A<i>Bacillus acidocaldarius</i><i>α</i>-Amylase That is Highly Stable to Heat under Acidic Conditions

Kanno, Mutsuo

doi:10.1080/00021369.1986.10867330

Cited by 4 publications

(4 citation statements)

References 3 publications

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“…Cu 2+ has been reported to inhibit the activity of amylases from B. circulans ( Takasaki 1982), B. coagulans ( Babu and Satyanarayana 1993) and B. licheniformis ( Krishnan and Chandra 1983). The occurrence of calcium‐independent amylases was reported in B. circulans ( Takasaki 1982), B. acidocaldarius ( Kanno 1986) and B. brevis ( Tsvetkov and Emanuilova 1989).…”

Section: Discussionmentioning

confidence: 99%

Production and partial characterization of thermostable and calcium-independent alpha-amylase of an extreme thermophile Bacillus thermooleovorans NP54

Malhotra

Noorwez

Satyanarayana

2000

Lett Appl Microbiol

131

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Aim: An investigation was carried out on the production of a-amylase by Bacillus thermooleovorans NP54, its partial puri®cation and characterization. Methods and Results: The thermophilic bacterium was grown in shake¯asks and a laboratory fermenter containing 2% soluble starch, 0Á3% tryptone, 0Á3% yeast extract and 0Á1% K 2 HPO 4 at 70 C and pH 7Á0, agitated at 200 rev min À1 with 6-h-old inoculum (2% v/v) for 12 h. When the enzyme was partially puri®ed using acetone (80% [v/v] saturation), a 43Á7% recovery of enzyme with 6Á2-fold puri®cation was recorded. The K M and V max (soluble starch) values were 0Á83 mg ml À1 and 250 mmol mg À1 protein min À1 , respectively. The enzyme was optimally active at 100 C and pH 8Á0 with a half-life of 3 h at 100 C. Both a-amylase activity and production were Ca 2 independent. Conclusions: Bacillus thermooleovorans NP54 produced calcium-independent and thermostable a-amylase. Signi®cance and Impact of the Study: The calcium-independent and thermostable aamylase of B. thermooleovorans NP54 will be extremely useful in starch sacchari®cation since the a-amylases used in the starch industry are calcium dependent. The use of this enzyme in starch hydrolysis eliminates the use of calcium in starch liquefaction and subsequent removal by ion exchange.

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Section: Discussionmentioning

confidence: 99%

Production and partial characterization of thermostable and calcium-independent alpha-amylase of an extreme thermophile Bacillus thermooleovorans NP54

Malhotra

Noorwez

Satyanarayana

2000

Lett Appl Microbiol

131

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“…Cu 2+ has been reported to inhibit the amylase activity of B. circulans [25], Bacillus coagulans [29] and B. licheniformis [26]. The occurrence of Ca 2+ -independent amylase has been reported in B. circulans [31], Bacillus acidocaldarius [30] and Bacillus brevis [31]. Ba 2+ exhibited a positive effect on the enzyme activity as reported in the thermophilic fungus Thermomyces lanuginosus strain ATCC 34626 [32].…”

Section: Resultsmentioning

confidence: 92%

“…Molecular weight of the purified enzyme was determined using a SDS-PAGE and native polyacrylamide gel electrophoresis (PAGE) (10% polyacrylamide gel). The purified protein (10 μg/ ml) was run along with medium molecular weight protein markers: phosphorylase (97), albumin (66), ovalbumin (45), carbonic anhydrase (30), trypsin inhibitor (20.1), and α-lactalbumin (14.4) (obtained from Pharmacia Biotech). The activity was demonstrated by native PAGE containing 1.0% soluble starch in 10% gel.…”

Section: Sds-page and Molecular Mass Determinationmentioning

confidence: 99%

Purification and Characterization of a Hyperthermostable and High Maltogenic α-Amylase of an Extreme Thermophile Geobacillus thermoleovorans

Rao

Satyanarayana

2007

Appl Biochem Biotechnol

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Synthetic dyes are released into the environment from textile industrial effluents. The discharge of this colored wastewater into rivers and lakes leads to a reduction in sunlight penetration in natural water bodies, which, in turn, decreases both photosynthetic activity and dissolved oxygen concentration and is toxic to living beings. Bacterial isolates are optimized for growth and biomass production before using them for decolorizing dye effluent. The bacterial isolates Bacillus sp. 1 and Bacillus sp. 2 were employed at different percentages by volume with standard nutrient concentration. Of these bacterial isolates Bacillus sp. 2 recorded maximum color reduction. The pH and electrical conductivity (EC) were reduced in the decolorized effluent, and a reduction in biologic oxygen demand, chemical oxygen demand, total suspended solids, and total dissolved solids (TDS) were also observed.

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“…with Ca-independency properties of thermal stability [27]. The occurrence of calcium-independent amylases was also reported in Bacillus circulans [28], Bacillus acidocaldarius [29], Bacillus brevis [30] and Bacillus thermooleovorans NP54. Furthermore, the thermostability of a calcium-free α-amylase from an alkalophilic Bacillus sp.…”

Section: Thermostability As Measured By Calcium Dependencymentioning

confidence: 93%

Engineering of a Bacillus α-Amylase with Improved Thermostability and Calcium Independency

Ghollasi

Khajeh

Naderi-Manesh

et al. 2010

Appl Biochem Biotechnol

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Successful industrial use of amylases requires that they are sufficiently stable and active at application conditions, e.g., at high temperature in starch-liquefaction process. In the present study, site-directed mutagenesis was used to enhance the thermal stability and calcium independency of a mesophilic alpha-amylase from Bacillus megaterium WHO. Mutations (A53S and H58I) were designed at the calcium-binding site based on the sequence alignment. Kinetic and thermostability parameters of the mutants were analyzed and compared with that of the wild type. In the presence of calcium, the affinity of the enzymes (wild type and mutants) toward starch was increased. In comparison to the wild type, calcium ion had more effect on the catalytic efficiency, k (cat)/K (m), and half-life (at 60 degrees C) of A53S mutant. In A53S, the dependence of half-life on calcium concentration showed that the enhanced calcium binding is likely to be responsible for the increased stability. In contrast, calcium-independent mutant (H58I) possessed high thermostability. In addition, thermodynamic parameters of amylolytic reaction exhibited an increase in the activation energy and the entropy of the system. Kinetics of irreversible thermal inactivation suggests that the activation energy increased by 1.4-fold in the most stable variant.

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ABacillus acidocaldariusα-Amylase That is Highly Stable to Heat under Acidic Conditions

Cited by 4 publications

References 3 publications

Production and partial characterization of thermostable and calcium-independent alpha-amylase of an extreme thermophile Bacillus thermooleovorans NP54

Production and partial characterization of thermostable and calcium-independent alpha-amylase of an extreme thermophile Bacillus thermooleovorans NP54

Purification and Characterization of a Hyperthermostable and High Maltogenic α-Amylase of an Extreme Thermophile Geobacillus thermoleovorans

Engineering of a Bacillus α-Amylase with Improved Thermostability and Calcium Independency

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