Relevance of substrates and products on the desorption of lipases physically adsorbed on hydrophobic supports

Virgen-Ortíz, José J.; Tacias-Pascacio, Veymar G.; Hirata, Daniela B.; Torrestiana-Sánchez, Beatriz; Rosales-Quintero, Arnulfo; Fernández-Lafuente, Roberto

doi:10.1016/j.enzmictec.2016.09.010

Cited by 112 publications

(75 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…42,43 The further coating of these biocatalysts with polyethylenimine (PEI) has been reported to prevent one of the main problems of this immobilization protocol: the enzyme release under drastic conditions (high temperatures and organic cosolvents) 54,63 or when used in reactions involving compounds with detergent features (fatty acids, partial glycerides, and even di or monoacetin). [64][65][66] The physical intermolecular crosslinking with PEI reduces this enzyme leakage, 67,68 and it is a step in some coimmobilization strategies. 69 Finally, the loading of the support with the enzyme may be another key factor to ensure that the lipase performance is really derived from the intrinsic properties of the lipases.…”

Section: Introductionmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

View full text Add to dashboard Cite

Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p‐nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl‐CALA was less stable than octyl‐CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl‐CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl‐CALA permitted some stabilization. While octyl‐CALA was more active vs. pNPB, octyl‐CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 35: e2735, 2019

show abstract

Section: Introductionmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

View full text Add to dashboard Cite

show abstract

“…These results may be explained by two factors. On the one hand, a relationship between the substrate concentration and enzyme desorption indicating that a high concentration of substrate forced enzyme leakage, inducing the enzyme instability and inactivation . On the other hand, the amount of naringinase used in this experiment was very limited resulting in incomplete contacts between the enzyme and substrate.…”

Section: Resultsmentioning

confidence: 94%

“…The weak interaction was derived from the decreased number of hydrogen bonds between water and PNIPAAm. The enzyme was desorbed when exposed to low temperatures, which resulted in good desorption via interfacial activation and provided the possibility of reversibility of the immobilization process for further study . Based on these results, a temperature of 25 °C was selected for enzyme desorption in subsequent enzymatic reaction.…”

Section: Resultsmentioning

confidence: 99%

“…On the one hand, a relationship between the substrate concentration and enzyme desorption indicating that a high concentration of substrate forced enzyme leakage, inducing the enzyme instability and inactivation. 28 On the other hand, the amount of naringinase used in this experiment was very limited resulting in incomplete contacts between the enzyme and substrate. However, a high substrate concentration might substantially inhibit the enzyme activity, therefore, a slight decrease in the substrate concentration may result in improved activity.…”

Section: Effect Of Flow Ratesmentioning

confidence: 99%

See 1 more Smart Citation

Enzyme immobilization on photopatterned temperature‐response poly (N‐isopropylacrylamide) for microfluidic biocatalysis

Zhu

Xiong

et al. 2019

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND Microfluidic chips have gained growing attention from the scientific community due to their large surface/interface area and fast mass transfer. However, their application is challenged by the instability of enzymes and time‐consuming catalytic process. Poly (N‐isopropylacrylamide) (PNIPAAm) coupled with photopatterning technology was applied to immobilize an enzyme on the microchannel surface to realize the biotransformation in this study. RESULTS The photopattern‐immobilized naringinase on a microchip achieved a yield of 93.63 ± 1.12% for isoquercitrin production within 5 min. The production of unit time per unit enzyme (g g−1 h−1) increased 2.1‐fold whereas the reaction time decreased to 1/12 of the time required in a batch reactor. The enzyme was absorbed and desorbed at 40 and 25 °C, respectively, and the release efficiency of immobilized naringinase reached 80.57%, indicating that most of the enzymes were replaced with fresh enzymes to proceed each enzymatic reaction. Six cycles of enzymatic hydrolysis reactions were completed successively, maintaining >60% of relative enzymatic activity. CONCLUSION The results indicated that using the immobilized enzyme on the photopatterned PNIPAAm in the enzymatic hydrolysis of rutin was an efficient and simple way to achieve a high yield of isoquercitrin. Thus, this approach represents a convenient and cost‐saving method to produce fine chemicals using microfluidic biocatalysis. © 2019 Society of Chemical Industry

show abstract

“…Nevertheless, there is a particular situation where enzymes become stabilized upon physical immobilization: the immobilization of lipases on hydrophobic supports via interfacial activation, allowing the immobilization, stabilization, purification and hyperactivation of the lipases in just one step [157]. Anyhow, the inherent drawback of this immobilization protocol is caused by the enzyme release from the carrier to the medium, under certain conditions and in the presence of detergent-like molecules [311], reducing the range of reaction conditions where these biocatalysts may be used (Figure 20). This has been solved using different heterofunctional supports, bearing different groups on the support surface with different functions for a better control of the immobilization procedure [312][313][314][315], performing the physical intermolecular crosslinking of the immobilized enzyme using polyethylenimine [316][317][318] or using dexOx as chemical crosslinking reagent [319] (Figure 21).…”

Section: -Use Of Dexox For Intermolecular Crosslinking Of Immobilizedmentioning

confidence: 99%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

View full text Add to dashboard Cite

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.

show abstract

Relevance of substrates and products on the desorption of lipases physically adsorbed on hydrophobic supports

Cited by 112 publications

References 45 publications

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Enzyme immobilization on photopatterned temperature‐response poly (N‐isopropylacrylamide) for microfluidic biocatalysis

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

Contact Info

Product

Resources

About