Investigation of Lipolytic-Secreting Bacteria from an Artificially Polluted Soil Using a Modified Culture Method and Optimization of Their Lipase Production.

Jaisoo Kim,Woojin Chung,Soonwoong Chang,Van Hong Thi Pham

doi:10.3390/microorganisms9122590

Abstract

Compared to lipases from plants or animals, microbial lipases play a vital role in different industrial applications and biotechnological perspectives due to their high stability and cost-effectiveness. Therefore, numerous lipase producers have been investigated in a variety of environments in the presence of lipidic carbon and organic nitrogen sources. As a step in the development of cultivating the unculturable functional bacteria in this study, the forest soil collected from the surrounding plant roots was used to create an artificially contaminated environment for lipase-producing bacterial isolation. The ten strongest active bacterial strains were tested in an enzyme assay supplemented with metal ions such as Ca2+, Zn2+, Cu2+, Fe2+, Mg2+, K+, Co2+, Mn2+, and Sn2+ to determine bacterial tolerance and the effect of these metal ions on enzyme activity. Lipolytic bacteria in this study tended to grow and achieved a high lipase activity at temperatures of 35–40 °C and at pH 6–7, reaching a peak of 480 U/mL and 420 U/mL produced by Lysinibacillus PL33 and Lysinibacillus PL35, respectively. These potential lipase-producing bacteria are excellent candidates for large-scale applications in the future.

Highlights

Lipases, which belong to the family of triacylglycerol ester hydrolase, can catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids without the addition of cofactors [1]
Pure isolates of lipase-producing bacteria were cultured and adjusted to 108 CFU/mL in a medium containing 1% of each type of carbon source, 5 g yeast extract, and 5 g NaCl
In comparison to the traditional medium, the ified medium was considerably efficient in isolating functional bacterial strains under harsh modified medium was considerably efficient in isolating functional bacterial strains unconditions

Summary

Introduction

Lipases, which belong to the family of triacylglycerol ester hydrolase, can catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids without the addition of cofactors [1]. Due to their stability in organic solvents, lipases are listed as the third largest group of commercialized enzymes after protease and carbohydrase [2,3]. Recognized for their significance, lipases have unique characteristics that assist in interacting at the interface between aqueous and non-aqueous media. The presence of oil waste was described as the cause of death of aquatic organisms since oil inhibits the diffusion of oxygen into water

Methods

Results

Discussion

Conclusion