Production, Partial Purification and Characterization of α-Amylase from High Molecular Weight Polycyclic Aromatic Hydrocarbons (HMW-PAHs) Degrading Bacillus subtilis BMT4i (MTCC 9447)

Lily, Madhuri Kaushish; Bahuguna, Ashutosh; Bhatt, Kamlesh Kumar; Dangwal, Koushalya

doi:10.5505/tjb.2012.07279

Cited by 4 publications

(1 citation statement)

References 36 publications

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“…The K m value in this study was in agreement with the K m value in other studies on Bacillus species, which ranged from 1.08 to 16.67 mg mL -1 21,28,29,45,46,54 . The V max value in the present study was higher than that of 47.62 U mg -1 proteins 45 and lower than that of 5000 U 46 and 1773 …”

Section: Kinetics Of A-amylasementioning

confidence: 45%

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Irfan¹

2017

Chem.Biochem.Eng.Q.

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University of the Punjab new campus Lahore PakistanThis study reveals the production of α-amylase through Bacillus subtilis by submerged fermentation of wheat bran as a substrate. Various conditions were optimized and maximum production was observed at initial medium pH of 7.0, incubation temperature of 35 °C with agitation speed of 140 rpm for 48 h of fermentation period. Peptone, ammonium sulphate and soluble starch favored enzyme production as nitrogen and carbon source, respectively. The crude α-amylase was purified 2.03-fold by column (sephadex G-100) chromatography having specific activity of 480.0 U mg -1 . The purified enzyme had molecular mass of 54.18 kDa as determined by 12 % SDS-PAGE. The optimum pH and temperature of the enzyme was 8.5 and 60 °C, respectively. Ca 2+ played an important role in the stability of the enzyme retaining relative activity of 87 % and 67 % at pH 9.5 and 80 °C, revealing the Ca 2+ dependency respectively. The enzyme was highly stable towards surfactants and oxidizing agents. Kinetic study indicated that the enzyme exhibit K m and V max value of 4.4 mg mL -1 and 714.2 U mL -1 using soluble starch as a substrate respectively.

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Section: Kinetics Of A-amylasementioning

confidence: 45%

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Irfan¹

2017

Chem.Biochem.Eng.Q.

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Exploring the bioremediation potential of Bacillus spp. for sustainable mitigation of hydrocarbon contaminants

Das,

Rajkumari

et al. 2024

Environmental Sustainability

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Purification and characterization of two isoforms of native α amylase from Ok-Rong mango (Mangifera indica Linn. cv. Ok-Rong)

Ubonbal

Porsoongnoen

Daduang

et al. 2017

Turkish Journal of Biochemistry

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Introduction:The tropical plant amylases involved in the fruit ripening stage is outstanding for their high activities in converting starch to sugars within a short period at high temperatures over 40°C.Methods:The α amylase iso-enzymes from Ok-Rong mango (Results:The enzyme was purified 105-fold with a final specific activity of 59.27 U mgConclusion:Two α amylase iso-enzymes were classified as members of the low-pI group of amylases with identical structure, properties and functions. They are mesophilic with high possibilities for application for many purposes.

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Production, Partial Purification and Characterization of α-Amylase from High Molecular Weight Polycyclic Aromatic Hydrocarbons (HMW-PAHs) Degrading Bacillus subtilis BMT4i (MTCC 9447)

Cited by 4 publications

References 36 publications

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Exploring the bioremediation potential of Bacillus spp. for sustainable mitigation of hydrocarbon contaminants

Purification and characterization of two isoforms of native α amylase from Ok-Rong mango (Mangifera indica Linn. cv. Ok-Rong)

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