A trimeric and thermostable lichenase from B. pumilus US570 strain: Biochemical and molecular characterization

•β-1,3;1,4-Glucanase was purified from a newly isolated Bacillus pumilus US570 strain.•It showed an optimum pH and temperature of 5 and 55°C respectively.•It has a noticeable thermostability making it useful for an industrial application.•It has a trimeric form with a molecular mass of about 75kDa.•...

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Bibliographic Details
Published in:International journal of biological macromolecules 2017-02, Vol.95, p.273-280
Main Authors: Elgharbi, Fatma, Ben Hlima, Hajer, Ameri, Rihab, Bejar, Samir, Hmida-sayari, Aïda
Format: Article
Language:English
Subjects:
3D model
Amino Acid Sequence
Bacillus - enzymology
Enzyme Stability
Glycoside Hydrolases - chemistry
Glycoside Hydrolases - metabolism
Hydrogen-Ion Concentration
Kinetics
Metals - pharmacology
Models, Molecular
Protein Multimerization
Protein Structure, Quaternary
Substrate Specificity
Temperature
Thermostable lichenase
Trimeric form
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Summary:•β-1,3;1,4-Glucanase was purified from a newly isolated Bacillus pumilus US570 strain.•It showed an optimum pH and temperature of 5 and 55°C respectively.•It has a noticeable thermostability making it useful for an industrial application.•It has a trimeric form with a molecular mass of about 75kDa.•The 3D model with three glucanase molecules in trimeric form was generated. New β-1,3;1,4-glucanase (GluUS570) was purified from a newly isolated Bacillus pumilus US570 strain. The enzyme was active in a wide range of pH and temperature and displayed a great thermostability with a half-life of 30min at 80°C. The enzyme was demonstrated to be a lichenase since it was only active toward glucan containing β-1,3;1,4- linkages. The analysis of the enzyme in native and denaturing conditions suggests that it has a trimeric form (75kDa). This is the first report on the purification and characterization of a bacterial lichenase with a trimeric structure. β-1,3;1,4-glucanase encoding gene was amplified, cloned and sequenced showing an open reading frame of 732bp encoding 243 amino acids. The GluUS570 enzyme showed 97% homology with glucanase from Bacillus lichenoformis. The 3D model of GluUS570 in trimeric form was generated and showed that a region named R2 was involved in the oligomerization of the enzyme.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2016.11.021