Isolation, purification and biochemical characterization of a thermophilic alkaline protease from hot water spring bacteria
| Autor: | Ashwini N. Puntambekar, Kiran Bharat Lokhande, Swamy K. Venkateswara, Manjusha S. Dake |
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| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Research Journal of Biotechnology. 17:118-129 |
| ISSN: | 2278-4535 0973-6263 |
| DOI: | 10.25303/1707rjbt1180129 |
| Popis: | Search for a new alkaline and thermostable protease is crucial to explore their industrial applications. Therefore, a thermophilic, alkaliphilic bacteria producing serine alkaline protease was isolated from a hot water spring. Isolated bacteria were identified as B. licheniformis strain 9AkScKu3 as per the results revealed from biochemical studies and 16s rRNA gene sequencing analysis. The purification fold of the enzyme was 23.91 with yield of 18.54%. The purified protease was optimally active at pH 9 and a temperature of 50°C. The enzyme exhibited thermal stability up to 70ºC. Metal ions Ca2+, Mg2+ and Cu2+ enhanced the activity of enzyme. The enzyme exhibited compatibility with 3% surfactants showing more than 100% stability with SDS, tween 20 and triton-x100. Enzyme retained 100% activity with 5% (v/v) H2O2 and organic solvents like toluene and n-hexane at 10% (v/v) concentration. Thus isolated thermophilic alkaline protease is a promising enzyme applicable in detergent formulation. |
| Databáze: | OpenAIRE |
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