AIMC Topic: Enzyme Stability

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Characterization of a Novel Mutansucrase (MUT-I) from G29: Enzymatic Properties and Product Analysis.

Journal of agricultural and food chemistry
Glucansucrases are extracellular enzymes capable of synthesizing diverse α-glucan polymers and oligosaccharides, including the industrially relevant mutan. The I-encoded mutansucrase (MUT-I) from G29 was biochemically characterized as a robust bioca...

Glycolysis-compatible urethanases for polyurethane recycling.

Science (New York, N.Y.)
Recycling thermoset polyurethanes is hindered by their cross-linked structures and chemically stable urethane bonds. Although chemo-enzymatic approaches offer promise, known urethanases remain inefficient under industrial glycolysis conditions. Here,...

Deep-Learning-Guided Mining and Clustering of Remote Amino Acid Residues for the Simultaneous Engineering of the Catalytic Activity and Thermostability of a Processive Endoglucanase.

ACS synthetic biology
Processive endoglucanases, which possess both endo- and exoglucanase activities, are considered highly promising catalysts in cellulose degradation. In this study, we employed multiple deep learning models, including MutCompute, DeepSequence, and ESM...

Modeling Enzyme Temperature Stability from Sequence Segment Perspective.

Journal of chemical information and modeling
Developing enzymes with desired thermal properties is crucial for a wide range of industrial and research applications, and determining temperature stability is an essential step in this process. Experimental determination of thermal parameters is la...

A computational pipeline for predicting distal hotspots in an artificial enzyme.

International journal of biological macromolecules
Targeting distal mutations holds promising implications for enzyme engineering. Here, we present an open-source computational workflow designed to explore the functional impact of distal sites, demonstrated on an artificial enzyme built on the widely...

Iterative enhancement of cutinase thermostability by multiple strategies based on combined directed evolution and computationally assisted design.

Bioresource technology
Cutinase exhibits versatile biocatalytic potential in polymer degradation, textile processing, and industrial biocatalysis, where enhancing the thermal stability under extreme conditions is essential for practical applications. To enhance the thermal...

Role of electrostatics in cold adaptation: A comparative study of eury- and stenopsychrophilic triose phosphate isomerase.

Biochimica et biophysica acta. Proteins and proteomics
Psychrophilic (cold-active) organisms have developed enzymes that facilitate sufficient metabolic activity at low temperatures to sustain life. This occurs through molecular adaptations that tend to increase protein flexibility at the expense of stab...

Thermal Adaptation of Cytosolic Malate Dehydrogenase Revealed by Deep Learning and Coevolutionary Analysis.

Journal of chemical theory and computation
Protein evolution has shaped enzymes that maintain stability and function across diverse thermal environments. While sequence variation, thermal stability and conformational dynamics are known to influence an enzyme's thermal adaptation, how these fa...

Cloning, Characterization, and Computer-Aided Evolution of a Thermostable Laccase of the DUF152 Family From Klebsiella michiganensis.

Proteins
Bacterial laccases exhibit relatively high optimal reaction temperatures and possess a broad substrate spectrum, thereby expanding the range of potential applications for laccase enzymes. This study aims to investigate the molecular evolution of bact...

Tailoring industrial enzymes for thermostability and activity evolution by the machine learning-based iCASE strategy.

Nature communications
The pursuit of obtaining enzymes with high activity and stability remains a grail in enzyme evolution due to the stability-activity trade-off. Here, we develop an isothermal compressibility-assisted dynamic squeezing index perturbation engineering (i...