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Polyextremotolerant Amylase Produced from Novel Enterococcus with Potpourri of Applications

  • Haritha MeruvuEmail author
Article
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Abstract

Amylolytic toluene-tolerant Enterococcus faecalis mercadA7 isolated from asbestos contaminated black soil from the Tokat province of Turkey was used for statistically optimized liquid phase fermentation to spawn elevated levels of amylase. Box Behnken technique of Response surface Methodology is followed to optimize three significant factors influencing Amylase production. To purify the amylase, ammonium sulfate fractionation, dialysis and gel filtration on Sephadex G-100 column chromatography were used. Submerged state fermentation at statistically optimized conditions augmented amylase production levels (8467 U ml−1) 8.74-fold compared to the conventional optimization. Purified amylase was found to possess specific activity of 1022 U mg−1, optimal activity at pH 9 and 60 °C, 80% stable at 8.0–10.0 pH range and 90% stable at 45–75 °C for 1 h; with Km value of 8.06 mg ml−1 and a Vmax of 4.36 mmol h−1 ml−1, noteworthy stability up to 43% toluene, and upto 8% NaCl. High titers of Amylase produced from Enterococcus faecalis mercadA7 might find applications in copious industrial processes due to noteworthy stability of the cell-free purified enzyme at elevated temperatures, alkaline, and high toluene or salt concentrated environments.

Keywords

Amylase Toluene Enterococcus faecalis mercadA7 Purification Characterization 

Notes

Funding

Financial assistance by TUBITAK, The Scientific and Technological Research Council of Turkey Grants Scholarships for 2216—Research Fellowship Program for International Researchers program (2015–2016), Grant Number: 21514107-115.99-129944 is deeply acknowledged by recipient Dr. Haritha Meruvu (Postdoctoral Research Scientist).

Compliance with Ethical Standards

Conflict of interest

The author declares no conflict of interest.

Research Involving Human Participants and/or Animals

No humans or animals are used or involved; no ethical issues, this work is done by the sole and corresponding author.

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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Department of BioEngineering, Faculty of Engineering and Natural SciencesGaziosmanpasa UniversityTokatTurkey
  2. 2.Department of Chemical Engineering, AU College of Engineering, Center for BiotechnologyAndhra UniversityVisakhapatnamIndia

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