Engineering of Thermal Stability in a Cold-Active Oligo-1,6-Glucosidase from Exiguobacterium sibiricum with Unusual Amino Acid Content.

doi:10.3390/biom11081229

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Article

Engineering of Thermal Stability in a Cold-Active Oligo-1,6-Glucosidase from Exiguobacterium sibiricum with Unusual Amino Acid Content.

Biomolecules - 17 Aug 2021

Berlina Yana Y, Petrovskaya Lada E, Kryukova Elena A, Shingarova Lyudmila N, Gapizov Sultan Sh, Kryukova Mariya V, Rivkina Elizaveta M, Kirpichnikov Mikhail P, Dolgikh Dmitry A

Abstract excerpt

A gene coding for a novel putative amylase, oligo-1,6-glucosidase from a psychrotrophic bacterium Exiguobacterium sibiricum from Siberian permafrost soil was cloned and expressed in Escherichia coli. The amino acid sequence of the predicted protein EsOgl and its 3D model displayed several features characteristic for the cold-active enzymes while possessing an unusually high number of proline residues in the...

Topics

Amino Acids
Circular Dichroism
Cloning, Molecular
Cold Temperature
Computational Biology
Enzyme Stability
Exiguobacterium
Glucosidases
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Mutagenesis
Mutagenesis, Site-Directed

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Oligo-1,6-Glucosidase

Permafrost

Proline

Protein Engineering

Source

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Identifiers

PMID: 34439895
DOI: 10.3390/biom11081229
PMCID: PMC8392543

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