Significant Enhancement of Structural Stability of the Hyperhalophilic ADH from<i>Haloferax volcanii</i>via Entrapment on Metal Organic Framework Support

Carucci, Cristina; Bruen, Larah; Gascón, Victoria; Paradisi, Francesca; Magner, Edmond

doi:10.1021/acs.langmuir.8b01037

Cited by 26 publications

(22 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzyme specificity, stability and tolerance to organic solvents were systematically studied. With this in situ approach, unlike other immobilization methods, the biocatalyst resulted in increased stability over a wider range of pH and temperature with retention of activity upon reuse of up to 4 cycles [69]. Electrostatic interactions between the halophilic enzyme and the Fe-BTC MOF might explain the enhancement in activity and decrease in halophilicity of the immobilized enzyme.…”

Section: Semiamorphous Fe-btcmentioning

confidence: 99%

See 1 more Smart Citation

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

et al. 2021

View full text Add to dashboard Cite

The industrial use of enzymes generally necessitates their immobilization onto solid supports. The well-known high affinity of enzymes for metal-organic framework (MOF) materials, together with the great versatility of MOFs in terms of structure, composition, functionalization and synthetic approaches, has led the scientific community to develop very different strategies for the immobilization of enzymes in/on MOFs. This review focuses on one of these strategies, namely, the one-pot enzyme immobilization within sustainable MOFs, which is particularly enticing as the resultant biocomposite Enzyme@MOFs have the potential to be: (i) prepared in situ, that is, in just one step; (ii) may be synthesized under sustainable conditions: with water as the sole solvent at room temperature with moderate pHs, etc.; (iii) are able to retain high enzyme loading; (iv) have negligible protein leaching; and (v) give enzymatic activities approaching that given by the corresponding free enzymes. Moreover, this methodology seems to be near-universal, as success has been achieved with different MOFs, with different enzymes and for different applications. So far, the metal ions forming the MOF materials have been chosen according to their low price, low toxicity and, of course, their possibility for generating MOFs at room temperature in water, in order to close the cycle of economic, environmental and energy sustainability in the synthesis, application and disposal life cycle.

show abstract

Section: Semiamorphous Fe-btcmentioning

confidence: 99%

“…Other reports describes the in situ immobilization of the halophilic HvADH2 in the Fe-BTC MOF [69]. Enzyme specificity, stability and tolerance to organic solvents were systematically studied.…”

Section: Semiamorphous Fe-btcmentioning

confidence: 99%

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Sometimes, it can be challenging to determine the window of opportunity of the cascade, especially if substrates and intermediates are not available, or if the reaction steps interact with each other in simultaneous mode. Typical parameters that can be interesting for optimizations are the solvent system [44,74,75], the concentration of reaction components (substrate [38], salts [24], co-solvents [76,77], cofactors [49], other additives), the pH of buffered reactions [49], reaction temperature [78], or also the necessity of cofactor regeneration. Choosing the reaction conditions for the whole cascade is always a compromise between the optimal reaction conditions for each enzyme of the cascade, especially if reactions take place in a simultaneous mode [79].…”

Section: Reaction Conditionsmentioning

confidence: 99%

Getting the Most Out of Enzyme Cascades: Strategies to Optimize In Vitro Multi-Enzymatic Reactions

et al. 2021

View full text Add to dashboard Cite

In vitro enzyme cascades possess great benefits, such as their synthetic capabilities for complex molecules, no need for intermediate isolation, and the shift of unfavorable equilibria towards the products. Their performance, however, can be impaired by, for example, destabilizing or inhibitory interactions between the cascade components or incongruous reaction conditions. The optimization of such systems is therefore often inevitable but not an easy task. Many parameters such as the design of the synthesis route, the choice of enzymes, reaction conditions, or process design can alter the performance of an in vitro enzymatic cascade. Many strategies to tackle this complex task exist, ranging from experimental to in silico approaches and combinations of both. This review collates examples of various optimization strategies and their success. The feasibility of optimization goals, the influence of certain parameters and the usage of algorithm-based optimizations are discussed.

show abstract

“…For the reduction reaction, it accepts a range of aromatic ketone substrates such as alkyl, methyl and alphahalo aryl ketones (Alsafadi et al 2017). Immobilization within epoxy resin and metal organic framework material further improves the enzyme activity over a broader pH range and temperature and enhances enzyme stability in organic solvents (Alsafadi and Paradisi 2014;Carucci et al 2018). It is also possible to improve the substrate scope of HvADH2 for biocatalysis through rational in silico enzyme design (Cassidy et al 2017).…”

Section: Biotechnological Potential Of H Volcaniimentioning

confidence: 99%

Haloferax volcanii for biotechnology applications: challenges, current state and perspectives

Haque

Paradisi

Allers

2019

Appl Microbiol Biotechnol

Self Cite

View full text Add to dashboard Cite

Haloferax volcanii is an obligate halophilic archaeon with its origin in the Dead Sea. Simple laboratory culture conditions and a wide range of genetic tools have made it a model organism for studying haloarchaeal cell biology. Halophilic enzymes of potential interest to biotechnology have opened up the application of this organism in biocatalysis, bioremediation, nanobiotechnology, bioplastics and the biofuel industry. Functionally active halophilic proteins can be easily expressed in a halophilic environment, and an extensive genetic toolkit with options for regulated protein overexpression has allowed the purification of biotechnologically important enzymes from different halophiles in H. volcanii. However, corrosion mediated damage caused to stainless-steel bioreactors by high salt concentrations and a tendency to form biofilms when cultured in high volume are some of the challenges of applying H. volcanii in biotechnology. The ability to employ expressed active proteins in immobilized cells within a porous biocompatible matrix offers new avenues for exploiting H. volcanii in biotechnology. This review critically evaluates the various application potentials, challenges and toolkits available for using this extreme halophilic organism in biotechnology.

show abstract

Significant Enhancement of Structural Stability of the Hyperhalophilic ADH fromHaloferax volcaniivia Entrapment on Metal Organic Framework Support

Cited by 26 publications

References 57 publications

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

Getting the Most Out of Enzyme Cascades: Strategies to Optimize In Vitro Multi-Enzymatic Reactions

Haloferax volcanii for biotechnology applications: challenges, current state and perspectives

Contact Info

Product

Resources

About