A Valuable Product of Microbial Cell Factories: Microbial Lipase

Abstract

As a powerful factory, microbial cells produce a variety of enzymes, such as lipase. Lipase has a wide range of actions and participates in multiple reactions, and they can catalyze the hydrolysis of triacylglycerol into its component free fatty acids and glycerol backbone. Lipase exists widely in nature, most prominently in plants, animals and microorganisms, among which microorganisms are the most important source of lipase. Microbial lipases have been adapted for numerous industrial applications due to their substrate specificity, heterogeneous patterns of expression and versatility (i.e., capacity to catalyze reactions at the extremes of pH and temperature as well as in the presence of metal ions and organic solvents). Now they have been introduced into applications involving the production and processing of food, pharmaceutics, paper making, detergents, biodiesel fuels, and so on. In this mini-review, we will focus on the most up-to-date research on microbial lipases and their commercial and industrial applications. We will also discuss and predict future applications of these important technologies.

Effect of entomopathogenic nematodes Steinernema species (steinernematidae: rhabditida) and Heterorhabditis bacteriophora (heterorhabditidae: rhabditida) on the digestive enzymes and midgut histology of the African migratory locust Locusta migratoria migratorioides (acrididae: orthoptera)

“…The hydrolysis of triacylglycerol into its free fatty acids and glycerol backbone is one of the many reactions that lipase is in charge of (Yao et al 2021). Because X. nematophila or P. luminescens bacteria secrete various secreted enzymes, such as hemolysis, lipases, and proteases that contribute to pathogenicity or nutrient acquisition for the bacterium and its nematode host, lipase activity was dramatically boosted (Richards and Goodrich-Blair 2010).…”

The first detection of two Aeromonas strains in mice of the genus Apodemus

“…M-2 strain exhibited gelatinase-negative, nonmotile, but lecithinase-positive phenotype after 48 h of incubation. Lipase activity was negative on egg yolk agar, but for lipase activity detection more accurate approaches, such as the colorimetric method is recommended 45 . Proteolytic activity was additionally detected in both strains.…”

The Conformational Transitions and Dynamics of Burkholderia cepacia Lipase Regulated by Water–Oil Interfaces

“…As the most established biocatalysts in the synthesis of chemical products and the release of fatty acids for food processing, , lipases are widely applied in industry. Most of the lipases contain the so-called “lid” subdomains located over the active sites that separate the active center from the reaction medium (Figure ).…”

“…Nevertheless, it is great challenge to obtain information about the motions of individual enzyme residues as well the conformational transitions, and to study the relationships between the structural dynamics and transitions with the enzyme activity has proven to be extremely challenging. 19 As the most established biocatalysts in the synthesis of chemical products and the release of fatty acids for food processing, 20,21 lipases are widely applied in industry. Most of the lipases contain the so-called "lid" subdomains located over the active sites that separate the active center from the reaction medium (Figure 1).…”