Practical importance of enzyme stability - I: Natural sources of more stable enzymes; II: Increase of enzyme stability by immobilization and treatment with low molecular weight reagents; III: Increase of enzyme stability by protein engineering

Zentgraf, B.; Ringpfeil, M.; Martínek, Karel; Mozhaev, Vadim V.; Ahern, Tim J.

doi:10.1351/pac199163101527

Cited by 24 publications

(8 citation statements)

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“…Temperature is one of the critical parameters in the optimization of enzymatic reactions, and in general an accelerated reaction rate is expected with increasing reaction temperature. However, irreversible denaturation of the enzyme is occurring at higher temperatures and in some cases a proper immobilization strategy can improve the thermo stability of enzymes [57]. Therefore, the influence of temperature on the activity of PMO CLEAs was studied between 40 and 80 • C (Fig.…”

Section: Transesterification Reaction In a Batch Reactormentioning

confidence: 99%

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

et al. 2015

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Section: Transesterification Reaction In a Batch Reactormentioning

confidence: 99%

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

et al. 2015

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“…In particular, the detailed knowledge of the limits of resistance of enzymes to the turnover in extreme non-physiological conditions (high temperatures, extreme ranges of pH and/or ionic strength, high concentration of organic solvents or presence of immobilizing matrixes ) is an important objective [12].…”

Section: Introductionmentioning

confidence: 99%

Theseus: A new software package for the handling and analysis of thermal denaturation data of biological macromolecules

Barone

Vecchio

Fessas

et al. 1992

Journal of Thermal Analysis

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A new software package (THESEUS) has been assembled for the analysis of the DSC data, concerning the thermal denaturation of biological macromolecules. The system is useful to obtain accurate physico-chemical information, bypassing the casual and systematic errors, very common in these experiments. It can also be used for handling data from other instruments and methodologies giving thermodynamic, spectroscopic or other kind of data as a function of temperature. Because many of the researches in this field are of exploratory nature and continuously new unfolding mechanisms are described or hypothesized in the current literature, we have written and assembled this powerful and flexible program of general applicability, in order to put the operator in a position to control each step of the calculation procedure and use his own experience for choosing the better way to solve unexpected problems.

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“…The specific growth rate and/or the yield coefficient of thermophilic bacteria could be improved by -continuous, instead of batch, cultivation, which would prevent the inhibition of bacterial -increasing system pressure in fermenters [22]. However, in no case did the yield coefficient realized by thermophiles under extreme physico-chemical conditions approach the values ofmesophilic microorganisms [6,22,27]. In order to establish rapid and efficient biotechnical processes on the basis of thermophiles for commercial use, the by-products of biomass production should be taken into coconsideration.…”

Section: Thermophilic Microorganisms As a Source Of More Stable Enzymesmentioning

confidence: 99%

“…Such stabilizing effects contribute to the long-term stability of an enzyme. Thermostability is also related to a higher resistance to most chemical denaturants [6,8,91.…”

Section: Introductionmentioning

confidence: 99%

Enzymes from thermophiles

Zentgraf¹

1992

Acta Biotechnologica

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The most frequently used sources of more stable enzymes are thermophilic bacteria, e.g. Bacillus, Closrridium, and Therrnus strains, occurring in natural as well as man-made habitats. They grow from 55 to 88 "C with a specific growth rate of up to 2.6 h-' and a yield coefficient of up to 0.4 gram of dry cell weight per gram of carbohydrate consumed. Several thermophilic strains, e.g. Bacillus sp. TP32, rapidly and effectively produce enzymes having a higher thermal stability and resistance to chemical denaturants in comparison to their mesophilic counterparts. Therefore, thermostable enzymes are of importance for bioorganic syntheses. For the further optimization of enzyme production, genetic engineering is applied.

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Practical importance of enzyme stability - I: Natural sources of more stable enzymes; II: Increase of enzyme stability by immobilization and treatment with low molecular weight reagents; III: Increase of enzyme stability by protein engineering

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Cited by 24 publications

References 0 publications

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

Theseus: A new software package for the handling and analysis of thermal denaturation data of biological macromolecules

Enzymes from thermophiles

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