New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase

Arana-Peña, Sara; Mendez-Sanchez, Carmen; Rios, Nathália Saraiva; Ortíz, Claudia; Gonçalves, Luciana Rocha Barros; Fernández-Lafuente, Roberto

doi:10.1016/j.ijbiomac.2019.03.163

Cited by 77 publications

(50 citation statements)

References 71 publications

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“…Moreover, immobilization may affect the activity of the different components in a different way, assuming that they have been optimized by the supplier for its main application, the final combi‐biocatalyst hardly will have optimal activity/stability properties. The use of the individual enzymes may be better for building combi‐biocatalysts, trying to use some of the recent strategies to coimmobilize enzymes that permit the reuse of the most stable enzymes when the least stable ones have been inactivated …”

Section: Resultsmentioning

confidence: 99%

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Stability/activity features of the main enzyme components of rohapect 10L

Magro

Kornecki

Klein

et al. 2019

Biotechnology Progress

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Rohapect 10L is an enzyme cocktail commercialized for juice clarification. Here, we characterized the activity and stability of five enzymatic activities present in this cocktail: total pectinase (PE), polygalacturonase (PG), pectin lyase (PL), pectin methyl esterase (PME), and total cellulase (CE) activities. All these enzyme activities have the maximum activity and stability at pH 4, conditions near those found in most fruit juices. However, if the enzymes need to be handled under different conditions (e.g., to immobilize them), their stability becomes extremely low in some cases, just at pH values slightly higher than the optimal one. For example, at pH 10 only CE was reasonably stable at 25°C, while many other enzyme activities were rapidly almost inactivated, even at 4°C. For these cases, different additives were evaluated, and we found that polyethylene glycol was positive or very positive for all enzyme stabilities, allowing keeping reasonable activities after several hours at pH 10 and 25°C. Another additive, that is, dextran, has a small positive effect for PE, PG, and CE, and a very positive effect for PL, albeit significantly destabilizing PME. Thus, the handling and use of this extract requires some care when is performed out of optimal conditions.

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Section: Resultsmentioning

confidence: 99%

“…The use of the individual enzymes may be better for building combibiocatalysts, trying to use some of the recent strategies to coimmobilize enzymes that permit the reuse of the most stable enzymes when the least stable ones have been inactivated. 26,27,91,92…”

Section: Discussionmentioning

confidence: 99%

Stability/activity features of the main enzyme components of rohapect 10L

Magro

Kornecki

Klein

et al. 2019

Biotechnology Progress

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“…Enzyme co-immobilization requires adequate immobilization methods considering a judicious selection of the support and mechanism of immobilization, and a thorough characterization of the enzymes and the kinetics of the reactions involved (Arana-Peña et al, 2019;El-Zahab, Meza, Cutright, & Wang, 2004;Hwang & Lee, 2019;Lopez-Gallego & Schmidt-Dannert, 2010;Ren et al, 2019;Sun et al, 2014;Torres & Batista-Viera, 2019;Yang, Dai, Wei, Zhu, & Zhou, 2019). It is expected that the activity of the enzymes can be preserved during co-immobilization while increasing their stability, hopefully attaining similar operational half-life values of each enzyme partner (Betancor & Luckarift, 2010).…”

Section: Enzymes Co-immobilizationmentioning

confidence: 99%

Biocatalysis in the winemaking industry: Challenges and opportunities for immobilized enzymes

Ottone

Romero

Aburto

et al. 2020

Comp Rev Food Sci Food Safe

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Enzymes are powerful catalysts already being used in a large number of industrial processes. Impressive advantages in enzyme catalysts improvement have occurred in recent years aiming to improve their performance under harsh operation conditions far away from those of their cellular habitat. Production levels of the winemaking industry have experienced a remarkable increase, and technological innovations have been introduced for increasing the efficiency at different process steps or for improving wine quality, which is a key issue in this industry. Enzymes, such as pectinases and proteases, have been traditionally used, and others, such as glycosidases, have been more recently introduced in the modern wine industry, and many dedicated studies refer to the improvement of enzyme performance under winemaking conditions. Within this framework, a thorough review on the role of enzymes in winemaking is presented, with special emphasis on the use of immobilized enzymes as a significant strategy for catalyst improvement within an industry in which enzymes play important roles that are to be reinforced paralleling innovation.

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“…However, it also involves some drawbacks, such as the decrease in the relative loading capacity of the support for each enzyme, the dependence of the overall stability of the whole biocatalyst on the particular stability of the less stable component of this combined catalyst, and the need to use the same immobilization technique for all enzymes [167]. Therefore, some new coimmobilization strategies are being studied [301][302][303][304]; one of the solutions proposed for the first above-mentioned problem involves the use of dexOx (Figure 19.) In fact, dexOx was used to coimmobilize tetrameric β-D-galactosidase from Kluyveromyces lactis [305,306] and the lipase from Thermomyces lanuginosus previously immobilized on hydrophobic magnetic nanoparticles [307]; after lipase immobilization, the enzyme was chemically aminated and thereafter, the lactase was coimmobilized via ion exchange on the aminated enzyme.…”

Section: Enzyme Coimmobilization Using Dexox As Gluementioning

confidence: 99%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

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Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1,2-diol moiety inside dextran, is a polymer that is very useful in many areas, including as a macromolecular carrier for drug delivery and other biomedical applications. In particular, it has been widely used for chemical engineering of enzymes, with the aim of designing better biocatalysts that possess improved catalytic properties, making them more stable and/or active for different catalytic reactions. This polymer possesses a very flexible hydrophilic structure, which becomes inert after chemical reduction; therefore, dexOx comes to be highly versatile in a biocatalyst design. This paper presents an overview of the multiple applications of dexOx in applied biocatalysis, e.g., to modulate the adsorption of biomolecules on carrier surfaces in affinity chromatography and biosensors design, to serve as a spacer arm between a ligand and the support in biomacromolecule immobilization procedures or to generate artificial microenvironments around the enzyme molecules or to stabilize multimeric enzymes by intersubunit crosslinking, among many other applications.

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New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase

Cited by 77 publications

References 71 publications

Stability/activity features of the main enzyme components of rohapect 10L

Stability/activity features of the main enzyme components of rohapect 10L

Biocatalysis in the winemaking industry: Challenges and opportunities for immobilized enzymes

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

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