Multiple mutants of a psychrophilic α-amylase 1 Stepwise adaptations to low temperature as revealed by multiple mutants of a psychrophilic α-amylase from an Antarctic bacterium*
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چکیده
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 temperature, leading to a higher activity. Significance: An experimental support to the activity-stability relationships.
منابع مشابه
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تاریخ انتشار 2011