Optimization to Low Temperature Activity in Psychrophilic Enzymes
نویسندگان
چکیده
منابع مشابه
Optimization to Low Temperature Activity in Psychrophilic Enzymes
Psychrophiles, i.e., organisms thriving permanently at near-zero temperatures, synthesize cold-active enzymes to sustain their cell cycle. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, the...
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The oxidative and fermentative activities of a psychrophilic bacterium (strain 82), whose maximal growth temperature is 35 C, were completely destroyed by exposure of the cells to 46 C for about 1 hr, whereas those of mesophilic Escherichia coli were unaffected. Similar results were obtained with cell-free extracts. In attempts to determine some of the specific enzymes inactivated in strain 82 ...
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Psychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affi...
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The enzyme ornithine carbamoyltransferase (OTCase) of Moritella abyssi (OTCase(Mab)), a new, strictly psychrophilic and piezophilic bacterial species, was purified. OTCase(Mab) displays maximal activity at rather low temperatures (23 to 25 degrees C) compared to other cold-active enzymes and is much less thermoresistant than its homologues from Escherichia coli or thermophilic procaryotes. In v...
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Background: Cold-adapted enzymes remain catalytically active at low temperatures. Results: Mutants of a cold-adapted alpha-amylase stabilized by engineered weak interactions and a disulfide bond have lost the kinetic optimization to low temperatures. Conclusion: The disappearance of stabilizing interactions in psychrophilic enzymes increases the dynamics of active site residues at low temperatu...
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ژورنال
عنوان ژورنال: International Journal of Molecular Sciences
سال: 2012
ISSN: 1422-0067
DOI: 10.3390/ijms130911643