Positive effect of glycerol on the stability of immobilized enzymes: Is it a universal fact?

Braham, Sabrina Ait; Siar, El Hocine; Arana-Peña, Sara; Bavandi, Hossein; Carballares, Diego; Morellon‐Sterling, Roberto; Andrades, Diandra de; Kornecki, Jakub F.; Fernández-Lafuente, Roberto

doi:10.1016/j.procbio.2020.12.015

Cited by 16 publications

(11 citation statements)

References 106 publications

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“…The concept of green chemistry is intrinsically linked to enzymatic catalysis, as enzymes can be obtained from renewable sources, and are capable of catalyzing various chemical reactions, being an alternative to the classical chemical catalysis 17 – 21 . The ability of enzymes to catalyze multiple distinctly different reactions is referred to as enzyme promiscuity 22 – 24 , Lipases (EC 3.1.1.3, carboxylesterase enzyme) 25 , 26 have previously shown unexpected activities and have been used in organic reactions such as Aldol condensation 27 , Hantzsch reaction 28 , Cannizzaro reaction 29 , Mannich reaction 30 , Baylis–Hillman reaction 31 , Knoevenagel condensation 32 , Michael addition 33 and Ugi reaction 34 .…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic decarboxylative Michael addition for synthesis of 1,4-benzoxazinone derivatives

Bavandi

Shahedi

Habibi

et al. 2022

Sci Rep

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The Candida antarctica lipase B (Novozym 435) is found to catalyze a novel decarboxylative Michael addition in vinylogous carbamate systems for the synthesis of 1,4-benzoxazinone derivatives. The reaction goes through Michael addition, ester hydrolysis and decarboxylation. A possible mechanism is suggested, with simultaneous lipase-catalyzed Michael addition and ester hydrolysis. The present methodology offers formation of complex products through multi-step reactions in a one pot process under mild and facile reaction conditions with moderate to high yields (51–90%) and no side product formation. The reaction seems to be is a great example of enzymatic promiscuity.

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Section: Introductionmentioning

confidence: 99%

Biocatalytic decarboxylative Michael addition for synthesis of 1,4-benzoxazinone derivatives

Bavandi

Shahedi

Habibi

et al. 2022

Sci Rep

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“…The addition of glycerol to the medium significantly stabilized the enzyme, and this was more significant when the glycerol concentration increased (the enzyme retained over 60% of the initial activity after 4 h in 40% glycerol) (Figure 4). This enzyme stabilizing effect of glycerol has been recently examined, and although it is not universal, it is a quite general phenomenon [44]. At 4 • C and in 40% glycerol, the enzyme maintained around 75% of its activity after 4 h (Figure 4).…”

Section: Handling Of Raaeupomentioning

confidence: 86%

“…Both factors may become a problem if the enzyme is unstable at alkaline pH values or it is sensible to reduction. These problems may be partially solved using some stabilizing additives, such as polyols (e.g., glycerol) [41][42][43][44], or by using alternative reducing agents that do not affect the enzyme [45].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of the Peroxygenase from Agrocybe aegerita. The Effect of the Immobilization pH on the Features of an Ionically Exchanged Dimeric Peroxygenase

Carballares

Morellon‐Sterling

et al. 2021

Catalysts

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This paper outlines the immobilization of the recombinant dimeric unspecific peroxygenase from Agrocybe aegerita (rAaeUPO). The enzyme was quite stable (remaining unaltered its activity after 35 h at 47 °C and pH 7.0). Phosphate destabilized the enzyme, while glycerol stabilized it. The enzyme was not immobilized on glyoxyl-agarose supports, while it was immobilized albeit in inactive form on vinyl-sulfone-activated supports. rAaeUPO immobilization on glutaraldehyde pre-activated supports gave almost quantitative immobilization yield and retained some activity, but the biocatalyst was very unstable. Its immobilization via anion exchange on PEI supports also produced good immobilization yields, but the rAaeUPO stability dropped. However, using aminated agarose, the enzyme retained stability and activity. The stability of the immobilized enzyme strongly depended on the immobilization pH, being much less stable when rAaeUPO was adsorbed at pH 9.0 than when it was immobilized at pH 7.0 or pH 5.0 (residual activity was almost 0 for the former and 80% for the other preparations), presenting stability very similar to that of the free enzyme. This is a very clear example of how the immobilization pH greatly affects the final biocatalyst performance.

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“…For example, although it is not yet clear how it works, the glycerol effect on the enzymatic stabilization after immobilization strongly depends on its concentration and pH, and in the case of CaL-B, it represents a cheap alternative as recently described. 43 Novozym 435 is the most widely used immobilized form of CaL-B obtained by the adsorption of CaL-B on a macroporous resin [poly(methyl methacrylate) cross-linked with divinylbenzene]. It was successfully applied in esterification and transesterification reactions in medium containing various solvents, or in SFSs.…”

Section: ■ Introductionmentioning

confidence: 99%

“…To alter the enzyme activity and stability, some additives might be added during the gelification process, including ionic liquids. − Based on the Reetz work, describing the use of polyvinyl alcohol or 18-crown-6 as additives in the entrapment of CaL-B by the sol–gel process, , our study looks into the possibility of using three different polyhydroxy compounds: β-cyclodextrin, polyvinylic alcohol, and glycerol. For example, although it is not yet clear how it works, the glycerol effect on the enzymatic stabilization after immobilization strongly depends on its concentration and pH, and in the case of CaL-B, it represents a cheap alternative as recently described …”

Section: Introductionmentioning

confidence: 99%

Green Process for the Enzymatic Synthesis of Aroma Compounds Mediated by Lipases Entrapped in Tailored Sol–Gel Matrices

Dudu

Lăcătuş

Bencze

et al. 2021

ACS Sustainable Chem. Eng.

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We report a simple enzymatic procedure for the synthesis of short-chained flavor esters by direct esterification of natural acids with short-chain primary alcohols mediated by lipase B from Candida antarctica entrapped in a tailored sol–gel matrix in the presence of three additives, using vacuum for water removal. Maximal immobilization yields (100%) were obtained for all three biocatalysts, while the enzyme loading and the synthetic activity depend on the used additive (6.7, 7.6, and 7.7 μg enzyme/mg biocatalyst for β-cyclodextrin, polyvinyl alcohol, and glycerol, respectively, and 76–110% recovered activity as compared with free lipase). The process was optimized using the reaction of hexan-1-ol with butyric acid as the model with significant conversion improvements (from <40% to >94%) reducing the alcohol/enzyme ratio (from 100:1 to 25:1 weight ratio) for all novel biocatalysts. Other short-chain flavor esters were prepared with excellent yields (>90%) under the previously established optimal conditions. Atom economy (90.53), E-factor (17.22), atom efficiency (88.36), mass intensity (18.58), and reaction mass efficiency (60.07) as relevant sustainability metrics were calculated for the preparative scale model reaction with glycerol as the additive. Based on our results, this green and sustainable new approach can be used for the synthesis of many flavor esters.

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Positive effect of glycerol on the stability of immobilized enzymes: Is it a universal fact?

Cited by 16 publications

References 106 publications

Biocatalytic decarboxylative Michael addition for synthesis of 1,4-benzoxazinone derivatives

Biocatalytic decarboxylative Michael addition for synthesis of 1,4-benzoxazinone derivatives

Immobilization of the Peroxygenase from Agrocybe aegerita. The Effect of the Immobilization pH on the Features of an Ionically Exchanged Dimeric Peroxygenase

Green Process for the Enzymatic Synthesis of Aroma Compounds Mediated by Lipases Entrapped in Tailored Sol–Gel Matrices

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