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Lipase And Esterase - To What Extent Can This Classification Be Applied Accurately? [lipases E Esterases: Como Definir E Classificar?]

TLDR
In this paper, specific lipase and esterase activities of five enzymes were investigated and compared in the presence of natural and synthetic substrates, and the results indicated that a new and broader definition of lipases may be necessary.
Abstract
Enzyme technology is an ever-growing field of knowledge and, in recent years, this technology has raised renewed interest, due to the search for new paradigms in several productive processes. Lipases, esterases and cutinases are enzymes used in a wide range of processes involving synthesis and hydrolysis reactions. The objective of this work was to investigate and compare the specific lipase and esterase activities of five enzymes – four already classified as lipases and one classified as cutinase - in the presence of natural and synthetic substrates. All tested enzymes presented both esterase and lipase specific activities. The highest specific esterase activity was observed for Aspergillus 1068 lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate, while the highest specific lipase activity was observed for Geotrichum sp. lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate. These results display some interface-independent lipolytic activity for all lipases tested. This is in accordance with the rationale that a new and broader definition of lipases may be necessary.

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Enzymatic modification of polysaccharides: Mechanisms, properties, and potential applications: A review.

TL;DR: This review discusses the methods of enzymatic functionalization of four well-known polysaccharides, chitosan, cellulose, pectin and starch, and the enzymes implicated in the modification such as laccases, peroxidases lipases, tyrosinases, and transglutaminases.
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A review on the important aspects of lipase immobilization on nanomaterials

TL;DR: The recent developments, some mechanisms, and influence of NMs on lipase immobilization and their activity are discussed, and multiple application potential of the immobilized lipases has also been considered.
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Effects of Aspergillus species inoculation and their enzymatic activities on the formation of volatile components in fermented soybean paste (doenjang)

TL;DR: The lipase activity was strongly correlated with the formation of long-chain fatty acid esters, which could be related to the distinctive organoleptic properties of rice-koji doenjang.
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Orange and mango by-products: Agro-industrial waste as source of bioactive compounds and botanical versus commercial description—A review

TL;DR: The current review sought to contextualize such a scenario by gathering definitions, relevant information and studies on agro-industrial wastes and by-products, international enzymes market, and recent studies on bioactive compounds.
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Biodeterioration of epoxy resin: a microbial survey through culture-independent and culture-dependent approaches.

TL;DR: This investigation provides new information on the potential microfloral inhabitants of epoxy resin discovering a new ecological niche, occupied mainly by several members of rock-colonizing microbial species.
References
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The α/β hydrolase fold

TL;DR: The alpha/beta hydrolase fold as mentioned in this paper is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function, including the serine protease catalytic triad.
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Microbial carboxyl esterases: classification, properties and application in biocatalysis

TL;DR: Esterases represent a diverse group of hydrolases catalyzing the cleavage and formation of ester bonds and are widely distributed in animals, plants and microorganisms and special emphasis is given on their application in organic synthesis for the resolution of racemates and prostereogenic compounds.
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Alpha Beta-Hydrolase Fold Enzymes Structures, Functions and Mechanisms

TL;DR: An overview of catalytic activities reported for the alpha/beta-hydrolase fold family of enzymes is given by discussing selected examples and the current state of knowledge of the molecular basis for catalysis and substrate specificity is outlined.
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Interfacial Enzyme Kinetics of Lipolysis

Robert Verger
TL;DR: The growing interest in the mechanisms controlling membrane-bound enzymes has incited a number of biochemists to study in more detail certain aspects of heterogeneous catalysis, and it will come as no surprise that most of the work reported so far deals with lipolysis.
Journal ArticleDOI

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

TL;DR: An improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained, and 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved.
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