Abstract:Hierarchical
systems that integrate nano- and macroscale structural
elements can offer enhanced enzyme stability over traditional immobilization
methods. Microparticles were synthesized using interfacial assembly
of lipase B from Candida antarctica with (CLMP-N)
and without (CLMP) nanoparticles around a cross-linked polymeric core,
to characterize the influence of the hierarchical assembly on lipase
stability in extreme environments. Kinetic analysis revealed that
the turnover rate (k
cat) significantly
increa… Show more
“…76 Techniques and approaches for improving the biocatalytic process Immobilisation of biocatalysts, as well as the development of biphasic systems, are techniques that could lead to better process efficiency, enable easier isolation of product or biocatalyst/solvent recovery, decrease the inhibitory effect of substrate/product, and shift reaction equilibrium towards product formation (in case of a biphasic system). Examples of the immobilisation of biocatalysts when running the reactions within DES-containing systems were presented by Xu et al 69,80 Andler et al 80 demonstrated improved enzyme (lipase B from C. antarctica) performance in terms of activity and stability, together with process sustainability, in DES via hierarchical assembly (systems that integrate nano-and macroscale structural elements can offer enhanced enzyme stability over traditional immobilisation methods). Xu et al 69 studied asymmetric reduction of 3-chloropropiophenone with Acetobacter sp.…”
Section: Substrate and Co-substrate Loadingmentioning
During the last decade, deep eutectic solvents (DESs) have emerged as a promising alternative to traditional organic solvents, from both environmental and technological perspectives. The number of structural combinations encompassed by DESs is tremendous; thus, it is possible to design an optimal DES for each specific enzymatic reaction system. In (bio)catalytic processes, a DES can serve as solvent/co-solvent, as an extractive reagent for an enzymatic product, and as a pretreatment solvent of enzymatic biomass. To date, hydrolases are the most studied enzymes in DESs, which is not surprising given that lipases are the most important industrial enzymes. At the same time, there are a limited number of papers dealing with synthetic reactions in DESs involving other hydrolytic enzymes (epoxide hydrolases, phospholipase, proteases and haloalkane dehalogenases), lyases, and dehydrogenases (as a part of the whole Saccharomyces cerevisae and Escherichia coli cell biocatalysis). When designing efficient biocatalytic processes involving DESs, independent of the reaction type and enzyme used, the following steps should be included: (i) preparation and characterisation of the DES, (ii) screening of the DES for optimal enzyme performance, (iii) selection and optimisation of the biocatalytic protocol, and (iv) recovery of the product/DES and DES recycling with possible scale-up. In this paper, we will present some practical aspects that we experienced while working with these solvents, together with some major observations that are available in the literature.
“…76 Techniques and approaches for improving the biocatalytic process Immobilisation of biocatalysts, as well as the development of biphasic systems, are techniques that could lead to better process efficiency, enable easier isolation of product or biocatalyst/solvent recovery, decrease the inhibitory effect of substrate/product, and shift reaction equilibrium towards product formation (in case of a biphasic system). Examples of the immobilisation of biocatalysts when running the reactions within DES-containing systems were presented by Xu et al 69,80 Andler et al 80 demonstrated improved enzyme (lipase B from C. antarctica) performance in terms of activity and stability, together with process sustainability, in DES via hierarchical assembly (systems that integrate nano-and macroscale structural elements can offer enhanced enzyme stability over traditional immobilisation methods). Xu et al 69 studied asymmetric reduction of 3-chloropropiophenone with Acetobacter sp.…”
Section: Substrate and Co-substrate Loadingmentioning
During the last decade, deep eutectic solvents (DESs) have emerged as a promising alternative to traditional organic solvents, from both environmental and technological perspectives. The number of structural combinations encompassed by DESs is tremendous; thus, it is possible to design an optimal DES for each specific enzymatic reaction system. In (bio)catalytic processes, a DES can serve as solvent/co-solvent, as an extractive reagent for an enzymatic product, and as a pretreatment solvent of enzymatic biomass. To date, hydrolases are the most studied enzymes in DESs, which is not surprising given that lipases are the most important industrial enzymes. At the same time, there are a limited number of papers dealing with synthetic reactions in DESs involving other hydrolytic enzymes (epoxide hydrolases, phospholipase, proteases and haloalkane dehalogenases), lyases, and dehydrogenases (as a part of the whole Saccharomyces cerevisae and Escherichia coli cell biocatalysis). When designing efficient biocatalytic processes involving DESs, independent of the reaction type and enzyme used, the following steps should be included: (i) preparation and characterisation of the DES, (ii) screening of the DES for optimal enzyme performance, (iii) selection and optimisation of the biocatalytic protocol, and (iv) recovery of the product/DES and DES recycling with possible scale-up. In this paper, we will present some practical aspects that we experienced while working with these solvents, together with some major observations that are available in the literature.
“…2), may offer a unique opportunity in improving immobilized enzyme activity retention while permitting improved handling and recovery compared to traditional nanomaterials. 28,37,38 Fig. 2Fluorescein isothiocyanate tagged lactase (green) immobilized in electrospun, hierarchical nanofiber mats.…”
Section: Enzyme Immobilizationmentioning
confidence: 99%
“…4Example of esterification reactions performed by lipase to produce value-added products from fatty acids. Reprinted with permission from Andler et al 37 Copyright 2017 American Chemical Society…”
Section: Applications Of Immobilized Enzymes In Food Waste Stream Valmentioning
Food processing generates byproduct and waste streams rich in lipids, carbohydrates, and proteins, which contribute to its negative environmental impact. However, these compounds hold significant economic potential if transformed into revenue streams such as biofuels and ingredients. Indeed, the high protein, sugar, and fat content of many food waste streams makes them ideal feedstocks for enzymatic valorization. Compared to synthetic catalysts, enzymes have higher specificity, lower energy requirement, and improved environmental sustainability in performing chemical transformations, yet their poor stability and recovery limits their performance in their native state. This review article surveys the current state-of-the-art in enzyme stabilization & immobilization technologies, summarizes opportunities in enzyme-catalyzed valorization of waste streams with emphasis on streams rich in mono- and disaccharides, polysaccharides, lipids, and proteins, and highlights challenges and opportunities in designing commercially translatable immobilized enzyme systems towards the ultimate goals of sustainable food production and reduced food waste.
“…We have previously prepared cross-linked microparticles of polydicyclopentadiene with interfacially assembled nanoparticle-conjugated lipase. − Polydicyclopentadiene is a mechanically robust polymer, produced from a ring-opening metathesis polymerization. , These ∼10 μM particles showed enhanced lipase stability across a wide range of pH values and temperatures but were difficult to recover from viscous solvents . As a result, the present work synthesized lipase-containing macroscale polydicyclopentadiene HIPEs.…”
Candida antarctica lipase B is stabilized in a porous, high internal phase emulsion (HIPE) of polydicyclopentadiene to enable biocatalytic waste stream upcycling. The immobilized lipase is subjected to thorough washing conditions and tested for stability in extreme environments and reusability. A porous internal microstructure is revealed through scanning electron microscopy. After preparation, lipase activity increased to 139 ± 9.7% of its original activity. After 10 cycles of reuse, immobilized lipase retains over 50% activity. Immobilized lipase retains activity after 24 h of exposure to temperatures ranging from 20 to 60 °C and pH values of 3, 7, and 10. In the most extreme environments tested, lipase retained 42.8 ± 21% relative activity after exposure to 60 °C and 49.4 ± 16% relative activity after exposure to pH 3. Polymerized HIPEs stabilize lipase and, thus, extend its working range. Further synthesis optimization has the potential to increase enzyme stability, immobilization efficiency, and uniformity. The reported hierarchical stabilization technique shows promise for use of immobilized lipase in non-ideal, industrially relevant conditions.
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