Bacterial lipases: an overview of production, purification and biochemical properties

Bacterial lipases: an overview of production, purification and biochemical properties

25 August 2003 / Revised: 22 December 2003 / Accepted: 22 December 2003 / Published online: 14 February 2004 | R. Gupta · N. Gupta · P. Rathi
The chapter provides an overview of bacterial lipases, emphasizing their production, purification, and biochemical properties. Lipases, or triacylglycerol hydrolases, are biotechnologically significant enzymes with applications in food, dairy, detergent, and pharmaceutical industries. They are primarily produced by microorganisms, particularly from genera such as *Bacillus*, *Pseudomonas*, and *Burkholderia*. Lipases are typically extracellular and produced through submerged fermentation using lipidic carbon sources like oils, fatty acids, and glycerol. The enzyme is commonly purified using hydrophobic interaction chromatography and modern techniques like reverse micellar and aqueous two-phase systems. Lipases exhibit a wide pH and temperature range, with alkaline lipases being more common. They are serine hydrolases with high stability in organic solvents and can show chemo-, regio-, and enantioselectivity. Recent research focuses on developing novel lipases through molecular approaches such as directed evolution and metagenomics. The chapter also discusses the sources of lipases, fermentation conditions, and the importance of these enzymes in various biotechnological applications.The chapter provides an overview of bacterial lipases, emphasizing their production, purification, and biochemical properties. Lipases, or triacylglycerol hydrolases, are biotechnologically significant enzymes with applications in food, dairy, detergent, and pharmaceutical industries. They are primarily produced by microorganisms, particularly from genera such as *Bacillus*, *Pseudomonas*, and *Burkholderia*. Lipases are typically extracellular and produced through submerged fermentation using lipidic carbon sources like oils, fatty acids, and glycerol. The enzyme is commonly purified using hydrophobic interaction chromatography and modern techniques like reverse micellar and aqueous two-phase systems. Lipases exhibit a wide pH and temperature range, with alkaline lipases being more common. They are serine hydrolases with high stability in organic solvents and can show chemo-, regio-, and enantioselectivity. Recent research focuses on developing novel lipases through molecular approaches such as directed evolution and metagenomics. The chapter also discusses the sources of lipases, fermentation conditions, and the importance of these enzymes in various biotechnological applications.
Reach us at info@study.space