Molecular Adaptations of Enzymes from Thermophilic and Psychrophilic Organisms

Arpigny, Jean Louis; Feller, Georges; Davail, Stéphane; Genicot, Sabine; Narinx, Emmanuel; Zekhnini, Z.; Gerday, Charles

doi:10.1007/978-3-642-78598-6_6

Cited by 22 publications

(13 citation statements)

References 70 publications

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“…However, the enzymes that are added to detergents for removal of macromolecular stains, e.g., subtilisin, lipase and glycosidases, are poorly active at the tap water tempeature, and required to be substituted by cold active enzymes [69]. Psychrophiles and psychrotrophs, both the groups are known to produce enzymes with high level of activity at low temperatures [70,71]. When compared to their mesophilic counterpart, these enzymes display high catalytic efficiencies in order to maintain proper metabolic fluxes at low temperatures [68,71].…”

Section: Alkaline Proteases From Psychrophiles/psychrotrophsmentioning

confidence: 99%

“…Psychrophiles and psychrotrophs, both the groups are known to produce enzymes with high level of activity at low temperatures [70,71]. When compared to their mesophilic counterpart, these enzymes display high catalytic efficiencies in order to maintain proper metabolic fluxes at low temperatures [68,71].…”

Section: Alkaline Proteases From Psychrophiles/psychrotrophsmentioning

confidence: 99%

“…It was deduced that several factors play important role to gain protein flexibility, including reduction of electrostatic non-covalent weak interactions (salt bridges, polar interactions between aromatic side chains, hydrogen bonds) and decrease of hydrophobicity [113,114]. Also, molecular adaptation appears to have induced looser surface loops, more polar surfaces exposed to solvent, lower affinity of Ca 2+ binding sites and less stabilized α-helices [71,111,115].…”

Section: Alkaline Proteases From Psychrophiles/psychrotrophsmentioning

confidence: 99%

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Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Garg¹,

Singh²

2015

Enz Eng

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Since the advent and release of Bio 40 (the first detergent with bacterial alkaline protease) in 1959, exploration of the microbial alkaline proteases has been exploited beyond expectations. The inventory of microbial alkaline proteases is difficult to draft as it is increasing daily. Most of these proteases are the result of studies in which one or a few isolates were targeted for an alkali-stable enzyme. Although, the worldwide research on microbial alkaline proteases has been widely performed, we still need an improved enzyme capable of catalyzing reactions under extreme conditions (also called as extremozymes), e.g., high alkalinity and salinity, anhydrous environment, cold and hot environment, etc. As the search for extremozymes is in progress, it is imperative to explore the extreme environments to get some novel microbial strains (extremophiles) for alkali-stable proteases. This review article is an effort to compile the scattered information on some extremophiles and their alkali-stable proteases, which may have better specific industrial applications. It includes: (i) various extreme environments relevant to industrial biocatalysts, (ii) strategies of extremophilic microbes and enzymes which make them able to tolerate such conditions, and (iii) an overview of some important work done so far to explore industrially relevant extremophilic enzymes from extremophiles.

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Section: Alkaline Proteases From Psychrophiles/psychrotrophsmentioning

confidence: 99%

Section: Alkaline Proteases From Psychrophiles/psychrotrophsmentioning

confidence: 99%

Section: Alkaline Proteases From Psychrophiles/psychrotrophsmentioning

confidence: 99%

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Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Garg¹,

Singh²

2015

Enz Eng

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“…Cold enzymes have been obtained from microorganisms living in environments where the temperatures never exceed 10 "C, and especially from Antarctic sea water, where they never exceed 2 "C. When compared to their mesophilic counterparts, these enzymes display high catalytic efficiencies in order to maintain appropriate metabolic fluxes at these low temperatures (Arpigny et al, 1994;Feller et al, 1996). Current hypotheses relate the increase in catalytic activity to a higher protein structural flexibility, allowing low energy cost conformational changes during catalysis (Hochachka & Somero, 1984).…”

Section: Introductionmentioning

confidence: 99%

“…From modeling studies based on sequence homologies, possible features of Reprint requests to: Jozef Van Beeumen, Vakgroep Biochemie, Fysiologie en Microbiologie, Universiteit Gent, Ledeganckstraat 35, B-9000 Gent, Belgium; e-mail: jozef.vanbeeumen@rug.ac.be. molecular adaptations to the cold were proposed recently (Arpigny et al, 1994). In psychrophilic enzymes, molecular adaptations appear to have induced looser surface loops, more polar surfaces exposed to solvent or lower hydrophobicity of the protein core, lower affinity of Ca2+ binding sites, a reduced number of salt bridges, less stabilized a-helices, and eventually weaker hydrogen bonding.…”

Section: Introductionmentioning

confidence: 99%

Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile pseudomonas aeruginosa

et al. 1997

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Abstract:A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P2,2,2,. A complete data set to 2.1 A resolution has been measured. The structure has been determined by the molecular replacement method using the coordinates of the mesophilic alkaline protease as a model. The molecular replacement solution displays a correlation coefficient of 0.39 and an R-factor of 0.48. Subsequent inspection of the electron density map in the active site region has confirmed the correctness of the solution. Model building and structure refinement will be initiated when the protease sequence becomes fully available. This is the second report, following one on an a-amylase, of the preliminary crystallographic characterization of a psychrophilic enzyme.

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Temperature Relationships: From Molecules to Biogeography

Somero¹

1997

Comprehensive Physiology

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The sections in this article are: Temperature Effects on Physiological, Biochemical, and Molecular Systems: Basic Considerations Temperature Effects on Proteins Determinants of Thermal Sensitivities of Protein Structure and Function Protein Structural Stability and Adaptation Temperature Adaptations in Enzyme Kinetic Properties Lead to Conservation of Metabolic Regulation and Rate of Function Rate Compensation to Temperature Through Alterations in Enzyme Concentration The Heat Shock Response Molecular Chaperones: Assistants in Protein Folding, Compartmentation, and Renaturation The Heat Shock Response and Induced Thermal Tolerance Acclimatization‐Induced Differences in the Heat Shock Response Interindividual and Intertissue Differences in the Heat Shock Response Evolutionary, Interspecific Differences in the Heat Shock Response Cellular Thermometers and Regulation of HSP Synthesis Cold Shock May Induce Stress Proteins Temperature Effects on Lipids and Membrane‐Localized Functions Temperature Effects on Membrane Lipids: Changes in Phase and Fluidity Membrane Fluidity and Compositional Changes Correlate With Effects on Membrane Functions Homeoviscous Adaptation: Occurrence and Efficacy Adaptation of Membrane Lipids: Regulation and Biophysical Effects Adaptive Regulation of Depot and Membrane Lipid Fluidity in Hibernators Membrane Lipids of Thermophilic Archaebacteria Membrane Adaptations Involving Extrinsic Factors: pH and Solutes Cuticular Waxes: Regulation of Body Temperature and Control of Water Loss Evaporative Cooling in Insects Temperature–pH Interactions Temperature Dependence of Body Fluid pH Values The Imidazole Alphastat Hypothesis Functional Manifestations of the Advantages of Alphastat Regulation Deviations from Alphastat Regulation in Small Mammalian Hibernators Variation in Alpha Imidazole among Species, Tissues, Histidyl Residues, and Methodologies Biogeographical Implications of Temperature Adaptation

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Molecular Adaptations of Enzymes from Thermophilic and Psychrophilic Organisms

Cited by 22 publications

References 70 publications

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile pseudomonas aeruginosa

Temperature Relationships: From Molecules to Biogeography

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