%0 Journal Article
%@ 2190-572X
%A Kaur , Manpreet
%A Kumar, Rakesh 
%A Katoch, Poonam
%A Gupta, Reena
%D 2023
%F open:3182
%I SPRINGER LINK
%J 3 Biotech
%K  Bacillus subtilis TTP-06; Characterization; MALDI-TOF MS; Native-PAGE; Purification; SDS-PAGE
%N 10
%T Purification and characterization of extracellular lipase from a thermotolerant strain: Bacillus subtilis TTP-06  
%U http://crdd.osdd.net/open/3182/
%V 13
%X 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.    
%Z The copyright of this article belongs to SPRINGER LINK