Purification and Biochemical Characterization of Alkalophilic Cellulase from the Symbiotic Bacillus subtilis BC1 of the Leopard Moth, Zeuzera pyrina (L.) (Lepidoptera: Cossidae)

In the current study, an extracellular cellulase belonging to symbiotic Bacillus subtilis Bc1 of the leopard moth is purified and characterized. The molecular mass of enzyme was 47.8 kDa using SDS-PAGE. The purified enzyme had optimum activity in temperature and pH around 60 °C and 8, respectively....

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Published in:Current microbiology 2020-07, Vol.77 (7), p.1254-1261
Main Authors: Dehghanikhah, Fahimeh, Shakarami, Jahanshir, Asoodeh, Ahmad
Format: Article
Language:English
Subjects:
Acetone
Animals
Bacillus subtilis
Bacillus subtilis - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Biomedical and Life Sciences
Biotechnology
Butterflies & moths
Calcium chloride
Carboxymethyl cellulose
Carboxymethylcellulose
Cellobiose
Cellulase
Cellulase - chemistry
Cellulase - isolation & purification
Cellulase - metabolism
Cellulose
Endoglucanase
Enzyme Stability
Enzymes
Gel electrophoresis
Kinetics
Life Sciences
Metal ions
Microbiology
Moths - microbiology
Nickel chloride
Organic solvents
pH effects
Sodium lauryl sulfate
Solvents
Symbiosis
Thin layer chromatography
Zeuzera pyrina
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description In the current study, an extracellular cellulase belonging to symbiotic Bacillus subtilis Bc1 of the leopard moth is purified and characterized. The molecular mass of enzyme was 47.8 kDa using SDS-PAGE. The purified enzyme had optimum activity in temperature and pH around 60 °C and 8, respectively. The purified cellulase was introduced as a stable enzyme in a wide variety of temperature (20–80 °C) and pH (4–10) and remained active to more than 74% at 80 °C for 1 h. Moreover, the cellulase extremely was stabled in the presence of metal ions and organic solvents and its activity was increased by acetone (20% v/v), CaCl 2 and CoCl 2 and inhibited by MnCl 2 and NiCl 2 . The values of enzyme's K m and V max were found to be 1.243 mg/mL and 271.3 µg/mL/min, respectively. The purified cellulase hydrolyzed cellulose, avicel and carboxymethyl cellulose (CMC) and the final product of CMC hydrolysis was cellobiose using thin-layer chromatography analysis. Consequently, owing to exo/endoglucanase activity and organic solvent, temperature and pH stability of the purified cellulase belong to B. subtilis BC1, it can be properly employed for various industrial purposes.
doi_str_mv 10.1007/s00284-020-01938-z
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source Springer Nature
subjects Acetone
Animals
Bacillus subtilis
Bacillus subtilis - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Biomedical and Life Sciences
Biotechnology
Butterflies & moths
Calcium chloride
Carboxymethyl cellulose
Carboxymethylcellulose
Cellobiose
Cellulase
Cellulase - chemistry
Cellulase - isolation & purification
Cellulase - metabolism
Cellulose
Endoglucanase
Enzyme Stability
Enzymes
Gel electrophoresis
Kinetics
Life Sciences
Metal ions
Microbiology
Moths - microbiology
Nickel chloride
Organic solvents
pH effects
Sodium lauryl sulfate
Solvents
Symbiosis
Thin layer chromatography
Zeuzera pyrina
title Purification and Biochemical Characterization of Alkalophilic Cellulase from the Symbiotic Bacillus subtilis BC1 of the Leopard Moth, Zeuzera pyrina (L.) (Lepidoptera: Cossidae)
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