Novozym 435: the “perfect” lipase immobilized biocatalyst?

Ortíz, Claudia; Ferreira, Marı́a Luján; Barbosa, Oveimar; Santos, José Cleiton Sousa dos; Rodrigues, Rafael C.; Berenguer-Murcia, Ángel; Briand, Laura E.; Fernández-Lafuente, Roberto

doi:10.1039/c9cy00415g

Cited by 471 publications

(410 citation statements)

References 544 publications

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“…Previous reports revealed that novozym 435 (a commercial immobilized Candida antarctica lipase B on polyacrylic resin) is an efficient catalyst for aza-Michael addition. [32][33][34] Furthermore, novozym 435 exhibits high thermostability in scCO 2. 35,36 Therefore, in this work, a stainless-steel vessel was employed with a working volume of 25 mL, and the aza-Michael addition catalyzed by novozym 435 was performed in scCO 2 (10 MPa) or organic solvents using benzylamine and methyl acrylate as substrates.…”

Section: Resultsmentioning

confidence: 99%

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Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Zhang

Wang

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND Aza‐Michael addition, a powerful method for the synthesis of β‐amino carbonyl derivatives, has been extensively studied in organic chemistry. In this study, the efficient and chemoselective aza‐Michael addition of amines to acrylates catalyzed by lipase in supercritical carbon dioxide (scCO2) was reported for the first time. RESULTS Under the optimal conditions [amine (1 mmol), acrylate (1 mmol), novozym 435 (20 mg), 40 °C, scCO2 (25 mL, 10 MPa)], the corresponding Michael adducts of amines to acrylates were exclusively obtained in high yields (60–93%) for a short reaction time (1 h). No aminolysis was observed when scCO2 was used as reaction medium. Moreover, novozym 435 showed high reusability in scCO2 for aza‐Michael addition. CONCLUSION The excellent chemoselectivity and reusability of novozym 435 in scCO2 indicate the method's great potential for practical application. © 2019 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

“…Previous reports revealed that novozym 435 (a commercial immobilized Candida antarctica lipase B on polyacrylic resin) is an efficient catalyst for aza‐Michael addition . Furthermore, novozym 435 exhibits high thermostability in scCO 2.…”

Section: Resultsmentioning

confidence: 99%

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Zhang

Wang

et al. 2019

J of Chemical Tech & Biotech

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“…CALB was utilized both as lyophilized enzyme and immobilized as Novozym 435. The latter preparation is most commonly employed, both in the laboratory and on industrial scale [43]. BSLA and CALB were produced by expressing the codon-optimized genes in E.coli BL21 (DE3) within pET22b.…”

Section: Bsla Activity In Dry Organic Solventsmentioning

confidence: 99%

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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“…For instance, the lipase B from Candida antarctica immobilized on acrylic resin (Novozyme 435, herein referred to as immobilized CALB) is one of the most applied biocatalysts, used in esterification, transesterification and hydrolysis reactions. Some of these applications have been detailed in a recent review by Fernandez‐Lafuente and co‐workers …”

Section: Lipase‐catalyzed Mechanoenzymatic Reactions By Ball Millingmentioning

confidence: 99%

“…Some of these applications have been detailed in ar ecent review by Fernandez-Lafuente and co-workers. [59] 2.1. CALB-catalyzed resolution of secondary alcohols by acetylation Hernµndez et al reportedt he first mechanochemical reactions catalyzed by immobilizedC ALB without anya queous or organic solvents.…”

Section: Lipase-catalyzed Mechanoenzymatic Reactions By Ball Millingmentioning

confidence: 99%

Mechanoenzymatic Transformations in the Absence of Bulk Water: A More Natural Way of Using Enzymes

2019

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Mechanochemical enzymatic reactions without bulk water have emerged as a low‐waste and efficient method to access useful chemicals and to depolymerize biomass components in a single step. This emergent mechanoenzymatic reaction strategy is able to take advantage of the stereospecificity, regio‐ and stereoselectivity, as well as renewability of enzymes, while avoiding bulk solvents, offering the opportunity to control the direction of the reaction, bypassing reactant solubility issues, and enabling reactions with water‐sensitive substrates or products. Enzymes are traditionally used in dilute aqueous solution, which is quite different from their crowded, water‐depleted natural environment. This review outlines recent work which demonstrates that enzymes can be equally or even more efficient under mechanochemical conditions, without bulk aqueous or organic solvent.

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Novozym 435: the “perfect” lipase immobilized biocatalyst?

Abstract: Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes with its advantages and drawbacks.

Cited by 471 publications

References 544 publications

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Bacillus subtilis Lipase A—Lipase or Esterase?

Mechanoenzymatic Transformations in the Absence of Bulk Water: A More Natural Way of Using Enzymes

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