Purification and characterization of lipase by Bacillus methylotrophicus PS3 under submerged fermentation and its application in detergent industry

• Published in: Journal of Genetic Engineering and Biotechnology Vol. 15; no. 2; pp. 369 - 377
• Main Authors: Sharma, Pushpinder, Sharma, Nivedita, Pathania, Shruti, Handa, Shweta
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2017; Academy of Scientific Research and Technology, Egypt; Elsevier
• Subjects: 16s rRNA; ammonium sulfate; Bacillus methylotrophicus Ps3; calcium; carboxylic ester hydrolases; Characterization; chromatography; Detergent; detergents; ethanol; gels; industry; Lipase; magnesium; methanol; Microbial Biotechnology; molecular weight; octoxynol; polyacrylamide gel electrophoresis; Purification; ribosomal RNA; soil; solvents; submerged fermentation; temperature; Characterization; 16s rRNA; Purification; Detergent; Lipase; Bacillus methylotrophicus Ps3
• ISSN: 1687-157X; 2090-5920
• DOI: 10.1016/j.jgeb.2017.06.007

Lipase production bacterial isolate was isolated from soil of service station and identified as Bacillus methylotrophicus PS3 by 16SrRNA with accession number |LN999829.1|. Lipase enzyme was purified by sequential methods of ammonium sulfate precipitation and Sephadex G-100 gel column chromatography. The molecular weight of purified enzyme was 31.40kDa on SDS-PAGE. This purification procedure resulted in 2.90-fold purification of lipase with a 24.10% final yield. The purified lipase presented maximal hydrolytic activity at a temperature of 55°C, and pH of 7.0. Lipase activity was stimulated by Triton X-100 and SDS with Mg2+ and Ca2+ metals employ a positive effect and outlast its stable in organic solvent i.e. methanol and ethanol.