Production optimization, purification and characterization of α-amylase from thermophilic<i>Bacillus licheniform</i>is TSI-14

Shukla, Rushit J.; Singh, Satya P.

doi:10.1002/star.201500046

Cited by 16 publications

(9 citation statements)

References 36 publications

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“…Concerning its enzymatic potentiality, V. halodenitrificans DASH exhibited positive response to protease, cellulase, lipase and negative results for amylase. The presence of a clear zone formed around the growth was taken as evidence of enzymatic activities [ 21 , 22 , 23 ].…”

Section: Resultsmentioning

confidence: 99%

Carotegenic Virgibacillus halodenitrificans from Wadi El-Natrun Salt Lakes: Isolation, Optimization, Characterization and Biological Activities of Carotenoids

Fayez

Youssif

Sabry

et al. 2022

Biology

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Carotenoids, as phytonutrient pigments, are signified by their unique beneficial features that serve human health and the surrounding ecosystem. Haloalkaliphiles from soda lakes produce different natural bioactive molecules; however, their ability to produce carotenoids has been limited. Therefore, this study focused on the screening and isolation of carotenoid-producing haloalkaliphilic microbes. Out of 10 isolates, a powerful carotigenic bacterium was isolated, characterized phenotypically and identified on the molecular level as Virgibacillus halodenitrificans. By employing statistical approaches like Plackett–Burman design and central composite design, the influence of significant nutritional variables on carotenoids production was screened and optimized. Predictive modeling manifested that carotenoid yield was 36.42 mg/mL, a 2.12-fold enhancement compared to the basal conditions through inoculating 1.8% of bacterial biomass on optimized medium containing yeast extract (2 g/mL), peptone (10 g/mL) and NaCl (233.6 g/mL). The carotenoids content was confirmed by UV-Vis spectrum which detected a characteristic unique peak with left and right shoulders at 461 nm, 490 and 522 nm. However, FTIR and Raman spectroscopy showed the presence of several functional groups. Meanwhile, LC–MS confirmed that the examined carotenoids were composed of β-carotene, lutein and β-Apo-8′-carotenal mixture. As a bioactive agent, the carotenoids of V. halodenitrificans DASH showed characteristic antagonistic potency against a wide spectrum of Gram-positive and Gram-negative pathogens. Interestingly, a potent antifungal capacity was observed against Candida albicans, reflecting promising mycocidal efficacy against COVID-19 white fungal post-infections. Furthermore, carotenoids (20 μg/mL) inhibited the biofilm formation of P. aeruginosa and S. aureus by 54.01 ± 3.97% and 80.082 ± 0.895%, respectively. Our results proposed that haloalkaliphiles of Wadi El-Natrun lakes are promising sources of carotenoids that exhibited efficiency as safe, biocompatible and natural bioactive agents for environmental, medical and industrial applications.

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Section: Resultsmentioning

confidence: 99%

Carotegenic Virgibacillus halodenitrificans from Wadi El-Natrun Salt Lakes: Isolation, Optimization, Characterization and Biological Activities of Carotenoids

Fayez

Youssif

Sabry

et al. 2022

Biology

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“…[18] Further, several Bacillus species with similar temperature range for amylase production has also been reported. [11,12,20] Besides temperature, pH plays a significant role in the growth and enzyme production of microorganisms. Growth and amylase production was studied in the range of pH 5-9; wherein optimum amylase production was observed at pH 7 (Figure 1b).…”

Section: Effect Of Temperature and Phmentioning

confidence: 99%

Purification and Characterization of an Amylase from a Newly Isolated Geobacillus thermoleovorans TTIO4 from the Hot Spring of Tuwa‐Timba

Shukla

Singh

2023

Starch Stärke

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A thermophilic amylase produced by a newly isolated Geobacillus thermoleovorans TTIO4 from a hot spring in India is investigated. The isolate TTIO4 optimally produces extracellular amylase at 55 °C, pH 7, and 24 h of growth. The amylase is purified by 42 fold with a yield of 9.7%. The enzyme has a molecular weight of 40 kDa. The purified amylase catalyzes the reaction optimally at 60 °C and pH 7. Besides, it displays maximum thermal stability at 50 °C for 18 h. While the catalyst is improved by Ca+2, it is wholly inhibited by Hg+2. Furthermore, the chelators, inhibitors and solvents adversely affect the enzyme activity. The amylase is stabilized by SDS, while other surfactants negatively affect the enzyme. Km, Vmax, Kcat, and Kcat/Km of the amylase are 0.26 mg mL−1, 192.3 µg mL−1 min−1, 1.92 s−1, and 7.383 s−1 mg−1, respectively. The deactivation constant, half‐life, and change in Gibb's free energy, enthalpy, and entropy are determined at 50–70 °C, which supports the thermal stability and substrate affinity of the amylase. The washing quality of commercial detergents is distinctly enhanced when supplemented with this enzyme. Therefore, this amylase possesses significant thermal and surfactant stability has significant commercial potential.

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“…The α-amylase secreted by Geobacillus stearothermophilus was purified to homogeneity (65-fold and 46% yield) through a series of steps 20 . Recently, Xie et al 15 have indicated 13.1 purification fold and 7.0% yield, Abdel-Fattah et al 21 have pointed out 59.3 purification fold and 12.6 % yield, and Shukla and Singh 22 have reported 37 purification fold and 16.8% yield using chromatography methods.…”

Section: Purification Of α-Amylasementioning

confidence: 99%

A Novel Raw Starch Hydrolyzing Thermostable α-Amylase Produced by Newly Isolated Bacillus mojavensis SO-10: Purification, Characterization and Usage in Starch Industries

Özdemir

Fincan

Karakaya

et al. 2018

Braz. arch. biol. technol.

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The aim of this study is the production, purification, and characterisation of thermostable raw starch hydrolyzing αamylase produced by Bacillus mojavensis SO-10. The maximum production conditions of α-amylase were found at 36 th hour, 35 °C and pH 7.0. We utilized three steps to purify the thermostable α-amylase and as a result, 34-fold and 18% yield were obtained. The molecular weight of purified α-amylase was determined as 73 kD. The Km and Vmax rates were detected as 0.010 mM and 3.38 µmol min −1 , respectively. This purified α-amylase exhibited the highest activity at pH 5.0-6.0 and 70 ºC and showed stability over a wide variety of pH and temperature at 4.0-8.0, and 40-50 ºC, respectively. The thermostable purified α-amylase exhibited stability in the presence of denaturing agents and heavy metal ions. The purified enzyme hydrolyzed the raw starches of corn and wheat grains in the ratio of 36.7% and 39.2% respectively. The end-yields of soluble starch hydrolysis were analyzed by thin-layer chromatography (TLC). In addition, the usage of purified α-amylase in clarification of apple juice and domestic washing detergent industries were evaluated.

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Production optimization, purification and characterization of α-amylase from thermophilicBacillus licheniformis TSI-14

Cited by 16 publications

References 36 publications

Carotegenic Virgibacillus halodenitrificans from Wadi El-Natrun Salt Lakes: Isolation, Optimization, Characterization and Biological Activities of Carotenoids

Carotegenic Virgibacillus halodenitrificans from Wadi El-Natrun Salt Lakes: Isolation, Optimization, Characterization and Biological Activities of Carotenoids

Purification and Characterization of an Amylase from a Newly Isolated Geobacillus thermoleovorans TTIO4 from the Hot Spring of Tuwa‐Timba

A Novel Raw Starch Hydrolyzing Thermostable α-Amylase Produced by Newly Isolated Bacillus mojavensis SO-10: Purification, Characterization and Usage in Starch Industries

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