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Article

Improvement of thermostability and halostability of β-1,3-1,4-glucanase by substituting hydrophobic residue for Lys48.

International journal of biological macromolecules - 1 Jan 2017

Lee Jong Min, Moon Soo Young, Kim Yu-Ri, Kim Kang Woong, Lee Bong-Joo, Kong In-Soo

Abstract excerpt

The aim of this study was to improve the stability of β-1,3-1,4-glucanase by substituting hydrophobic residue for specific amino acid. The results indicated that the catalytic efficiency, thermostability and halostability were enhanced simultaneously by replacement of Lys48 with Ala (K48A) or Leu (K48L). Comparison of kinetic parameters revealed that catalytic efficiency of mutants is enhanced as a result of the...

Topics

Alanine
Amino Acid Sequence
Amino Acid Substitution
Bacillus
Bacterial Proteins
Biocatalysis
Endo-1,3(4)-beta-Glucanase
Enzyme Stability
Hot Temperature
Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ionic Liquids

Kinetics

Leucine

Lysine

Mutagenesis, Site-Directed

Mutation

Sequence Alignment

Sodium Chloride

Source

Identifiers

PMID: 27765566
DOI: 10.1016/j.ijbiomac.2016.10.043

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