Kaur , Manpreet and Kumar, Rakesh and Katoch, Poonam and Gupta, Reena (2023) Purification and characterization of extracellular lipase from a thermotolerant strain: Bacillus subtilis TTP-06. 3 Biotech, 13 (10). ISSN 2190-572X
Full text not available from this repository. (Request a copy)Abstract
In current study, lipase from a thermotolerant Bacillus subtilis TTP-06 was purified in a stepwise manner by using ammonium sulfate precipitation and column chromatography. Thenceforth, it was subjected to sodium dodecyl sulfate- and native-polyacrylamide gel electrophoresis to check the homogeneity of the purified enzyme. The ideal substrate concentration, pH, temperature, reaction duration and lipase specificity were identified. With a yield of 11.02%, purified lipase displayed activity of 8.51 U/mg. Thenceforward, the homogeneously purified enzyme was considered to be a homo-dimer of 30 kDa subunits. Enzyme had Km and Vmax value of 9.498 mM and 19.92 mol mg-1 min-1, respectively. Additionally, the matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) method was used to investigate the purified lipase and estimate its 3-D structure, which revealed a catalytic triad of serine, aspartate and histidine.
| Item Type: | Article |
|---|---|
| Additional Information: | The copyright of this article belongs to SPRINGER LINK |
| Uncontrolled Keywords: | Bacillus subtilis TTP-06; Characterization; MALDI-TOF MS; Native-PAGE; Purification; SDS-PAGE |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 16 Jul 2024 05:26 |
| Last Modified: | 16 Jul 2024 05:26 |
| URI: | http://crdd.osdd.net/open/id/eprint/3182 |
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