Efficient Production of Bacillus flexus β-amylase in Brevibacillus choshinensis and its Potential as an Industrial Catalyst

β-amylases catalyze the generation of β-maltose from the non-reducing end of starch through hydrolysis of α-1,4-glucosidic bonds. Bacterial β-amylases are more suitable for β-maltose production, but their yields are typically too low. In this study, the β-amylase from Bacillus flexus CCTCC2015368 was efficiently produced in Brevibacillus choshinensis. The purified recombinant β-amylase had a specific activity of 2650 U/mg using soluble starch as the substrate, its optimal temperature and pH were 50°C and 7.0, respectively, and its half-life at 50°C and pH 7.0 was 34 h. When produced in the 3-L fermenter under optimal fermentation conditions, the β-amylase activity in the culture supernatant peaked at 4470 U/mL (1.7 mg/mL). After optimizing the reaction conditions, the highest yield of maltose (86.9%) from 30% (wt/vol) potato starch was obtained by combining the B. flexus β-amylase with isoamylase and maltogenic amylase. This study laid the foundation for the large-scale production and wide application of recombinant the B. flexus β-amylase.

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Publication Details

Journal
Applied Biochemistry and Microbiology
Published
2025-04-01
DOI
https://doi.org/10.1134/s0003683824604116
Primary Topic
Enzyme Production and Characterization
Type
article
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article

Efficient Production of Bacillus flexus β-amylase in Brevibacillus choshinensis and its Potential as an Industrial Catalyst

Xinhua Qi, Bowen Xu, X. K. Qiao, Kang Xu
Applied Biochemistry and Microbiology
Enzyme Production and Characterization
article

Efficient Production of Bacillus flexus β-amylase in Brevibacillus choshinensis and its Potential as an Industrial Catalyst

Xinhua Qi, Bowen Xu, X. K. Qiao, Kang Xu
article en

Abstract

β-amylases catalyze the generation of β-maltose from the non-reducing end of starch through hydrolysis of α-1,4-glucosidic bonds. Bacterial β-amylases are more suitable for β-maltose production, but their yields are typically too low. In this study, the β-amylase from Bacillus flexus CCTCC2015368 was efficiently produced in Brevibacillus choshinensis. The purified recombinant β-amylase had a specific activity of 2650 U/mg using soluble starch as the substrate, its optimal temperature and pH were 50°C and 7.0, respectively, and its half-life at 50°C and pH 7.0 was 34 h. When produced in the 3-L fermenter under optimal fermentation conditions, the β-amylase activity in the culture supernatant peaked at 4470 U/mL (1.7 mg/mL). After optimizing the reaction conditions, the highest yield of maltose (86.9%) from 30% (wt/vol) potato starch was obtained by combining the B. flexus β-amylase with isoamylase and maltogenic amylase. This study laid the foundation for the large-scale production and wide application of recombinant the B. flexus β-amylase.

Applied Biochemistry and MicrobiologyVol. 61(2)
Sinopec (China) (CN), Jiangnan University (CN), American Petroleum Institute (US), Tobacco Research Institute (CN)
Openalex Percentile: Top 92%
Enzyme Production and Characterization
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