Cloning and characterization of thermostable amylopullulanase TbbApu and its C-terminal truncated variants with enhanced activity in organic solvents

Mumcu, Hande; Kayrav, Aycan; İşleyen, Naciye Durmuş; Karagüler, Nevin Gül

doi:10.1016/j.enzmictec.2022.110176

Enzyme and Microbial Technology

2023

DOI: 10.1016/j.enzmictec.2022.110176

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Cloning and characterization of thermostable amylopullulanase TbbApu and its C-terminal truncated variants with enhanced activity in organic solvents

Hande Mumcu

Aycan Kayrav

Naciye Durmuş İşleyen

et al.

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2024

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Cited by 6 publications

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Cloning, purification, and functional characterization of recombinant pullulanase from Bacillus cereusATCC 14579 for improved detergent performance

Zafar,

Masood,

Rahman

et al. 2024

J Surfact & Detergents

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The present study outlines the approach that was employed for cloning, expression, and characterization of the recombinant pullulanase enzyme from Bacillus cereus ATCC 14579 into Escherichia coli BL21(DE3) using pET‐25b (+) expression vector. The recombinant pullulanase enzyme was purified using ammonium sulfate precipitation and immobilized metal ion affinity chromatography (IMAC). The molecular mass of the purified pullulanase enzyme was measured using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) as 95 kDa. The purified recombinant pullulanase enzyme demonstrated significant thermal stability, maintaining its structural integrity and functionality at temperatures as high as 90°C over a period of 4 h. The inclusion of divalent metal ions, specifically Ca2+ and Mg2+, had a positive effect on the activity of the pullulanase enzyme. Conversely, the presence of Co2+ and EDTA (Ethylene Diamine Tetra Acetic acid) resulted in suppression of the enzyme activity. The purified pullulanase enzyme demonstrated remarkable resistance when exposed to organic solvents. The enzyme activity was notably decreased in the presence of SDS (Sodium Dodecyl Sulfate) while β‐mercaptoethanol and tween‐60 did not substantially affect the enzyme activity and stability which suggest its potential applicability in the detergent sector. This discovery indicates a potential approach to improve the effectiveness of currently available detergents in the marketplace.

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Cloning, purification, and functional characterization of recombinant pullulanase from Bacillus cereusATCC 14579 for improved detergent performance

Zafar,

Masood,

Rahman

et al. 2024

J Surfact & Detergents

View full text Add to dashboard Cite

show abstract

A malto-oligosaccharide forming thermostable acidic α-amylase from Bacillus stercoris YSP18 isolated from sediment of Sikkim hot spring: heterologous expression and characterisation

Sharma,

Mondal,

Tamang

et al. 2024

Syst Microbiol and Biomanuf

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A review of the principles and biotechnological applications of glycoside hydrolases from extreme environments

Ashcroft,

Munoz-Munoz

2024

International Journal of Biological Macromolecules

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Cloning and characterization of thermostable amylopullulanase TbbApu and its C-terminal truncated variants with enhanced activity in organic solvents

Cited by 6 publications

References 42 publications

Cloning, purification, and functional characterization of recombinant pullulanase from Bacillus cereusATCC 14579 for improved detergent performance

Cloning, purification, and functional characterization of recombinant pullulanase from Bacillus cereusATCC 14579 for improved detergent performance

A malto-oligosaccharide forming thermostable acidic α-amylase from Bacillus stercoris YSP18 isolated from sediment of Sikkim hot spring: heterologous expression and characterisation

A review of the principles and biotechnological applications of glycoside hydrolases from extreme environments

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