-solvent effects on exchange rates (B. Souhail et al.). Preferential hydration changes upon protein unfolding in water-cosolvent mixtures (H.O. Hammou et al.). Characterizing protein-cosolvent interactions coupled to protein refolding by kinetic calorimetry (M.C. Boulaich et al.). Characterizing cosolvent effects on protein stability: cold-denaturation of ubiquitin in the presence of guanidine (B. Ibarra Molero, J.M. Sánchez-Ruiz). Acetylcholinesterase-ethanol interactions: inactivation, substrate and ligand exclusion (F. Ortega et al.). Effect of a mixed stabilizer-denaturant system on the stability of enzyme activity at high temperatures: lysozyme as a model (Y. Sangeeta Devi et al.). A simple folding method for high level production of the hydrophobic disulfide bonded hepatitis B X protein by inclusion body route and its structural analysis (I. Marczinovits et al.). Protein Engineering and Thermophile Enzymes. Rigidity of thermophilic enzymes (A. Fontana et al.). Improvement of thermal stability of a diagnostic enzyme, Streptomyces cholesterol oxidase, by random and site-directed mutageneses and a structural interpretation (Y. Murooka et al.). Protein engineering for thermostabilisation of proteins: some theoretical rules and application to a ß-glucanase (E. Querol et al.). Mechanism of stabilization of the ß-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus (M. Moracci et al.). A strategy for engineering thermostability: the case of cyclodextrin glycosyltransferase (J. Uitdehaag, B.W. Dijkstra). Thermophilic esterases and the amino acid "traffic rule" in the hormone sensitive lipase subfamily (G. Manco et al.). Cloning and stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagensis (H. Slusarczyk et al.). Usefulness of bacterial thermostable enzymes in clinical chemical analysis (K. Tomita et al.). Effect of temperature and Ca2+ on the degree of multiple attack exhibited by mesophilic and thermophilic &agr;-amylases (A. Kramhøft, B. Svensson). Degradation and denaturation of stable enzymes (D. Thompson et al.). Non-conventional Media. Engineering stability of enzymes in systems with organic solvents (V.V. Mozhaev). Inactivation of enzymes at the aqueous-organic interface (P.J. Haling et al.). Exploiting hysteresis for high activity enzymes in organic media (J. Partridge et al.). Limited proteolysis of proteins by thermolysin in aqueous trifluorethanol (P. Polverino et al.). Enzyme inactivation by inert gas bubbling (M. Caussette et al.). Effects of water-miscible solvents on the stability and specificity of cyclodextringlucosyltransferases (A.D. Blackwood, C. Bucke). Stabilization of immobilized enzymes against organic solvents: complete hydrophilization of enzymes environments by solid-phase chemistry with poly-functional macromolecules (R. Fernández-Lafuente et al.). Effect of sorbitol on immobilized &agr;-chymotrypsin thermostability in low-water systems (T. de Diego, P. Lozano, M.J. Ñíguez, J.L. Iborra). Stability of immolilized enzyme-polyelectrolyte complex agains irreversible inactivation by organic solvents (V. Levitzky et al.). Enhancement of invertase activity in organic media for oligosaccharide synthesis (S. Bielecki, R.I. Somiari). Effects of crown ethers on the activity of enzymes in peptide formation in organic media (D.J. van Unen et al.). Recovery of the activity of an immobilized lipase after its use in fat transesterification (S. Ferreira-Dias et al.). Effects of lipid-borne compounds on the activity and stability of lipases in microaqueous systems for lipase-catalyzed interesterification (X. Xu et al.). Stabilisation of lipases for activity in ammoniolysis (F. van Rantwijk et al.). Water sorption isotherm as a tool to explore hydration of the microenvironment of biocatalysts (J.M. Sanchez-Montero et al.). Thermal stability of free and immobilised Pseudomonas cepacia lipase in aqueous and organic media (G. Pencreac'h, J.C. Baratti). The stabilization of enzyme in organic solvent at low temperature (H.J. Lee et al.). A comparative study of thermal inactivation of enzymes in supercritical carbon dioxide (A. Gießauf et al.). Studies of the stability of aminoacylase in some organic solvents (L. Boross et al.). Cutinase activity and enantioselectivity in supercritical fluids (N. Fontes et al.). Effect of pressure on enzyme activity in compressed gases (M.C. Almeida et al.). Immobilized Enzymes. Activity and structural stability of adsorbed enzymes (W. Norde, T. Zoungrana). Covalent immobilization of glucose oxidase on A1PO4 as inorganic support (F.M. Bautista et al.). The effect of site-specific immobilization on the thermal stability of thermolysin-like neutral proteases (J. Mansfeld et al.). Immobilization of hydantoin cleaving enzymes from Arthrobacter aurescens DSM 3747 - Effect of the coupling method on the stability of the L-N-carbamoylase (M. Pietzsch et al.). Thermoinactivation of ß-xylosidase immobilized on nylon (M.J. Dueñas, P. Estrada). Increase of thermal stability of tannin acyl hydrolase by covalent immobilization through its carbohydrate side chain. Application in tea cream solubilisation (P. Nicholas et al.). Stability in presence of organic solvents of dextransucrase from Leuconostoc mesenteroides NRRL B-512F immobilized in calcium-alginate beads (M. Alcalde et al.). Immobilisation and characteristics of glucose oxidase immobilised on Convective Interaction Media (CIM) disks (A. Podgornik et al.). Immobilization of spinach leaf hydroperoxide lyase (L.M. Simon et al.). A new immobilization system for Candida rugosa lipase: characterization and applications (K. Carbone, M. Casarci). Soybean lipoxygenases: purification and stability of the free and immobilized enzymes (A. Chikere et al.). Stabilization of lipase B from Candida antartica by immobilization on different supports (M. Arroyo et al.). Covalent immobilization of crude and partially-purified lipases onto inorganic supports: stability and hyperactivation (A.R. Alcántara et al.). Immobilization of alkaline phosphatases on various supports (B. Surinenaite et al.). Stabilization of serine proteinases by immobilization (V. Bendikiene, B. Juodka). Whole Cells. Immobilized cells: plasmid stability and plasmid transfer (J.M. Barbotin et al.). Stabilization of immobilised cells systems using a modified metal surface, fructose polymer levan and high cell concentration (M. Bekers et al.). Plasmid stability in recombinant Saccharomyces cerevisiae expressing the EXG1 gene in free immobilized cultures (A. Guillán et al.). Bioreductions by Pyrococcus furiosus at elevated temperatures (E. van den Ban et al.). Stability of free and immobilized Mycobacterium sp. cells in aqueous and organic media (P. Fernandes et al.). Operational stability of immobilized C. reinhardtii cells: an approach to its potential as biocatalyst for N-consuming processes (I. Garbayo, C. Vílchez). Induction and stability of cholesterol oxidase from cells of a Rhodococcus (J. Kreit, P. Germain). Stability of functionally active fusion proteins during their biosynthesis and isolation from expressing bacterial cells (L.M. Vinokurov et al.). Miscellaneous. Production of bio-esters by immobilized lipases (K. Bélafi-Bakó et al.). An aspergillus flavus strain promoting oleic acid esterification in isooctane (V. Loscos et al.). Covalent enzyme immobilization in different porous polymer membranes (H.-G. Hicke et al.). Functionalised cross-linked polyvinyl alcohol as new matrix for lipase immobilization (E. Cernia et al.). Enzymatic biphasic membrane reactors for the synthesis of chiral products (H.A. Sousa, J.P.S.G. Crespo). Coinmobilization of enzymes and cells on chitosan and derivatives (A. Heras et al.). Parameters affecting the activity of Mucor miehei esterase 30 000 in a solvent free-system (M. Karra-Chaabouni et al.). Recombinant antigens by fusion of antigenic epitopes to a GST partner (J. Molnár et al.). Modification of metal substrates and its application to the study of redox proteins (T. Pineda et al.). Influence of some inducers on ligninolytic enzymes from corncop cultures of Phanerochaete chrysosporium in semi-solid-state conditions (S. Rodríguez Couto et al.). NMR study of hydration of liquid phase during lipase catalysed esterification in non aqueous media (C. Sarazin et al.). &agr;-chymotrypsin-catalysed synthesis of N-acetyl-L-tyrosine esters in organic media (K. László, L.M. Simon). Purification and characterization of penicillin V acylase from Streptomyces lavendulae (R. Torres et al.). Studies on the regioselective acylation of sugars catalyzed by lipase in tert-butanol (V. Sereti et al.). Activity of cardosin A and B in the presence of organic solvents (A.C. Sarmento et al.). Effect of fermentation conditions in the enzyme activity and steroselectivity of crude lipase from Candida rugosa (R.M. de la Casa et al.). Biotransformations catalyzed by Candida rugosa lipase partially purified by precipitation and by organic solvents treatment (S. Chamorro et al.). Effect of pH and temperature on immobilised Thiobacillus ferrooxidans cells over nickel alloy fibre (J.M. Gómez, D. Cantero). Index of authors.


Six years after the symposium on Stability and Stabilization of Enzymes, a second symposium, Stability and Stabilization of Biocatalysts, on which this book is based, was organized. At the symposium, 210 participants representing all continents came together to learn from 150 oral and poster communications.

The volume brings up-to-date the work already going on, and identifies possible breakthroughs in the research. This timely book therefore presents cutting edge developments in topics such as non-covalent processes in solution, protein engineering and thermophile enzymes, immobilized enzymes, non-conventional media, and whole cells.
An excellent addition to the available literature, it will make a useful contribution to this key area of applied biocatalysis.


No. of pages:
© Elsevier Science 1998
10th November 1998
Elsevier Science
Hardcover ISBN:
eBook ISBN:


@qu:...The book will be a valuable reference texts for all chemist and biochemist working in biotechnology and industrial microbiology. @source:Aslib Book Guide

Ratings and Reviews

About the Authors

F.J. Plou

Affiliations and Expertise

Department of Biocatalysis, CSIC Institute of Catalysis, Campus University Autonoma, 28049 Madrid, Spain

J.L. Iborra

Affiliations and Expertise

Department of Biochemistry and Molecular Biology "B", Faculty of Chemistry, University of Murcia, Spain

P.J. Halling

Affiliations and Expertise

Department of Pure & Applied Chemistry, University of Strathclyde, Glasgow, UK

About the Editor

A. Ballesteros