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Function and biotechnology of extremophilic enzymes in low water activity

Ram Karan, Melinda D Capes, Shiladitya DasSarma

Aquatic Biosystems · 2012 · Review

doi:10.1186/2046-9063-8-4

Abstract

Enzymes from extremophilic microorganisms usually catalyze chemical reactions in non-standard conditions. Such conditions promote aggregation, precipitation, and denaturation, reducing the activity of most non-extremophilic enzymes, frequently due to the absence of sufficient hydration. Some extremophilic enzymes maintain a tight hydration shell and remain active in solution even when liquid water is limiting, e.g. in the presence of high ionic concentrations, or at cold temperature when water is close to the freezing point. Extremophilic enzymes are able to compete for hydration via alterations especially to their surface through greater surface charges and increased molecular motion. These properties have enabled some extremophilic enzymes to function in the presence of non-aqueous organic solvents, with potential for design of useful catalysts. In this review, we summarize the current state of knowledge of extremophilic enzymes functioning in high salinity and cold temperatures, focusing on their strategy for function at low water activity. We discuss how the understanding of extremophilic enzyme function is leading to the design of a new generation of enzyme catalysts and their applications to biotechnology.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 25, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

Enzymes are nature's biocatalysts endowed with high catalytic power, remarkable substrate specificity, and ability to work under mild reaction conditions. These unique features led to enzyme applications in competitive bioprocesses as one of the foremost areas of biotechnology research. Most enzymes are active within a defined set of standard conditions close to what is considered normal for mesophilic terrestrial organisms. However, much of the biosphere is extreme by comparison (e.g. cold oceans and dry, salty deserts). Not surprisingly, the biosphere contains a very large number of extremophilic microorganisms with enzymes capable of functioning in unusual conditions.

The discovery of thermostable DNA polymerases and their impact on research, medicine, and industry has underscored the potential benefits of enzymes from extreme environments. Since that time, the biotechnological and industrial demand for stable enzymes functioning in harsh operational conditions has surged. A great deal of current effort is aimed at screening for new sources of novel enzymes capable of functioning in extreme conditions. The parallel development of sophisticated molecular biology tools has also enabled engineering of enzymes with novel properties using techniques such as site-directed mutagenesis, gene shuffling, directed evolution, chemical modifications and immobilization.

Microorganisms which grow in extreme conditions have been an important source of stable and valuable enzymes. Their enzymes, sometimes called "extremozymes", perform the same enzymatic functions as their non-extreme counterparts, but they can catalyze such reactions in conditions which inhibit or denature the less extreme forms. Interestingly, some of the enzymes derived from extremophiles display polyextremophilicity, i.e. stability and activity in more than one extreme condition, including high salt, alkaline pH, low temperature, and non-aqueous medium. A basic understanding of the stability and function of extremozymes under extreme conditions is important for innovations in biotechnology.

One of the underlying reasons for limited enzyme activity in extreme conditions is their effects on water structure and dynamics. When water activity is perturbed by extreme temperatures, high salinity, or other extreme conditions, normally structured liquid water may become limiting to enzymes, with deleterious consequences to enzyme structure and/or function. For example, at high salinity, water is sequestered in hydrated ionic structures, limiting the availability of free water molecules for protein hydration. An analogous effect is felt by enzymes in cold temperatures due to the freezing of water molecules, forming structured ice-like lattices that are less available to interact with proteins. Therefore, improved hydration characteristics in some extremozymes are critical for their function in their natural conditions. An interesting and potentially useful consequence of the hydration properties of such enzymes may be in extending their range of function to non-aqueous environments. Enzymes capable of functioning in the presence of organic solvents may permit their use in some specialized applications, such as for catalysis of reactions using novel substrates. As a result, a better understanding of molecular mechanisms used by such extremozymes for improved solubility and hydration is of substantial biotechnological interest.

Salt adapted enzymes

Water molecules are known to play a critical role in biological functions of proteins by binding to the surface and incorporating into the interior of protein molecules. Water has a tendency to form ordered cages around hydrophobic groups on the protein surface. Salt ions are known to disrupt the local water structure, diminishing the number of intermolecular hydrogen bonds. High salt concentrations critically affect the solubility, binding, stability, and crystallization of proteins. The interactions between proteins and protein subunits in solution are also altered by salts. The electrostatic interactions between charged amino acids are also perturbed with significant consequences for protein structure and function. The effects depend on the chemical nature of the salts, generally following the position of ions in the Hofmeister series.

Water is necessary for native structure, proper function, and to prevent aggregation of proteins. As salt ions inside the cell increases, water is removed from hydrophobic regions of protein surfaces, until proteins are no longer sufficiently hydrated (Figure 1). Non-halophilic proteins are generally less able to compete with salts and lose their structure and activity at relatively lower ionic concentration. However, halophilic proteins are able to successfully compete with salt ions for hydration and maintain their functional conformation in the presence of high ionic concentration (Table 1). This is especially true for proteins from halophilic microorganisms which use the salt-in mechanism for osmotic stabilization (e.g. halophilic archaea and some halophilic bacteria). Such halophilic proteins have evolved a specific set of molecular features that help them to compete with ions for water and maintain a stable hydration shell. In fact, in comparison to non-halophilic enzymes, halophilic enzymes are found to have multilayered hydration shells that are of considerably greater size and order (Figure 1).

In order to enhance activity in high salt concentrations, an increase in the number of charged amino acids, especially acidic residues at the protein surface, is observed in halophilic proteins (Figure 2). Bioinformatic studies of the extreme halophile Halobacterium sp. NRC-1 and other species have shown that an increase in the number of acidic (glutamic acid, and to a lesser extent, aspartic acid) over basic residues is a general property of proteins predicted from the genomes of halophilic microorganisms (Figure 2). Glutamate residues have superior water binding capacity over all other amino acids and are generally found in excess on the surface of halophilic proteins. Acidic amino acids can constitute a high fraction of an individual protein, with up to 20-23% having been reported. The negatively charged amino acids in halophilic proteins bind hydrated cations and help maintain a surface hydration layer, reducing their surface hydrophobicity, and contributing to mutual electrostatic repulsion. These properties prevent aggregation at high salt concentrations.

X-ray and neutron diffraction structures have confirmed that the high content of acidic residues play significant roles in binding of essential water molecules and salt ions, preventing protein aggregation and providing flexibility to protein structure through electrostatic repulsion (Figure 3). For example, the structure of malate dehydrogenase from the extremely halophilic archaeaon Haloarcula marismortui received considerable attention from Mevarech and co-workers and the group of Zaccai. The presence of clusters of acidic residues has been observed in the crystal structure of dihydrofolate reductase (DHFR) and proliferating cell nuclear antigen (PCNA) from the extremely halophilic archaeaon Haloferax volcanii. Crystal structure of the glucose dehydrogenase of the extremely halophilic archaeaon H. mediterranei has also contributed much information about halophilic adaptation and concluded that the surface of enzyme was predominantly acidic in nature and contributed to the halophilic characters of the enzyme. In another study, Tadeo et al. reported that by altering the amino acid composition at the protein surface, it is possible to modify the salt dependence of proteins and interconvert salt tolerant and non-tolerant proteins. Through the analysis of a large number of mutants, they concluded that the effect of salt on protein stability is largely independent of the total protein charge. In a recent study, a model of the recombinant esterase from H. marismortui, cloned and overexpressed in Escherichia coli, confirmed the enrichment of acidic residues and showed a high negative potential from clusters of aspartate and glutamate residues, with most acidic residues confined on the surface.

An interesting finding also apparent from the genome-wide bioinformatic analysis of predicted proteins was the deficit of protein surface lysine residues in halophilic proteins. This observation is consistent with the reduction in hydrophobic surfaces in halophilic proteins, resulting in increased hydration at the protein surface. This prediction was confirmed directly via the structure of glucose dehydrogenase from the extreme halophile H. mediterranei solved by Britton et al., where lysine residues on the enzyme surface have their side chains buried and better ordered than those from non-halophiles (Figure 3). In halophilic proteins, lysine residues are often replaced by arginines, likely due to the greater hydrophilicity of the guanidinyl side chain, with a substantial role in maintaining the active protein structure.

Halophilic proteins have also been found to contain a low content of bulky hydrophobic side chains on their surface, compared to non-halophilic proteins. The number of larger hydrophobic amino acid residues (phenylalanine, isoleucine, and leucine) is reduced compared to small (glycine and alanine) and borderline hydrophobic (serine and threonine) amino acid residues. These findings are also consistent with increased flexibility, increased surface hydration, and reduced surface hydrophobicity of halophilic proteins.

In halophilic proteins, oppositely charged neighboring residues often interact to form salt bridges and these salt bridges play significant roles in protein folding, structure, and oligomerization (Figure 3). For example, the crystal structure of malate dehydrogenase from H. marismortui showed an increase in the number of salt bridges compared with the non-halophilic homologs, which enhanced enzyme stability at high salt concentrations. This enzyme exists as a tetramer at high salt concentrations and dissociates into monomers as the salinity is reduced. Similarly Madern et al. have shown that isocitrate dehydrogenase from the halophilic archaeon H. volcanii exists as a dimer at high salt concentration but at low salt concentration it is irreversibly deactivated, due to dissociation of the dimer towards an inactive, partially folded monomeric species. Halobacterium sp. ferredoxin studied using CD and fluorescence techniques showed that the increase in salt concentration decreased electrostatic repulsion by ion binding, likely stabilizing oligomerization necessary for catalytic activity.

High salt concentrations generally enhance native conformation and functionality in halophilic proteins. Salt concentrations may significantly affect the folding, conformation, subunit structure, and kinetics of halophilic proteins. Withdrawal of salt generally results in the gradual loss of protein structure and unfolding of halophilic proteins. Okamoto et al. studied the role of salt on the kinetics of a high salt-active extracellular protease from the moderately halophilic bacterium Halobacillus sp. with fluorescence resonance energy transfer (FRET) and found that NaCl and other kosmotropic salts have a positive effect on catalytic activity of the enzyme. Their results suggested that these salts are excluded from the solvation shell of proteins because they have higher affinity for water than for the protein surface. Using far-ultraviolet circular dichroism (farUV-CD), Müller-Santos et al. showed that in salt-free medium, an esterase from H. marismortui was completely unfolded and secondary structures appeared only in the presence of high concentrations of salt. The salt-dependent activity profiles of nucleoside diphosphate kinases from extremely halophilic archaea Haloarcula quadrata and H. sinaiiensis, have also been studied by farUV-CD spectroscopy, with salt-dependent oligomerization observed only for the latter. Srimathi et al. investigated a cold adapted amylase from the psychrophile Pseudoalteromonas haloplanktis by CD and fluorescence techniques. This cold-active amylase showed increased activity and improved folding at higher concentrations of salt similar to halophilic enzymes, indicating similar mechanisms of enhanced activity in both high salt and low temperature conditions.

Salt is also known to play a critical role in protein-DNA interactions. O'Brien et al. studied the effect of salt on the thermodynamic-structural relationship of the binding of TATA box-binding protein (TBP) from Pyrococcus woesei, a moderately halophilic and hyperthermophilic organism, to its DNA binding site. This group hypothesized that uptake of cations and discharge of water accompanies protein-DNA complex formation. Subsequently Bergqvist et al. used site-directed mutagenesis to change cation binding sites, i.e. negatively charged, acidic glutamate residues on the protein surface. Consistent with the hypothesis, they found that some of the mutants were able to convert the halophilic, relatively salt insensitive TBP into non-halophilic, salt sensitive variants.

While the underlying molecular mechanisms of halophilic protein function are still not fully understood, available studies have begun to shed considerable light on their strategies for adaptation to high salinity and relatively low water activity. Based on the many available studies, clustered surface negative charges, decreased hydrophobicity at the surface of the protein, and enrichment of salt bridges appear to be general strategies for improving the function of halophilic proteins in high salt, low water conditions. However, these mechanisms may not be universal, and additional research will continue to provide further insights into their function and activity. It is clear, however, that enzymes isolated from halophiles possess extraordinary structural and catalytic properties that allow function at low water activity. These exceptional biomolecules have great potential for applications to many biotechnological and industrial processes (Table 2).

Cold active enzymes

Like high salinity, cold temperatures also critically affect the properties and structures of enzymes as well as the surrounding water. Cold temperatures affect the dynamic activity of bulk water as well as the spheres of hydration surrounding the protein surface. Since water acts as a lubricant, easing the essential peptide amide-carbonyl hydrogen bonding dynamic, the effects of water are highly dependent on the temperature. Dependence of the strength of aqueous hydrogen bonds on temperature is neither linear nor monotonic but unimodal, with the maximum density for pure water at approximately 4°C. Broken hydrogen bonds are found in high-density water while strong networks of hydrogen bonds are found in low-density water. Deficiency or disturbance of hydrogen bonds and water networks around the protein may be linked to the loss of biological activity and protein denaturation at low temperatures.

As temperature decreases, the water molecules surrounding the protein surface become more ordered and thereby less associated with the protein, eventually pushing the system equilibrium toward the unfolded or denatured state. This change in protein structure is driven by an increase in hydration energies of non-polar groups at lower temperature. The hydration energies of cold-active enzymes are generally less affected by lower temperature, and their lower inherent surface hydrophobicity is less sensitive than mesophilic proteins, keeping their structures more intact. In effect, cold active proteins are able to hold on more tightly to the available water, similar to salt adapted proteins.

Temperature and viscosity of the medium are inversely related, with viscosity halved when the temperature is reduced from 37°C to 0°C. Low temperatures therefore reduce the speed of reactions at least in part due to the strong effect of temperature on viscosity of the medium. Based on biophysical considerations, reaction rates are predicted to decrease 2-3 fold for every 10°C decrease in temperature, according to the Arrhenius equation. As a result, the effect of reduced temperature on enzyme activity is very significant, and the design of cold-active enzymes must have some structural adaptations to maintain the level of 'breathing' necessary for catalysis.

Studies of cold active enzymes have suggested that both an increase in interactions with the solvent and an increase in structural flexibility contribute to maintaining catalytic activity at lower temperatures (Table 1). Aurilia et al. used Fourier transform infrared spectroscopy (FTIR) and molecular dynamics simulations to investigate a cold active esterase from P. haloplanktis and found that the flexibility of the protein loop near the active site plays a crucial role in its function. An α-amylase from the same organism was investigated by D'Amico et al. and shown using differential scanning calorimetry and fluorescence spectroscopy to have high conformational flexibility and electrostatic potential at the protein surface, which lowers activation energy for hydrolysis. The temperature dependence of alkaline phosphatase from the Antarctic strain TAB5 was studied by selection of thermostable and thermolabile variants. The study showed that cold activity is sensitive to slight changes in the protein sequence, particularly in residues located within or close to the active site of the enzyme.

There are relatively few solved three-dimensional structures of cold-active proteins compared to mesophilic or thermophilic proteins. While overall structures of cold adapted proteins are generally almost identical to mesophilic and thermophilic homologs, variations that are observed confirm an overall increase in protein flexibility and solvent interactions. For example, the crystal structures of cold active superoxide dismutase from P. haloplanktis and Aliivibrio salmonicida were compared with the mesophilic homolog from E. coli. Both cold-active superoxide dismutases showed an increased flexibility of the active site residues with respect to their mesophilic homologue. Bae and Phillips compared the crystal structures of adenylate kinases from the psychrophile B. globisporus and the mesophile B. subtilis with the thermophilic B. stearothermophilus enzyme. They concluded that the maintenance of proper flexibility is critical for the cold active proteins to function at their environmental temperatures. Similarly the crystal structure of Alteromonas haloplanctis α-amylase and Pseudomonas fluorescens β-lactamase showed a decrease in the number of hydrogen-bonds favoring more flexibility in these cold-active enzymes. The crystal structure of a cold active malate dehydrogenase from Aquaspirillium arcticum showed similar features to be responsible for cold activity, including an increased flexibility around the active site region, more favorable surface charge distribution for substrate and cofactor interactions, and reduced intersubunit ion pair interactions.

A bioinformatic study of amino acid contacts that differ between proteins adapted to different temperatures, which included nearly 400 psychrophilic proteins, found that interactions with the solvent at the protein surface play an important role in temperature adaptation. Additional bioinformatic and experimental studies have also suggested that the temperature-dependent activity of cold active enzymes may be altered by changing the amino acid composition, especially the overall protein charge, decreasing the hydrophobicity in the core of the enzyme, or decreasing the number of hydrogen bonds, salt bridges, or bound ions at the surface.

Amino acids present on the protein surface of cold active enzymes have been shown to play critical roles in both activity in cold and in high salinity, with increased activity and improved folding at higher concentrations of salt. Moreover, the crystal structure of a cold-active iron superoxide dismutase from the A. salmonicida also showed an increase in the net negative charge on the surface of cold-active iron superoxide dismutase. These findings and others suggest that solvent interactions of cold active enzymes display remarkable similarity to salt adapted enzymes.

While the adaptive mechanisms of cold active proteins are still under investigation, the best understood mechanisms include increased conformational flexibility at the expense of stability and enhanced interactions with the solvent. To increase flexibility, many structural modifications and the disappearance of discrete stabilizing interactions (electrostatic interactions and an improved interaction of surface side chains with the solvent) have been observed. While nearly all cold active enzymes studied to date have shown these tendencies, there are examples of unusual enzymes, e.g. enzymes displaying rapid kinetics, which display temperature independent characteristics. Triosephosphate isomerase from Vibrio marinus is an example of a temperature independent enzyme. The number of cold active proteins studied is expanding and additional future research including comparisons with closely related mesophilic homologs will provide further insights into enzymology at low temperature. The novel properties of cold active enzymes are likely to be valuable for a variety of applications in biotechnology and industry.

Enzyme function in organic solvents

One of the most useful outcomes of a better understanding of enzyme-solvent interactions is the potential engineering of new and more effective catalysts functioning in non-aqueous environments. Such enzymes may be useful for both biofuel and bioenergy applications, where large quantity of ethanol or other organic solvents are produced, and for synthetic chemistry, especially when catalysis of desired chemical reactions requires the presence of organic solvents. Organic solvents in the reaction mixture increase the solubility of hydrophobic substrates, and have the potential to improve the kinetic equilibrium and increase the yield and specificity of the product. However, limiting the disruption of molecular interactions in enzymes by organic solvents and the concomitant loss of activity remains a significant challenge.

A main factor responsible for loss of enzyme activity in organic solvents is the loss of crucial water molecules. The low water content restrains protein conformation mobility and affects Km and Vmax values. This rigidity increases resistance to thermal vibrations and reduces the enzyme-substrate interactions, leading to a reduced catalytic rate. Loss of water can also disrupt hydrogen bond formation between protein subunits on the exterior surface and active site interactions in the interior of proteins may be weakened. The presence of organic solvents can cause disruption of the forces important to the hydrophobic core due to the increased hydrophobicity of the medium. Low water activity may limit diffusion of substrates and stabilize the ground state of the enzyme or change the enzyme conformation altogether. Enzymes in non-aqueous systems can be active provided that the enzyme surface and the active site region are well hydrated.

The polarity of organic solvents is the most important factor in the balance between stabilization and inactivation of enzymes. Co-solvents systems (water plus water-miscible organic solvents), organic aqueous biphasic systems (water plus water-immiscible organic solvents), nearly anhydrous systems, and reverse micelles may be the result of addition of organic solvents with water. The relative proportion of organic solvent and water depends on the miscibility of the components. Highly polar, miscible organic solvents may strip the hydration layer from the enzyme surface, affecting enzyme flexibility and catalytic activity. Hydrophobic solvents, in contrast, may form a two-phase non-homogeneous system, leaving the hydration shell of the protein intact. However, they may sequester substrate away from the enzyme, depending on solubility and partitioning between phases. For improved activity in two-phase systems, a microenvironment or surface where favorable conditions (high enzyme activity, high substrate concentration, and low product solubility) driving high reaction rates may be desirable.

Published studies of the mechanism of adaptation of enzymes to function in organic solvent are relatively few. Ogino et al. investigated the mechanism of organic solvent tolerance in a Pseudomonas aeruginosa PST-01 protease by site-directed and random mutagenesis. They reported that the disulfide bonds and amino acid residues located on the surface of the molecule play important roles in organic solvent stability of the enzymes. The structural analysis of organic solvent effects on a protease from a similar P. aeruginosa strain also identified two disulfide bonds as well as a number of hydrophobic clusters at the protein surface. These hydrophobic patches and disulfide bonds were proposed to be responsible for the solvent-stable nature of the enzyme. Recently, Karabec et al. solved the crystal structure of alcohol dehydrogenase from Rhodococcus ruber DSM 44541 and suggested that salt-bridges play a significance role in the stability of this enzyme in non-aqueous media.

Organic solvent mediated enzymatic reactions have many advantages over aqueous enzymatic reactions: (i) increased solubility of apolar substrate and alteration in substrate specificity, (ii) enhanced regio-and stereo-selectivity, (iii) absence of racemization, (iv) lack of requirement of side chain protection, (v) reduced water activity altering the hydrolytic equilibrium, (vi) elimination of microbial contamination, and (vii) suppression of unwanted water-dependent side reactions. Additionally, enzymes in organic solvents tend to be more rigid than in water (due to increased electrostatic and hydrogen bonding interactions among the surface residues of enzyme) and provide the possibility of techniques such as molecular imprinting. In molecular imprinting, the enzyme solution is freeze-dried with a ligand ("imprinter") that locks the enzymes into a catalysis favorable condition during lyophilization and enhances the enzyme activity in organic solvents. In some cases, it has been found that molecular imprinting increases enzyme activity in organic solvents when co-lyophilized with an inorganic salt such as KCl. KCl prevents the reversible denaturation of proteins and produces a strong additive activation effect during the drying process. Among the disadvantages of non-aqueous organic enzyme catalysis, the loss of catalytic activity is the most common. Many enzymatic reactions are also susceptible to substrate and/or product inhibition, and expensive natural cofactors for enzyme activity may be required for full activity. Finally, labor and cost-intensive preparation of biocatalysts and enzymes may require narrow operation parameters, limiting the value of some enzymes that may be active in the presence of organic solvents. However, the potential for organic solvent mediated enzyme catalysis to enable desirable biotechnological aims remains a major motivating factor for additional research.

Conclusion

Extremophilic salt adapted and cold active enzymes have expanded our understanding of enzyme stability and activity mechanisms, protein structure-function relationships, and enzyme engineering and evolution. The still emerging understanding of protein-solvent interactions are likely to aid in development of new catalysts for use in novel synthetic applications, including enzymes operating in low water activity and organic solvents, and in the development of efficient catalytic systems active in organic solvents for applications in bioenergy and biotechnology.

Competing interests

The authors declare that they have no competing interests.

Authors' contributions

The manuscript was drafted by RK and revised and finalized together with MDC and SD. All authors have read and approved the final manuscript.

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    Georlette D Blaise V Collins T D'Amico S Gratia E Hoyoux A Marx JC Sonan G Feller G Gerday C Some like it cold: biocatalysis at low temperaturesFEMS Microbiol Rev2004 282542

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    Somero GN Temperature as a selective factor in protein evolution: The adaptational strategy of "compro-mise"J exp Zool1975 194175188

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    Koutsioulis D Wang E Tzanodaskalaki M Nikiforaki D Deli A Feller G Heikinheimo P Bouriotis V Directed evolution on the cold adapted properties of TAB5 alkaline phosphataseProtein Eng Des Sel2008 21319327

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    Bae E Phillips GN Jr Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinasesJ Biol Chem2004 272820228208

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    Aghajari N Feller G Gerday C Haser R Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular levelStructure1998 615031516

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    Michaux C Massant J Kerff F Frère JM Docquier JD Vandenberghe I Samyn B Pierrard A Feller G Charlier P Van Beeumen J Wouters J Crystal structure of a cold-adapted class C beta-lactamaseFEBS J2008 816871697

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    Zartler ER Jenney FE Jr Terrell M Eidsness MK Adams MW Prestegard JH Structural basis for thermostability in aporubredoxins from Pyrococcus furiosus and Clostridium pasteurianumBiochemistry2001 4072797290

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    Davail S Feller G Narinx E Gerday C Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41J Biol Chem1994 261744817453

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    Feller G Zekhnini Z Lamotte-Brasseur J Gerday C Enzymes from cold-adapted microorganisms. The class C beta-lactamase from the antarctic psychrophile Psychrobacter immobilis A5Eur J Biochem1997 1186191

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    Russell RJ Gerike U Danson MJ Hough DW Taylor GL Structural adaptations of the cold-active citrate synthase from an Antarctic bacteriumStructure1998 3351361

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    Feller G D'Amico D Gerday C Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctisBiochemistry1999 1446134619

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  98. 98.

    Alvarez M Zeelen JP Mainfroid V Rentier-Delrue F Martial JA Wyns L Wierenga RK Maes D Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus kinetic and structural propertiesJ Biol Chem1998 2732199206

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    Fjerbaek L Christensen KV Norddahl B A review of the current state of biodiesel production using enzymatic transesterificationBiotechnol Bioeng2009 512981315

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  102. 102.

    Lee DH Kim JM Shin HY Kang SW Kim SW Biodiesel production using a mixture of immobilized Rhizopus oryzae and Candida rugosa lipasesBiotechnol Bioprocess Eng2006 6522525

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  103. 103.

    Lee JH Kim SB Kang SW Song YS Park C Han SO Kim SW Biodiesel production by a mixture of Candida rugosa and Rhizopus oryzae lipases using a supercritical carbon dioxide processBioresour Technol2011 221052108

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    Deng L Xu XB Haraldsson GG Tan TW Wang F Enzymatic production of alkyl esters through alcoholysis: A critical evaluation of lipases and alcoholsJ Am Oil Chem Soc2005 5341347

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  106. 106.

    Kumari V Shah S Gupta MN Preparation of biodiesel by lipasecatalyzed transesterification of high free fatty acid containing oil from Madhuca indicaEnergy Fuels2007 1368372

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  107. 107.

    Shah S Gupta MN Lipase catalyzed preparation of biodiesel from Jatropha oil in a solvent-free systemProcess Biochem2007 3409414

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  108. 108.

    Gupta A Khare SK Enzymes from solvent-tolerant microbes: Useful biocatalysts for non-aqueous enzymologyCrit Rev Biotechnol2009 294454

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  109. 109.

    Doukyua N Ogino H Organic solvent-tolerant enzymesBiochem Eng J2010 48270282

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  110. 110.

    Klibanov AM Why are enzymes less active in organic solvents than in water?Trends Biotechnol1997 1597101

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  111. 111.

    Zhu X Zhou T Wu X Cai Y Yao D Xie C Liu D Covalent immobilization of enzymes within micro-aqueous organic mediaJ Mol Catal B: Enzym2011 72145149

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    Ru MT Dordick JS Reimer JA Clark DS Optimizing the salt-induced activation of enzymes in organic solvents: Effects of lyophilization time and water contentBiotechnol Bioeng1999 63233241

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  113. 113.

    Torres S Castro GR Non-aqueous biocatalysis in homogeneous solvent systemsFood Technol Biotechnol2004 42271277

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  114. 114.

    Gupta MN Roy I Enzymes in organic media. Forms, functions and applicationsEur J Biochem2004 1325752583

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  115. 115.

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  116. 116.

    Ogino H Uchiho T Yokoo J Kobayashi R Ichise R Ishikawa H Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in its organic solvent stabilityAppl Environ Microbiol2001 67942947

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  117. 117.

    Ogino H Uchiho T Doukyu N Yasuda M Ishimi K Ishikawa H Effect of exchange amino acid residues of the surface region of the PST-01 protease on its organic solvent-stabilityBiochem Biophys Res Commun2007 35810281033

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  118. 118.

    Gupta A Ray S Kapoor S Khare SK Solvent-stable Pseudomonas aeruginosa PseA protease gene: identification, molecular characterization, phylogenetic and bioinformatic analysis to study reasons for solvent stabilityJ Mol Microbiol Biotechnol2008 15234243

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    Karabec M Łyskowski A Tauber KC Steinkellner G Kroutil W Grogan G Gruber K Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541Chem Commun (Camb)2010 3463146316

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    Rich JO Dordick JS Vulfson J, Halling PJ, Holland HLImprinting enzymes for use in organic mediaEnzymes in Nonaqueous Media2000 Humana Press: Totowa, NJ

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  121. 121.

    Rich JO Mozhaev VV Dordick JS Clark DS Khmelnitsky YL Molecular imprinting of enzymes with water-insoluble ligands for nonaqueous biocatalysisJ Am Chem Soc2002 12452545255

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    Khmelnitsky Y Biotransformations in organic chemistry1997 A textbook, third edition, by Faber K, Springer-Verlag, Berlin

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  123. 123.

    Berman HM Westbrook J Feng Z Gilliland G Bhat TN Weissig H Shindyalov IN Bourne PE The Protein Data BankNucleic Acids Res2000 28235242

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    Guex N Peitsch MC SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelingElectrophoresis1997 1827142723

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    Premkumar L Greenblatt HM Bageshwar UK Savchenko T Gokhman I Sussman JL Zamir A Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homologProc Natl Acad Sci USA2005 2174937498

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    Evilia C Ming X DasSarma S Hou YM Aminoacylation of an unusual tRNA(Cys) from an extreme halophileRNA2003 7794801

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    Bohm G Jaenicke R A structure-based model for the halophilic adaptation of dihydrofolate reductase from Halobacterium volcaniiProtein Eng1994 7213220

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    Poidevin L MacNeill SA Biochemical characterisation of LigN, an NAD+-dependent DNA ligase from the halophilic euryarchaeon Haloferax volcanii that displays maximal in vitro activity at high salt concentrationsBMC Mol Biol2006 744

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  129. 129.

    Bandyopadhyay AK Krishnamoorthy G Padhy LC Sonawat HM Kinetics of salt-dependent unfolding of [2Fe-2S] ferredoxin of Halobacterium salinarumExtremophiles2007 4615625

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  130. 130.

    Britton KL Stillman TJ Yip KSP Forterre P Engel PC Rice DW Insights into the molecular basis of salt tolerance from the study of glutamate dehydrogenase from Halobacterium salinarumJ Biol Chem1998 27390239030

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    Chantawannakul P Yoshimune K Shirakihara Y Shiratori A Wakayama M Moriguchi M Crystallization and preliminary X-ray crystallographic studies of salt-tolerant glutaminase from Micrococcus luteus K-3Acta Crystallogr D Biol Crystallogr2003 3566568

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  132. 132.

    Mevarech M Eisenberg H Neumann E Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterizationBiochemistry1977 1737813785

    Not in our library10.1021/bi00636a009

  133. 133.

    Bonnete ÂF Madern D Zaccaõ ÈG Stability against denaturation mechanisms in halophilic malate dehydrogenase ''adapt'' to solvent conditionsJ Mol Biol1994 244436447

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  134. 134.

    Madern D Pfister C Zaccai G Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological saltsEur J Biochem1995 310881095

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  135. 135.

    Richard SB Madern D Garcin E Zaccai G Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortuiBiochemistry2000 59921000

    Not in our library10.1021/bi991001a

  136. 136.

    Madern D Zaccai G Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic proteinBiochimie2004 86295303

    Not in our library10.1016/j.biochi.2004.04.004

  137. 137.

    Tehei M Zaccai G Adaptation to extreme environments: macromolecular dynamics in complex systemsBiochim Biophys Acta2005 3404410

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  138. 138.

    Manikandan K Bhardwaj A Gupta N Lokanath NK Ghosh A Reddy VS Ramakumar S Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: structural insights into alkalophilicity and implications for adaptation to polyextreme conditionsProtein Sci2006 819511960

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    Davlieva M Shamoo Y Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organism Marinibacillus marinusActa Crystallogr Sect F Struct Biol Cryst Commun2009 8751756

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  140. 140.

    Asgeirsson B Hauksson JB Gunnarsson GH Dissociation and unfolding of cold-active alkaline phosphatase from atlantic cod in the presence of guanidinium chlorideEur J Biochem2000 2164036412

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  141. 141.

    Tsigos I Mavromatis K Tzanodaskalaki M Pozidis C Kokkinidis M Bouriotis V Engineering the properties of a cold active enzyme through rational redesign of the active siteEur J Biochem2001 26850745080

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  142. 142.

    Gudjónsdóttir K Asgeirsson B Effects of replacing active site residues in a cold-active alkaline phosphatase with those found in its mesophilic counterpart from Escherichia coliFEBS J2008 1117127

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  143. 143.

    Bauvois C Jacquamet L Huston AL Borel F Feller G Ferrer JL Crystal structure of the cold-active aminopeptidase from Colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolaseJ Biol Chem2008 342331523325

    Not in our library10.1074/jbc.m802158200

  144. 144.

    Huston AL Haeggström JZ Feller G Cold adaptation of enzymes: structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A(4) hydrolaseBiochim Biophys Acta2008 1118651872

    Not in our library10.1016/j.bbapap.2008.06.002

  145. 145.

    D'Amico S Gerday C Feller G Structural determinants of cold adaptation and stability in a large proteinJ Biol Chem2001 2762579125796

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  146. 146.

    Siddiqui KS Poljak A Guilhaus M Feller G D'Amico S Gerday C Cavicchioli R Role of disulfide bridges in the activity and stability of a cold-active alpha-amylaseJ Bacteriol2005 1762066212

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  147. 147.

    Papaleo E Pasi M Tiberti M De Gioia L Molecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutationsPLoS One2011 9e24214

    Not in our library10.1371/journal.pone.0024214

  148. 148.

    Birolo L Tutino ML Fontanella B Gerday C Mainolfi K Pascarella S Sannia G Vinci F Marino G Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modellingEur J Biochem2000 927902802

    Not in our library10.1046/j.1432-1327.2000.01299.x

  149. 149.

    Skálová T Dohnálek J Spiwok V Lipovová P Vondrácková E Petroková H Dusková J Strnad H Králová B Hasek J Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9Å resolutionJ Mol Biol2005 2282294

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  150. 150.

    Lorentzen MS Moe E Jouve HM Willassen NP Cold adapted features of Vibrio salmonicida catalase: characterisation and comparison to the mesophilic counterpart from Proteus mirabilisExtremophiles2006 5427440

    Not in our library10.1007/s00792-006-0518-z

  151. 151.

    Riise EK Lorentzen MS Helland R Smalås AO Leiros HK Willassen NP The first structure of a cold-active catalase from Vibrio salmonicida at 1.96 Å reveals structural aspects of cold adaptationActa Crystallogr D Biol Crystallogr2007 2135148

    Not in our library10.1107/s0907444906043812

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    Lonhienne T Zoidakis J Vorgias CE Feller G Gerday C Bouriotis V Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacteriumJ Mol Biol2001 310291297

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  153. 153.

    Russell RJ Gerike U Danson MJ Hough DW Taylor GL Structural adaptations of the cold-active citrate synthase from an Antarctic bacteriumStructure1998 6351361

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  154. 154.

    Gerike U Danson MJ Hough DW Cold-active citrate synthase: mutagenesis of active-site residuesProtein Eng2001 14655661

    Not in our library10.1093/protein/14.9.655

  155. 155.

    Bell GS Russell RJM Connaris H Hough DW Danson MJ Taylor GL Stepwise adaptations of citrate synthase to survival at life's extremes from psychrophile to hyperthermophileEur J Biochem2002 26962506260

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  156. 156.

    Kumar S Nussinov R Different roles of electrostatics in heat and in cold: Adaptation by citrate synthaseChem Bio Chem2004 5280290

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  157. 157.

    Jung SK Jeong DG Lee MS Lee JK Kim HK Ryu SE Park BC Kim JH Kim SJ Structural basis for the cold adaptation of psychrophilic M37 lipase from Photobacterium lipolyticumProteins2008 1476484

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    Simpson PJ Codd R Cold adaptation of the mononuclear molybdoenzyme periplasmic nitrate reductase from the Antarctic bacterium Shewanella gelidimarinaBiochem Biophys Res Commun2011 4783788

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  159. 159.

    Carginale V Trinchella F Capasso C Scudiero R Parisi E Gene amplification and cold adaptation of pepsin in Antarctic fish. A possible strategy for food digestion at low temperatureGene2004 2195205

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  160. 160.

    Miyazaki K Wintrode PL Grayling RA Rubingh DN Arnold FH Directed evolution study of temperature adaptation in a psychrophilic enzymeJ Mol Biol2000 29710151026

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    Aghajari N Van Petegem F Villeret V Chessa JP Gerday C Haser R Van Beeumen J Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold adapted proteasesProteins2003 50636647

    Not in our library10.1002/prot.10264

  162. 162.

    Xie BB Bian F Chen XL He HL Guo J Gao X Zeng YX Chen B Zhou BC Zhang YZ Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility and hydrogen bondingJ Biol Chem2009 1492579269

    Not in our library10.1074/jbc.m808421200

  163. 163.

    Zhong CQ Song S Fang N Liang X Zhu H Tang XF Tang B Improvement of low-temperature caseinolytic activity of a thermophilic subtilase by directed evolution and site-directed mutagenesisBiotechnol Bioeng2009 5862870

    Not in our library10.1002/bit.22473

  164. 164.

    Sigurdardóttir AG Arnórsdóttir J Thorbjarnardóttir SH Eggertsson G Suhre K Kristjánsson MM Characteristics of mutants designed to incorporate a new ion pair into the structure of a cold adapted subtilisin-like serine proteinaseBiochim Biophys Acta2009 3512518

    Not in our library10.1016/j.bbapap.2008.11.018

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    Almog O González A Godin N de Leeuw M Mekel MJ Klein D Braun S Shoham G Walter RL The crystal structures of the psychrophilic subtilisin S41 and the mesophilic subtilisin Sph reveal the same calcium-loaded stateProteins2009 2489496

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    Karan R Khare SK Stability of haloalkaliphilic Geomicrobium sp. protease modulated by saltBiochemistry (Mosc)2011 76686693

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    Karan R Singh RK Kapoor S Khare SK Gene identification and molecular characterization of solvent stable protease from a moderately haloalkaliphilic bacterium, Geomicrobium sp. EMB2J Microbiol Biotechnol2011 2129135

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  168. 168.

    Ohtani N Haruki M Morikawa M Kanaya S Heat labile ribonuclease HI from a psychrotrophic bacterium: gene cloning, characterization and site-directed mutagenesisProtein Eng2001 12975982

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  169. 169.

    Narinx E Baise E Gerday C Subtilisin from psychrophilic Antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to coldProtein Eng1997 1012711279

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    Matsumoto M Yokouchi H Suzuki N Ohata H Matsunaga T Saccharification of marine microalgae using marine bacteria for ethanol productionAppl Biochem Biotechnol2003 108247254

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  171. 171.

    Fukushima T Mizuki T Echigo A Inoue A Usami R Organic solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1Extremophiles2005 98589

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  172. 172.

    Chakraborty S Khopade A Kokare C Mahadik K Chopade B Isolation and characterization of novel a-amylase from marine Streptomyces sp. D1J Mol Catalysis B Enzymatic2009 581723

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    Kosjek B Stampfer W Pogorevc M Goessler W Faber K Kroutil W Purification and characterization of a chemotolerant alcohol dehydrogenase applicable to coupled redox reactionsBiotechnol Bioeng2004 865562

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    Kobori H Sullivan CW Shizuya H Heat-labile alkaline phosphatase from antarctic bacteria: rapid 5' end-labeling of nucleic acidsProc Natl Acad Sci USA1984 8166916695

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    Hoyoux A Jennes I Dubois P Genicot S Dubail F François JM Baise E Feller G Gerday C Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktisAppl Environ Microbiol2001 6715291535

    Not in our library10.1128/aem.67.4.1529-1535.2001

  176. 176.

    Maugard T Gaunt D Legoy MD Besson T Microwave-assisted synthesis of galacto-oligosaccharides from lactose with immobilized beta-galactosidase from Kluyveromyces lactisBiotechnol Lett2003 25623629

    Not in our library10.1023/a:1023060030558

  177. 177.

    Hildebrandt P Wanarska M Kur J A new cold-adapted β-D-galactosidase from the Antarctic Arthrobacter sp. 32c- gene cloning, overexpression, purification and propertiesBMC Microbiology2009 9151

    Not in our library10.1186/1471-2180-9-151

  178. 178.

    Bridiau N Issaoui N Maugard T The effects of organic solvents on the efficiency and regioselectivity of N-acetyl-lactosamine synthesis, using the β-galactosidase from Bacillus circulans in hydro-organic mediaBiotechnol Prog2010 2612781289

    Not in our library10.1002/btpr.445

  179. 179.

    Hatori Y Sato M Orishimo K Yatsunami R Endo K Fukui T Nakamura S Characterization of recombinant family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum strain NRC-1Chitin Chitosan Res2006 12201

    Not in our library

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    Essghaier B Hedi A Bejji M Jijakli H Boudabous A Sadfi-Zouaoui N Characterization of a novel chitinase from a moderately halophilic bacterium, Virgibacillus marismortui strain M3-23Annal Microbiol2011 DOI: 10.1007/s13213-011-0324-4

    Not in our library

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    Doukyu N Aono R Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp ST-200Appl Environ Microbiol1998 6419291932

    Not in our library10.1128/aem.64.5.1929-1932.1998

  182. 182.

    Yoshimune K Shirakihara Y Wakayama M Yumoto I Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator TrisFEBS J2010 3738748

    Not in our library10.1111/j.1742-4658.2009.07523.x

  183. 183.

    Hotta Y Ezaki S Atomi H Imanaka T Extremely stable and versatile carboxyl esterase from a hyperthermophilic archaeonAppl Environ Microbiol2002 6839253931

    Not in our library10.1128/aem.68.8.3925-3931.2002

  184. 184.

    Khudary RA Venkatachalam R Katzer M Elleuche S Antranikian G A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterizationExtremophiles2010 14273285

    Not in our library10.1007/s00792-010-0306-7

  185. 185.

    Kirk O Christensen MW Lipases from Candida antarctica: Unique biocatalysts from a unique originOrg Process Res Dev2002 6446451

    Not in our library

  186. 186.

    Giudice AL Michaud L de Pascale D Domenico MD di Prisco G Fani R Bruni V Lipolytic activity of Antarctic cold adapted marine bacteriaJ Appl Microbiol2006 10110391048

    Not in our library10.1111/j.1365-2672.2006.03006.x

  187. 187.

    Joseph B Ramteke PW Kumar PA Studies on the enhanced production of extracellular lipase by Staphylococcus epidermidisJ Gen Appl Microbiol2006 52315320

    Not in our library10.2323/jgam.52.315

  188. 188.

    Amoozegar MA Salehghamari E Khajeh K Kabiri M Naddaf S Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2J Basic Microbiol2008 48160167

    Not in our library10.1002/jobm.200700361

  189. 189.

    Gaur R Gupta A Khare SK Purification and characterization of lipase from solvent tolerant Pseudomonas aeruginosa PseAProcess Biochem2008 4310401046

    Not in our library

  190. 190.

    Pérez D Martín S Fernández-Lorente G Filice M Guisán JM Ventosa A García MT Mellado E A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA)PLoS ONE2011 6e23325

    Not in our library10.1371/journal.pone.0023325

  191. 191.

    Kamekura M Hamakawa T Onishi H Application of halophilic nuclease H of Micrococcus varians subsp. halophilus to commercial production of flavoring agent 5'-GMPAppl Environ Microbiol1982 44994995

    Not in our library10.1128/aem.44.4.994-995.1982

  192. 192.

    Truong LV Tuyen H Helmke E Binh LT Schweder T Cloning of two pectate lyase genes from the marine Antarctic bacterium Pseudoalteromonas haloplanktis strain ANT/505 and characterization of the enzymesExtremophiles2001 53544

    Not in our library10.1007/s007920000170

  193. 193.

    Ryu K Kim J Dordick JS Catalytic properties and potential of an extracellular protease from an extreme halophileEnzym Microb Technol1994 16266275

    Not in our library10.1016/0141-0229(94)90165-1

  194. 194.

    Kim J Dordick JS Unusual salt and solvent dependence of a protease from an extreme halophileBiotechnol Bioeng1997 55471479

    Not in our library10.1002/(sici)1097-0290(19970805)55:3<471::aid-bit2>3.0.co;2-9

  195. 195.

    Bobe IM Abdelmoez W Ogino H Yasuda M Ishimi K Ishikawa H Kinetics and mechanism of a reaction catalyzed by PST-01 protease from Pseudomonas aeruginosa PST-01Biotechnol Bioeng2004 86365373

    Not in our library10.1002/bit.20052

  196. 196.

    Tsuchiyama S Doukyu N Yasuda M Ishimi K Ogino H Peptide synthesis of aspartame precursor using organic solvent-stable PST-01 protease in monophasic aqueous organic solvent systemsBiotechnol Prog2007 23820823

    Not in our library10.1021/bp060382y

  197. 197.

    Gupta A Roy I Khare SK Gupta MN Purification and characterization of a solvent stable protease from Pseudomonas aeruginosa PseAJ Chrom A2005 1069155161

    Not in our library10.1016/j.chroma.2005.01.080

  198. 198.

    Pawar R Zambare V Barve S Paratkar G Application of protease isolated from Bacillus sp. in enzymatic cleansing of contact lensesBiotechnol2009 8276280

    Not in our library

  199. 199.

    Ruiz DM Iannuci NB Cascone O De Castro RE Peptide synthesis catalysed by a haloalkaliphilic serine protease from the archaeon Natrialba magadii (Nep)Lett Appl Microbiol2010 51691696

    Not in our library10.1111/j.1472-765x.2010.02955.x

  200. 200.

    Akolkar AV Durai D Desai AJ Halobacterium sp. SP1 (1) as a starter culture for accelerating fish sauce fermentationJ Appl Microbiol2010 1094453

    Not in our library10.1111/j.1365-2672.2009.04626.x

  201. 201.

    Karan R Khare SK Purification and characterization of a solvent stable protease from Geomicrobium sp EMB2Environ Technol2010 1010611072

    Not in our library10.1080/09593331003674556

  202. 202.

    Karan R Singh SP Kapoor S Khare SK A novel organic solvent tolerant protease from a newly isolated Geomicrobium sp. EMB2 (MTCC 10310): production optimization by response surface methodologyN Biotechnol2011 2136145

    Not in our library10.1016/j.nbt.2010.10.007

  203. 203.

    Collins T Hoyoux A Dutron A Georis J Genot B Dauvrin T Arnaut F Gerday C Feller G Use of glycoside hydrolase family 8 xylanases in bakingJ Cereal Sci2006 437984

    Not in our library

  204. 204.

    Dornez E Verjans P Arnaut F Delcour JA Courtin CM Use of psychrophilic xylanases provides insight into the xylanase functionality in bread makingJ Agric Food Chem2011 1795539562

    Not in our library10.1021/jf201752g

  205. 205.

    Wang K Li G Yu SQ Zhang CT Liu YH A novel metagenome-derived beta-galactosidase: gene cloning, overexpression, purification and characterizationAppl Microbiol Biotechnol2010 88155165

    Not in our library10.1007/s00253-010-2744-7

  206. 206.

    Prakash P Jayalakshmi SK Prakash B Rubul M Sreeramulu K Production of alkaliphilic, halotolerent, thermostable cellulase free xylanase by Bacillus halodurans PPKS-2 using agro waste: single step purification and characterizationWorld J Microbiol Biotechnol2011 DOI: 10.1007/s11274-011-0807-2

    Not in our library10.1007/s11274-011-0807-2

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