title: Purification and characterization of extracellular lipase from a thermotolerant strain: Bacillus subtilis TTP-06  
creator: Kaur , Manpreet
creator: Kumar, Rakesh 
creator: Katoch, Poonam
creator: Gupta, Reena
subject: QR Microbiology
description: 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.    
publisher: SPRINGER LINK
date: 2023-10
type: Article
type: PeerReviewed
relation: https://link.springer.com/article/10.1007/s13205-023-03717-6
identifier:   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     
relation: http://crdd.osdd.net/open/3182/