Comparison of lipases and glycoside hydrolases as catalysts in synthesis reactions

Adlercreutz, Patrick

doi:10.1007/s00253-016-8055-x

Cited by 23 publications

(33 citation statements)

References 31 publications

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“…The CALB Novozym 435 produced and immobilized by Novozymes, however, is expressed in Aspergillus oryzae and it is, therefore, glycosylated [44]. Three different aw were tested < 0.1 to establish whether BSLA shows the activity in dry solvent only observed for lipases, with aw = 0.23 as a low value at which most enzymes lose all their activity and aw = 0.75, an activity at which most enzymes are active [10,21,45,46]. To rigorously ascertain these values of the solvent and reagents, including the internal standard, decane and the enzyme preparations were equilibrated via the vapor phase with dried molecular sieves (activated at elevated temperatures, 5 Å) for aw < 0.1 [47].…”

Section: Bsla Activity In Dry Organic Solventsmentioning

confidence: 99%

“…This is seen as a reliable but not decisive criterion [2,9]. (5) The activity of the enzyme in the presence of (water-miscible) organic solvents has been proposed as a property of lipases, but other enzymes fulfill this criterion, too [2,[10][11][12][13][14]. (6) A parameter already investigated some time ago is the activity of lipases in the absence of water, i.e., in modestly polar, water-non-miscible solvents at very low water activities (a w ).…”

Section: Introductionmentioning

confidence: 99%

“…(6) A parameter already investigated some time ago is the activity of lipases in the absence of water, i.e., in modestly polar, water-non-miscible solvents at very low water activities (a w ). Out of all enzymes tested, only lipases and the closely related cutinases are active at low a w [1][2][3][4][5]10,[15][16][17][18][19]. While not all lipases display this property, it is highly distinctive [20,21].…”

Section: Introductionmentioning

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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Section: Bsla Activity In Dry Organic Solventsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Bacillus subtilis Lipase A—Lipase or Esterase?

et al. 2020

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“…This issue has been well explored by Padhi et al, and they proposed the conversion of MAG to fatty acid methyl esters (FAMEs) through transesterification of glycerol using the lipase synthesized from Penicillium camemberti . Adlercreutz has illustrated application of lipases in catalyzing reversed hydrolysis and transesterification reactions and compared their performance with glycoside hydrolases . Other applications include synthesis of sucrose esters using lipases from various sources such as M. meihei by transesterification of sucrose with methanol which have considerable applications in the production of emulsifiers, personal care and cosmetic products .…”

Section: Lipase‐catalyzed Reactionsmentioning

confidence: 99%

“…Adlercreutz has illustrated application of lipases in catalyzing reversed hydrolysis and transesterification reactions and compared their performance with glycoside hydrolases. 37 Other applications include synthesis of sucrose esters using lipases from various sources such as M. meihei by transesterification of sucrose with methanol which have considerable applications in the production of emulsifiers, personal care and cosmetic products. 206 Also, specialty fats were synthesized using interesterification of blends of palm stearin with sal and mango fats using commercial lipozyme TLIM produced from T. lanuginosus.…”

Section: Transesterificationmentioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

302

148

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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On the donor substrate dependence of group‐transfer reactions by hydrolytic enzymes: Insight from kinetic analysis of sucrose phosphorylase‐catalyzed transglycosylation

Klimacek

Sigg

Nidetzky

2020

Biotech & Bioengineering

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Chemical group‐transfer reactions by hydrolytic enzymes have considerable importance in biocatalytic synthesis and are exploited broadly in commercial‐scale chemical production. Mechanistically, these reactions have in common the involvement of a covalent enzyme intermediate which is formed upon enzyme reaction with the donor substrate and is subsequently intercepted by a suitable acceptor. Here, we studied the glycosylation of glycerol from sucrose by sucrose phosphorylase (SucP) to clarify a peculiar, yet generally important characteristic of this reaction: partitioning between glycosylation of glycerol and hydrolysis depends on the type and the concentration of the donor substrate used (here: sucrose, α‐d‐glucose 1‐phosphate (G1P)). We develop a kinetic framework to analyze the effect and provide evidence that, when G1P is used as donor substrate, hydrolysis occurs not only from the β‐glucosyl‐enzyme intermediate (E‐Glc), but additionally from a noncovalent complex of E‐Glc and substrate which unlike E‐Glc is unreactive to glycerol. Depending on the relative rates of hydrolysis of free and substrate‐bound E‐Glc, inhibition (Leuconostoc mesenteroides SucP) or apparent activation (Bifidobacterium adolescentis SucP) is observed at high donor substrate concentration. At a G1P concentration that excludes the substrate‐bound E‐Glc, the transfer/hydrolysis ratio changes to a value consistent with reaction exclusively through E‐Glc, independent of the donor substrate used. Collectively, these results give explanation for a kinetic behavior of SucP not previously accounted for, provide essential basis for design and optimization of the synthetic reaction, and establish a theoretical framework for the analysis of kinetically analogous group‐transfer reactions by hydrolytic enzymes.

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Comparison of lipases and glycoside hydrolases as catalysts in synthesis reactions

Cited by 23 publications

References 31 publications

Bacillus subtilis Lipase A—Lipase or Esterase?

Bacillus subtilis Lipase A—Lipase or Esterase?

Recent advances on sources and industrial applications of lipases

On the donor substrate dependence of group‐transfer reactions by hydrolytic enzymes: Insight from kinetic analysis of sucrose phosphorylase‐catalyzed transglycosylation

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