Archaeal lipolytic enzymes: Current developments and further prospects
Lipolytic enzymes include triacylglycerol lipases (EC 3.1.1.3) and esterases (EC 3.1.1.1) that catalyze the cleavage and formation of ester bonds. They are potential industrial biocatalysts because of their broad range of activities on natural and synthetic substrates, high stability in organic solv...
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Published in | Biotechnology advances Vol. 61; p. 108054 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
01.12.2022
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Subjects | |
Online Access | Get full text |
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Summary: | Lipolytic enzymes include triacylglycerol lipases (EC 3.1.1.3) and esterases (EC 3.1.1.1) that catalyze the cleavage and formation of ester bonds. They are potential industrial biocatalysts because of their broad range of activities on natural and synthetic substrates, high stability in organic solvents, thermal stability, stability in highly acidic and alkaline pH conditions and enantio-, regio- and chemo-selectivity. They also have varied applications in different sectors, among which industrial biotechnology, the production of cleaning agents, and pharmaceuticals are the most important ones. Identifying extremophilic lipolytic enzymes is of paramount interest and is a growing field in academic and industrial research. This review is focused on the current knowledge and future avenues of investigation on lipolytic enzymes sourced from the underexploited archaeal domain. Archaea is a potential source for novel extremophilic enzymes, which have high demand in the industries. The archaeal lipases and esterases are clustered into different families based on their similarity/dissimilarity at the genetic level and protein structures. The updated information on characterized and putative lipase sequences has also been presented in this paper. Common structural scaffolds of archaeal lipases have been deduced and discussed in this review. However, huge diversity at the level of their genetic sequences has yet to be correlated with the structure-function relationship. Based on their biochemical properties, possible applications and future prospective of archaeal lipolytic enzymes have also been proposed. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0734-9750 1873-1899 1873-1899 |
DOI: | 10.1016/j.biotechadv.2022.108054 |