Physico-chemical properties, kinetic parameters, and glucose inhibition of several beta-glucosidases for industrial applications

Andrades, Diandra de; Graebin, Natália G.; Ayub, Marco Antônio Záchia; Fernández-Lafuente, Roberto; Rodrigues, Rafael C.

doi:10.1016/j.procbio.2019.01.008

Cited by 16 publications

(16 citation statements)

References 57 publications

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“…Compared with the free enzyme, immobilized enzyme can be easily separated from reaction solution and reused, which greatly decreased the cost of the enzyme under practical application [39‐, 40]. In this study, the M‐MWCNs‐PPL could be recovered by magnetic separation easily, washed with cold diethyl ether, and then reused directly.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of substituted 2H‐chromenes catalyzed by lipase immobilized on magnetic multiwalled carbon nanotubes

Liu

Zhao

Zhang

et al. 2020

Biotech and App Biochem

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Porcine pancreas lipase (PPL) was immobilized on magnetic multiwalled carbon nanotubes successfully for the synthesis of substituted 2H‐chromenes. The catalytic activity of immobilized PPL was much higher than that of free PPL. Effects of reaction medium, temperature, and enzyme dosage were also investigated. Under optimum reaction conditions (acetylacetone (1 mmol), salicylaldehyde (1 equivalent), methanol (10 equivalent), and immobilized PPL (protein content: 30 mg; 65 °C; DMF 5 mL; 5 H), the immobilized PPL showed an excellent catalytic performance on the synthesis of substituted 2H‐chromenes. Moreover, the immobilized PPL exhibited satisfactory thermostability, operational simplicity, and reusability in this reaction.

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Section: Resultsmentioning

confidence: 99%

Synthesis of substituted 2H‐chromenes catalyzed by lipase immobilized on magnetic multiwalled carbon nanotubes

Liu

Zhao

Zhang

et al. 2020

Biotech and App Biochem

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“…One condition that will always change during the process is the ratio between the concentrations of substrate and reaction product. Furthermore, in many instances, the enzymes may be inhibited by the reaction product [101][102][103][104][105][106][107][108]. That way, it is possible that one specific enzyme can exhibit an optimal performance in the absence of product or if the concentration of substrate is much higher than the concentration of the product, but it may suffer a strong inhibition due to its presence, stopping the reaction long before reaching the total modification of the substrate even when this may be thermodynamically feasible [109] (Figure 2).…”

Section: Modification Of Monofunctional Substratesmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

Self Cite

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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“…One strategy to facilitate the effective β-glucosidase implementation is the design and implementation of the enzyme in the format of enzyme-immobilized preparations [17,18]. Enzyme immobilization is an enabling technology that facilitates enzyme handling, permits its cyclic reuse and continuous use, and, if properly designed, might contribute to increasing the operational stability of the enzyme [19,20].…”

Section: Introductionmentioning

confidence: 99%

“…Studies mainly involve the immobilization into preexisting materials and the evaluation of the influence of the material supports in the interplay with different immobilization chemistries. Catalytic properties as recovered activity and stability were evaluated [18][19][20][21][22][23][24][25][26]. Active immobilization by adsorption (anion exchange based ionic adsorption) or covalent binding (via aldehyde chemistry) to porous material supports have been shown as a promising strategy to obtain active and stable catalysts of different βglucosidases.…”

Section: Introductionmentioning

confidence: 99%

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

Alvarez-Gonzalez¹,

Santos²,

Ladero³

et al. 2022

Catalysts

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Cellulose saccharification to glucose is an operation of paramount importance in the bioenergy sector and the chemical and food industries, while glucose is a critical platform chemical in the integrated biorefinery. Among the cellulose degrading enzymes, β-glucosidases are responsible for cellobiose hydrolysis, the final step in cellulose saccharification, which is usually the critical bottleneck for the whole cellulose saccharification process. The design of very active and stable β-glucosidase-based biocatalysts is a key strategy to implement an efficient saccharification process. Enzyme immobilization and reaction engineering are two fundamental tools for its understanding and implementation. Here, we have designed an immobilized-stabilized solid-supported β−glucosidase based on the glyoxyl immobilization chemistry applied in porous solid particles. The biocatalyst was stable at operational temperature and highly active, which allowed us to implement 25 °C as working temperature with a catalyst productivity of 109 mmol/min/gsupport. Cellobiose degradation was implemented in discontinuous stirred tank reactors, following which a simplified kinetic model was applied to assess the process limitations due to substrate and product inhibition. Finally, the reactive process was driven in a continuous flow fixed-bed reactor, achieving reaction intensification under mild operation conditions, reaching full cellobiose conversion of 34 g/L in a reaction time span of 20 min.

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Physico-chemical properties, kinetic parameters, and glucose inhibition of several beta-glucosidases for industrial applications

Cited by 16 publications

References 57 publications

Synthesis of substituted 2H‐chromenes catalyzed by lipase immobilized on magnetic multiwalled carbon nanotubes

Synthesis of substituted 2H‐chromenes catalyzed by lipase immobilized on magnetic multiwalled carbon nanotubes

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

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