Abstract
Lipolytic enzymes include esterases and lipases that are capable of hydrolyzing and synthesizing ester linkages in triglycerides. These ubiquitous biocatalysts are found in all domains of life. However, the focus of this chapter exclusively covers lipolytic extremozymes from psychro- and (hyper-)thermophiles, while enzymes from mesophilic prokaryotes are not considered. Lipases and esterases from extremophiles display optimal catalytic activity from the freezing point of water up to 100 °C. Due to their tolerance against harsh conditions and their ability to hydrolyze a broad range of natural and non-natural esters, they are considered to be applicable in versatile industry fields. Transesterification reactions of lipases and esterases play an important role in the food industry, whereas the release of free fatty acids is relevant e. g. in the laundry industry aiming at developing cost-efficient and energy-saving washing processes. In addition, lipolytic hydrolases display enantio- and regioselectivity making them highly applicable in the industrial production of pharmaceuticals and other pure compounds. We will review recent developments in the screening and recombinant production of lipolytic extremozymes, and highlight some of the industrial applications.
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Elleuche, S., Schröder, C., Antranikian, G. (2016). Lipolytic Extremozymes from Psychro- and (Hyper-)Thermophilic Prokaryotes and Their Potential for Industrial Applications. In: Rampelotto, P. (eds) Biotechnology of Extremophiles:. Grand Challenges in Biology and Biotechnology, vol 1. Springer, Cham. https://doi.org/10.1007/978-3-319-13521-2_12
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