Hydrolysis and Formation of Carboxylic Acid Esters

Paravidino, Monica; Böhm, Philipp; Gröger, Harald; Hanefeld, Ulf

doi:10.1002/9783527639861.ch8

Cited by 18 publications

(25 citation statements)

References 334 publications

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“…However, as it was noticed that some lipases did not exhibit this behavior, or only displayed interfacial activation for some specific substrates, other criteria were looked for. The most acknowledged assumes that lipases promote the hydrolysis (and synthesis) of ester bonds with long chain fatty acids (C10 and longer), whereas esterases prefer sshorter chain fatty acids (Jaeger et al, 1999;Paravidino et al, 2012). These carboxyl hydrolases may be required to operate in demanding environments or specific activities may be targeted, in either case paving the way for tapping marine sources, namely through the construction of metagenomic libraries (Jeon et al, 2011).…”

Section: Lipases/esterasesmentioning

confidence: 99%

Marine enzymes and food industry: insight on existing and potential interactions

Fernandes

2014

Front. Mar. Sci.

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Evidence that support the marine environment as source of useful biocatalysts for application in several areas of industry pile up, both as scientific reports or patent applications. Marine microorganisms have to endure habitats characterized by extreme conditions of salinity, temperature or pressure. Their enzymes present concomitant features, viz. thermostability or halostability, which are appealing for practical applications. The food sector is a field where enzymes are used, given their specificity, compliance with strict regulations, relatively mild operational conditions required and environmental friendly nature. The specific features presented by marine enzymes can be advantageously used both for process improvement or to develop new processes and products. In the present review the role of relevant types of enzymes for the food sector is described and recent findings on those enzymes from marine are put into context. The information provided is illustrative that in spite of the relative novelty concerning the use of marine enzymes within the scope of the food sector, some processes have reached commercial status and promising results are being obtained with several others. Moreover, there is still a vast field of resources for enzyme activity to be explored, namely since the screening process that has been considerably improved with the contribution of metagenomic libraries. It can thus be considered that future and exciting developments can be expected concerning the use of marine enzymes in the food and feed areas.

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Section: Lipases/esterasesmentioning

confidence: 99%

Marine enzymes and food industry: insight on existing and potential interactions

Fernandes

2014

Front. Mar. Sci.

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“…This has led to the longstanding question: how can we distinguish between a lipase and an esterase? As the simple hydrolysis of an ester does not suffice, a range of different criteria has been suggested [1][2][3][4][5]. (1) The oldest distinction is the kinetic and structural criterion of interfacial activation, which was already described in 1936 [6].…”

Section: Introductionmentioning

confidence: 99%

“…It is commonly used in organic synthesis and is highly suitable for lipases and also other enzymes with an α/β hydrolase fold. To date, only lipases were shown to be active in toluene with a very low a w [1,3].Catalysts 2019, 9, x FOR PEER REVIEW 2 of 17 interfacially activated nor does it have a lid (criteria one and two) [9,[22][23][24] and sequence data are not conclusive, but it is a minimal α/β hydrolase fold enzyme [9,23,25]. The substrate range clearly qualifies BSLA as a lipase, as does the stability in the presence of solvents [9,[26][27][28][29].…”

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confidence: 99%

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Bacillus subtilis Lipase A—Lipase or Esterase?

et al. 2020

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The question of how to distinguish between lipases and esterases is about as old as the definition of the subclassification is. Many different criteria have been proposed to this end, all indicative but not decisive. Here, the activity of lipases in dry organic solvents as a criterion is probed on a minimal α/β hydrolase fold enzyme, the Bacillus subtilis lipase A (BSLA), and compared to Candida antarctica lipase B (CALB), a proven lipase. Both hydrolases show activity in dry solvents and this proves BSLA to be a lipase. Overall, this demonstrates the value of this additional parameter to distinguish between lipases and esterases. Lipases tend to be active in dry organic solvents, while esterases are not active under these circumstances.Catalysts 2020, 10, 308 2 of 17 lipase A (BSLA) [9]. BSLA is a small (181 amino acids, 19 kDa) serine hydrolase ( Figure 1). It is neither interfacially activated nor does it have a lid (criteria one and two) [9,[22][23][24] and sequence data are not conclusive, but it is a minimal α/β hydrolase fold enzyme [9,23,25]. The substrate range clearly qualifies BSLA as a lipase, as does the stability in the presence of solvents [9,[26][27][28][29]. This stability has even been significantly improved in recent mutational studies and BSLA mutants can be very stable in the presence of water-miscible solvents, such as dimethyl sulfoxide (DMSO), dioxane and trifluoroethanol [30,31]. Studies on BSLA in dry organic solvents are, however, missing. As an experimental parameter, we demonstrate the activity of BSLA in dry toluene. Toluene is not water-miscible and has a logP of 2.5 [32]. It is commonly used in organic synthesis and is highly suitable for lipases and also other enzymes with an α/β hydrolase fold. To date, only lipases were shown to be active in toluene with a very low a w [1,3].Catalysts 2019, 9, x FOR PEER REVIEW 2 of 17 interfacially activated nor does it have a lid (criteria one and two) [9,[22][23][24] and sequence data are not conclusive, but it is a minimal α/β hydrolase fold enzyme [9,23,25]. The substrate range clearly qualifies BSLA as a lipase, as does the stability in the presence of solvents [9,[26][27][28][29]. This stability has even been significantly improved in recent mutational studies and BSLA mutants can be very stable in the presence of water-miscible solvents, such as dimethyl sulfoxide (DMSO), dioxane and trifluoroethanol [30,31]. Studies on BSLA in dry organic solvents are, however, missing. As an experimental parameter, we demonstrate the activity of BSLA in dry toluene. Toluene is not watermiscible and has a logP of 2.5 [32]. It is commonly used in organic synthesis and is highly suitable for lipases and also other enzymes with an α/β hydrolase fold. To date, only lipases were shown to be active in toluene with a very low aw [1,3].

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“…Lipases are frequently used for the transformation of organic compounds because of their stereo-selectivities which can satisfy the growing demand for obtaining optically active compounds 14,15 . Although acylglycerols are the natural substrates of lipases, they can also catalyze the hydrolysis of a wide range of artificial water-insoluble esters with a high degree of enantio-specificity.…”

Section: Introductionmentioning

confidence: 99%