@article{open3182,
          volume = {13},
          number = {10},
           month = {October},
          author = {Manpreet Kaur  and Rakesh  Kumar and Poonam Katoch and Reena Gupta},
            note = {The copyright of this article belongs to SPRINGER LINK},
           title = {Purification and characterization of extracellular lipase from a thermotolerant strain: Bacillus subtilis TTP-06
},
       publisher = {SPRINGER LINK},
            year = {2023},
         journal = {3 Biotech},
        keywords = { Bacillus subtilis TTP-06; Characterization; MALDI-TOF MS; Native-PAGE; Purification; SDS-PAGE},
             url = {http://crdd.osdd.net/open/3182/},
        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.

}
}