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|Title:||Production and eco friendly application of alkaline protease from Bacillus amyloliquifaciens sp1|
Shirkot, C K
|Keywords:||Alkaline protease;Bacillus amyloliquefaciens;Silver release;X-ray films;Thermostabilty|
|Abstract:||Alkaline protease from Bacillus amyloliquefaciens SP1 has been characterized in detail for its ecofriendly application of release of silver particles from gelatin layers of used X-ray films. It exhibited optimum activity at broad temperature range and maximum at 60⁰C under alkaline pH environment (8-12). Thermal inactivation of the crude enzyme followed ﬁrst order kinetics. The half-life of the enzyme at 50, 60 and 65⁰C was 70, 15 and 12.6 min, respectively and the denaturation energy was 114.87 kJ/mol. Enzyme retained 53.83 and 108.33% of its initial activity after heating for 15 min at pH 8.0 and temperature 60⁰C, in presence and absence of 10 mM MnSO4, respectively. Enzymatic decomposition of gelatin layers was enhanced by increase of enzyme concentration from 38 to 3630 µg/ml/min, at 60⁰C and pH 8.0. This study reported the shortest time of 1.30 min at 3630 µg/ml/min and 4 : 30 min at 74 µg/ml/min of enzyme concentration for hydrolysis of gelatin layers. Keeping in mind that, nowadays recycling is needed and imperative, this is the first study to report that after addition of Mn2+ ions, thermal stability of enzyme increased and it could be effectively reused for 8 cycles as compared with enzyme without protective agents which also increase its yield of silver recovery i.e. 19.56 ± 0.78% by eight times.|
|ISSN:||0975-0967 (Online); 0972-5849 (Print)|
|Appears in Collections:||IJBT Vol.17(3) [July 2018]|
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