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A statistical approach for the productionof thermostable and alklophilic alpha-amylase from Bacillusamyloliquefaciens KCP2 under solid-state fermentation

View Article: PubMed Central

ABSTRACT

The bacterial strain producing thermostable, alklophilic alpha-amylase wasidentified as Bacillus amyloliquefaciens KCP2using 16S rDNA gene sequencing data (NCBI Accession No: KF112071). Medium componentswere optimized through the statistical approach for the synthesis of alpha-amylaseby the organism under solid-state fermentation using wheat bran as the substrate.The medium components influencing the enzyme production were identified using atwo-level fractional factorial Plackett–Burman design. Among the various variablesscreened, starch, ammonium sulphate and calcium chloride were found to be mostsignificant medium components. The optimum levels of these significant parameterswere determined employing the response surface Central Composite design whichsignificantly increased the enzyme production with the supplementation of starch0.01 g, ammonium sulphate 0.2 g and 5 mM calcium chloride in the production medium.Temperature and pH stability of the alpha-amylase suggested its wide application inthe food and pharmaceutical industries.

No MeSH data available.


Effect temperature on enzyme activity (a) and stability (b)
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Fig3: Effect temperature on enzyme activity (a) and stability (b)

Mentions: The alpha-amylase produced by B.amyloliquefaciens KCP2 was assessed at different pH and temperatureranges and it was observed that the activity was very low at acidic pH, butincrease in the pH led to gradual increase in enzyme activity. The maximumactivity of the enzyme was observed at pH 8.0 and was found to be highly stable inalkaline pH (Fig. 2a, b). The optimumtemperature for alpha-amylase activity was found to be 65 °C and it showed goodstability in the temperature range of 30–90 °C. More than 85 % of residualactivity was observed in case of temperature ranging from 30 to 70 °C(Fig. 3a, b).Fig. 2


A statistical approach for the productionof thermostable and alklophilic alpha-amylase from Bacillusamyloliquefaciens KCP2 under solid-state fermentation
Effect temperature on enzyme activity (a) and stability (b)
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4362744&req=5

Fig3: Effect temperature on enzyme activity (a) and stability (b)
Mentions: The alpha-amylase produced by B.amyloliquefaciens KCP2 was assessed at different pH and temperatureranges and it was observed that the activity was very low at acidic pH, butincrease in the pH led to gradual increase in enzyme activity. The maximumactivity of the enzyme was observed at pH 8.0 and was found to be highly stable inalkaline pH (Fig. 2a, b). The optimumtemperature for alpha-amylase activity was found to be 65 °C and it showed goodstability in the temperature range of 30–90 °C. More than 85 % of residualactivity was observed in case of temperature ranging from 30 to 70 °C(Fig. 3a, b).Fig. 2

View Article: PubMed Central

ABSTRACT

The bacterial strain producing thermostable, alklophilic alpha-amylase wasidentified as Bacillus amyloliquefaciens KCP2using 16S rDNA gene sequencing data (NCBI Accession No: KF112071). Medium componentswere optimized through the statistical approach for the synthesis of alpha-amylaseby the organism under solid-state fermentation using wheat bran as the substrate.The medium components influencing the enzyme production were identified using atwo-level fractional factorial Plackett–Burman design. Among the various variablesscreened, starch, ammonium sulphate and calcium chloride were found to be mostsignificant medium components. The optimum levels of these significant parameterswere determined employing the response surface Central Composite design whichsignificantly increased the enzyme production with the supplementation of starch0.01 g, ammonium sulphate 0.2 g and 5 mM calcium chloride in the production medium.Temperature and pH stability of the alpha-amylase suggested its wide application inthe food and pharmaceutical industries.

No MeSH data available.