Title of Invention: PRINTABLE MAGNETIC POWDERS AND 3D PRINTED OBJECTS FOR BIONANOCATALYST IMMOBILIZATION Abstract: The invention provides materials, and in particular, magnetic materials, for the universal immobilization of enzymes and enzyme systems. Described herein are highly magnetic and highly porous composite blends of thermoplastics with magnetic particles to form powders, single-layered, or multiple-layered materials that are used as scaffolds for magnetically immobilized enzymes known as bionanocatalysts (BNCs). Designed objects are produced using 3D printing by sintering composite magnetic powders. In some embodiments, Selective Laser Sintering (SLS) is used. The invention provides the use of the material compositions for 3D printing of enzyme supports and flow cells allowing continuous production of, e.g., small molecules. Detailed Description: CROSS REFERENCE TO RELATED APPLICATIONS This application claims the benefit of U.S. Provisional Application No. 62/737,910, filed Sep. 27, 2018, which is incorporated herein by reference in its entirety. FIELD OF THE INVENTION The invention provides materials, and in particular, magnetic materials, for the universal immobilization of enzymes and enzyme systems. Described herein are high magnetism and high porosity composite blends of thermoplastics with magnetic particles to form powders, single-layered, or multiple-layered materials that are used as scaffolds for magnetically immobilized enzymes known as bionanocatalysts (BNCs). Designed objects are produced using 3D printing by sintering composite magnetic powders. In some embodiments, Selective Laser Sintering (SLS) is used. The invention provides the use of the composition materials for 3D printing of enzyme supports and flow cells allowing continuous production of small molecules. BACKGROUND OF THE INVENTION Biocatalysis, as a green technology, has become increasingly popular in chemical manufacturing over traditional expensive and inefficient processes. Its applications include the production of food ingredients, flavors, fragrances, commodity and fine chemicals, and active pharmaceuticals. When producing chemicals at industrial scale, however, enzymes can suffer drastic losses in activity and loading causing a significant drop in performance. Magnetic enzyme immobilization involves the entrapment of enzymes in mesoporous magnetic clusters that self-assemble around the enzymes (level 1). The immobilization efficiency depends on a number of factors that include the initial concentrations of enzymes and nanoparticles, the nature of the enzyme surface, the electrostatic potential of the enzyme, the nature of the nanoparticle surface, and the time of contact. Enzymes used for industrial purposes in biocatalytic processes should be highly efficient, stable before and during the process, reusable over several biocatalytic cycles, and economical. Mesoporous aggregates of magnetic nanoparticles may be incorporated into continuous or particulate macroporous scaffolds (level 2). The scaffolds may or may not be magnetic. Such scaffolds are discussed in WO2014/055853, WO2017/180383, and Corgie et al., Chem. Today 34(5):15-20 (2016), incorporated by reference herein in their entirety. Highly magnetic scaffolds are designed to immobilize, stabilize, and optimize any enzyme. This includes full enzyme systems, at high loading and full activity, and for the production of, e.g., small molecules. Selective laser sintering (SLS) is an additive manufacturing (AM) technique that uses a laser as the power source to sinter powdered materials such as nylon or polyamide. A laser automatically aimed at points in space, defined by a 3D model, binds the material together to create a solid structure. It is similar to direct metal laser sintering (DMLS) but differs in technical details. DMLS uses a comparable concept, but in DMLS the material is fully melted rather than sintered. This allows one to manufacture materials with different properties (e.g. crystal structure and porosity). SLS is a relatively new technology that may be expanded into commercial-scale manufacturing processes. SLS is an additive manufacturing layer technology. It involves high-powered lasers (e.g. a carbon dioxide laser) to fuse small particles of plastic, metal, ceramic, or glass powders into a mass that has a desired three-dimensional shape. The laser selectively fuses powdered material by scanning cross-sections generated from a 3-D digital description of the part (for example from a CAD file or scan data) on the surface of a powder bed. After each cross-section is scanned, the powder bed is lowered by a one-layer thickness, a new layer of material is applied on top, and the process is repeated until the part is completed. 3D printing involves processes in which material is joined or solidified under computer control to create three-dimensional objects. Material is added together (e.g. liquid molecules or powder grains) that is fused together. 3D printing is used in both rapid prototyping and additive manufacturing. Objects can be of almost any shape or geometry and typically are produced using digital model data from a 3D model or another electronic data source such as an Additive Manufacturing File (AMF). Typically, materials are added in sequential layers. There are many different technologies, like stereolithography (SLA) or fused deposit modeling (FDM). SUMMARY OF THE INVENTION The invention provides materials, and in particular, magnetic materials, for the universal immobilization of enzymes and enzyme systems. Described herein are high magnetism and high porosity composite blends of thermoplastics with magnetic particles to form powders, single-layered, or multiple-layered materials that are used as scaffolds for magnetically immobilized enzymes known as bionanocatalysts (BNCs). Designed objects are produced by 3D printing by sintering composite magnetic powders. In some embodiments, Selective Laser Sintering (SLS) is used. The invention provides the use of the composition materials for 3D printing of enzyme supports and flow cells allowing continuous production of small molecules. With the ability to immobilize any enzymes for any processes, the materials disclosed herein, when functionalized with enzymes or enzyme systems, may be used for producing pharmaceutical actives, agricultural actives, flavors and fragrances, fine and commodity chemicals, and food ingredients. The invention provides a magnetic macroporous powder, comprising a thermoplastic polymer and magnetic microparticles, wherein the powder is operative for immobilizing self-assembled mesoporous aggregates of magnetic nanoparticles. In some embodiments, the magnetic particles have a size of between about 50-100 μm, 10-50 μm, 5-10 μm, 10 μm, or 5 μm. In other embodiments, the magnetic particles have a size of less than 5 μm, greater than 100 μm or have an average size of about 150 μm, about 75 μm, or about 15 μm. In some embodiments, the magnetic particles have a concentration of between 0 and 10% by weight. In other embodiments, the magnetic particles have a concentration of 10 to 50% or 50 to 90% by weight. In some embodiments, the thermoplastic polymer comprises a polymer selected from the group consisting of Polyvinyl alcohol (PVA), Acrylic (PMMA), Acrylonitrile butadiene styrene (ABS), Polyamide including Nylon 6, Nylon 11 and Nylon 12, Polylactic acid (PLA), Polybenzimidazole (PBI), Polycarbonate (PC), Polyether sulfone (PES), Polyoxymethylene (POM), Polyetherether ketone (PEEK), Polyetherimide (PEI), Polyethylene (PE), Polyphenylene oxide (PEO), Polyphenylene sulfide (PPS), Polypropylene (PP), Polystyrene (PS), Polyvinyl chloride (PVC), polytetrafluoroethylene (PTFE), co-polyesters, and chemically functionalized derivatives thereof. In some embodiments, the magnetic microparticles comprise a magnetic material selected from the group consisting of magnetite (Fe3O4), hematite (α-Fe2O3), maghemite (γ-Fe2O3), a spinel ferrite, lodestone, cobalt, nickel, rare earth, and magnetic composites. In preferred embodiments, the rare earth is neodymium, gadolinium, sysprosium, samarium-cobalt, or neodymium-iron-boron. In other embodiments, the magnetic composite comprises a ceramic, ferrite, or alnico magnet. The invention provides that, in the magnetic macroporous powders disclosed herein, the thermoplastic polymer and the magnetic microparticles are chemically, thermally, or physically blended. In some embodiments, the macropores have a size of between 0.5-200 μm. In some embodiments, the macroporous powders of the invention further comprise cellulose fibers, cellulose nanofibers, glass fibers, or carbon fibers or other reinforcement macro structures. Some embodiments of the magnetic macroporous powder of the invention further comprise self-assembled mesoporous aggregates of magnetic nanoparticles and an enzyme magnetically immobilized within the mesopores or on their surface. The invention provides shaped magnetic macroporous scaffolds, comprising the magnetic macroporous powders disclosed herein, wherein a powder has been formed into the shape by three-dimensional (3D) printing. In some embodiments, the shape is a cylinder, an orb, a bead, a strip, a capsule, a cube, a squared rod, a pyramid, a diamond, a lattice, or an irregular shape. In some embodiments, the shaped magnetic macroporous scaffolds described herein further comprise self-assembled mesoporous aggregates of magnetic nanoparticles. In preferred embodiments, the self-assembled mesoporous aggregates of magnetic nanoparticles further comprise one or more enzymes magnetically immobilized within said mesopores or on the surface of said magnetic nanoparticles. In some embodiments of the invention, the enzyme is selected from the group consisting of hydrolases, hydroxylases, hydrogen peroxide producing enzymes (HPP), nitralases, hydratases, dehydrogenases, transaminases, ketoreductases (KREDS) ene reductases (EREDS), imine reductases (IREDS), catalases, dismutases, oxidases, dioxygenases, lipoxidases, oxidoreductases, peroxidases, laccases, synthetases, transferases, oxynitrilases, isomerases, gludosidases, kinases, lyases, sucrases, invertases, epimerases, and lipases. In some embodiments of the invention, two or more enzymes are combined. In other embodiments of the invention, the self-assembled mesoporous aggregates of magnetic nanoparticles comprise microsomes, wherein a first enzyme requiring a diffusible cofactor having a first enzymatic activity is contained within the microsomes, wherein a second enzyme comprising a cofactor regeneration activity is magnetically-entrapped within the mesopores, wherein the cofactor is utilized in the first enzymatic activity; wherein the first and second enzymes function by converting a diffusible substrate into a diffusible product; and wherein the magnetic nanoparticles are magnetically associated with the magnetic macroporous scaffold. In other embodiments of the invention, the self-assembled mesoporous aggregates of magnetic nanoparticles comprises a first enzyme requiring a diffusible cofactor having a first enzymatic activity; a second enzyme comprising a cofactor regeneration activity; wherein the cofactor is utilized in the first enzymatic activity; wherein the first and second enzymes are magnetically-entrapped within the mesopores formed by the aggregates of magnetic nanoparticles and the first and second enzymes function by converting a diffusible substrate into a diffusible product. In preferred embodiments, the first enzyme is an oxidative enzyme. In more preferred embodiments, the oxidative enzyme is a Flavin-containing oxygenase and further comprising a third enzyme having a co-factor reductase activity that is co-located with the first enzyme. In a more preferred embodiment, the oxidative enzyme is a P450 monooxygenase and the composition further comprises a third enzyme having a co-factor reductase activity that is co-located with the first enzyme. In a more preferred embodiment, the P450 monooxygenase and the third enzyme are comprised within a single protein. In a more preferred embodiment, the single protein comprises a bifunctional cytochrome P450/NADPH—P450 reductase. In a more preferred embodiment, the single protein has BM3 activity and has at least a 90% sequence identity to SEQ ID NO:1. In some embodiments of the invention, the macroporous scaffolds disclosed herein are formed in a shape suited for a particular biocatalytic process. The invention provides a method of making a shaped magnetic macroporous scaffold comprising the magnetic macroporous powders disclosed herein, comprising additively manufacturing (AM) the shaped magnetic macroporous scaffold using a three-dimensional (3D) printer, wherein the shape is taken from a 3D model. In some embodiments, the 3D model is an electronic file. In preferred embodiments, the electronic file is a computer-aided design (CAD) or a stereolithography (STL) file. In some embodiments, the AM is Fused Filament Fabrication (FFF) or Selective Laser Sintering (SLS). In some embodiments of the invention, the macropores are formed using a soluble agent selected from the group consisting of a salt, a sugar, or a small soluble polymer. The soluble agent is removed with a solvent. The invention provides a method of making a device for catalyzing an enzymatic reaction, comprising combining a shaped magnetic macroporous scaffold with self-assembled mesoporous aggregates of magnetic nanoparticles and an enzyme, wherein the enzyme is magnetically immobilized within the mesopores. The invention provides a method of catalyzing a reaction between a plurality of substrates, comprising exposing the magnetic macroporous powders disclosed herein comprising an enzyme to the substrates under conditions in which the enzyme catalyzes the reaction between the substrates. The invention provides a method of catalyzing a reaction between a plurality of substrates, comprising exposing the shaped magnetic macroporous scaffold disclosed herein comprising an enzyme to the substrates under conditions in which the enzyme catalyzes the reaction between the substrates. In other embodiments, the reaction is used in the manufacture of a pharmaceutical product, a medicament, a food product, a flavor, a fragrance, a sweetener, an agrochemical, an antimicrobial agent, a toxin, a detergent, a fuel product, a biochemical product, a paper product, or a plastic product. In other embodiments, the reaction is used in a process for removing a contaminant from a solution. In preferred embodiments, the solution is an aqueous solution, a solvent, or an oil. In some embodiments, the methods of manufacturing disclosed herein further comprise the step of removing the mesoporous aggregates and replacing them with a fresh preparation of mesoporous aggregates. In other embodiments, the method is carried out using flow cell and continuous manufacturing. BRIEF DESCRIPTION OF THE DRAWINGS SEM images of a polypropylene magnetite composite extruded composite after: (FIG. 1A) cryogenic size reduction and sieving through a 100 micron opening; (FIG. 1B) selective laser sintering at a chamber temperature of 105° C., surface temperature of 125° C., and a laser speed of 650 mm/s; and (FIG. 1C) enzyme immobilization of the sintered scaffold (cross) showing the BNCs (invertase enzyme) magnetically captured on the surface. SEM images of a Nylon 12 magnetite composite produced through a dissolution coating process. FIG. 2A shows a backscatter detector. FIG. 2B shows it at 10,000 times magnification. FIG. 3 shows an article size analysis of a polypropylene magnetite extruded composite after cryogenic size reduction. Sintering of 3D printing objects for enzyme immobilization. 3D renderings are shown for a strip (FIG. 4A), a bead (FIG. 4B), a cross (FIG. 4C), and a static mixing element (FIG. 4D). The corresponding SLS printed objects are shown in FIGS. 4E, 4F, 4G, and 4H. They were printed using a 110° C. chamber temperature, 125° C. fabrication surface temperature, and a 650 mm/s laser speed. FIG. 4I depicts a 3D render of a printed bar for enzyme immobilization. FIG. 4J depicts the SLS printed bar. Immobilization of invertase. FIG. 5A shows the immobilization yields of invertase on 3D printed polypropylene-magnetite scaffolds (Polypropylene-magnetite cross and bead). Immobilization conditions: 500 μg/mL NP pH 3. FIG. 5B shows the relative activity of free and immobilized invertase (100 μg/mL) for the hydrolysis of raffinose after 5 minutes, as determined by the reducing-sugar PAHBAH assay. Immobilization of lipase. FIG. 6A shows the immobilization yields of CALB on 3D printed scaffolds (Polypropylene-magnetite cross and bead). Immobilization conditions: 250 μg/mL NP pH 3. FIG. 6B shows the relative activity of free and immobilized CALB (100 μg/mL) for the hydrolysis of p-NPL after 4 minutes as determined by colorimetric assay. Re-use of the 3D printed scaffolds on a polypropylene-magnetite cross and beads. FIG. 7A shows the relative activity of free CALB (100 μg/mL) and previously immobilized crosses and beads (post-wash in boiling pH 2 water for 10 mins) for the hydrolysis of p-NPL after 4 minutes as determined by colorimetric assay. FIG. 7B shows the re-immobilization yields of CALB on 3D printed scaffolds (cross and bead). Immobilization conditions were 250 μg/mL NP at pH 3. FIG. 7C shows the relative activity of free CALB and re-immobilized CALB on washed scaffolds as determined by p-NPL hydrolysis. FIG. 8 shows a plot of a flow-rate, F, (mL/min) from a sucrose reaction mixture in a flow cell of immobilized invertase (modeled as a PBR) as a function of various initial sucrose concentrations, So. It also shows the conversion of sucrose into glucose and fructose, X. FIG. 9 shows the relative activity of immobilized HRP to free enzyme normalized for immobilization yield for the co-oxidation of 4-AAP and phenol as determined by colorimetric assay. FIG. 10: A 3D printed flow cell set up with a syringe pump. HRP was immobilized onto the flow cell and the activity was confirmed by the colorimetric assay for co-oxidation of 4-AAP and phenol. DETAILED DESCRIPTION OF THE INVENTION The present invention provides compositions and methods for supporting and enhancing the effectiveness of BNC's. This is accomplished, for the first time, using powders, single-layered, and multi-layered forms that are highly magnetic, highly-porous thermoplastic blends. They may be formed using 3D printing that involves sintering composite magnetic powders. The invention has many benefits over the prior art. It enables the universal immobilization of enzymes for small molecule syntheses. The materials may contain large macropores or a high magnetic surface area for BNC immobilization. Flexible compositions for sintered magnetic scaffolds can be made with any meltable thermoplastics and magnetic material composition. The materials can be made resistant to solvents. The process is flexible and tunable to manufacture objects using 3D designs that magnetically capture the BNCs. It is scalable from micro-structures to flow cells for biocatalytic reactors. A large surface area may result from the sintering process itself. Materials can also be recycled by removing the BNCs and then re-functionalized them for repeated use. In some embodiments, thermoplastics such as polypropylene, polyethylene, nylon, and polylactic acid (PLA) are blended with magnetic materials (e.g. magnetite MMP) via melting/extrusion or via coating of the magnetic material by dissolving the plastic in a solvent. In other embodiments, the powders are sintered by a laser using SLS. Porosity may be formed during SLS. In other embodiments, an extruded composite material is size reduced via cryomilling or another form of milling. In other embodiments, composite powders are sieved to an ideal particle size. In preferred embodiments, the particle sizes are 60+/−20 μm. Powders or 3D printed objects can be functionalized with BNCs containing one or more enzymes or enzyme systems. BNCs are magnetically trapped at the surface of the powders or 3D printed objects. Composite powders may also be optimized for flowability. In some embodiments, 3D objects can be printed to optimize flow within to be used in flow reactors. In some embodiments, 3D objects and composite powders can be washed from the BNCs by an acid wash, rinsed with water, and then re-functionalized with fresh BNCs. Highly magnetic scaffolds (Macroporous Magnetic Scaffolds or MMP) are designed to immobilize, stabilize and optimize any BNCs containing enzymes. This includes full enzyme systems at high loading and full activity for the production of small molecules. By combining natural or engineered enzymes with cofactor recycling systems, the scaffolds allow one to scale up biocatalysis to innovations to manufacturing scale and production. MMP made of thermoplastic and magnetic materials of the invention can take the form of magnetic powders that are suitable for use in sequential batch reactions. For flow chemistry application, these powders can be 3D printed by SLS as structures, as functional objects, or as flow cells or plate reactors. High surface areas allow one to maximize the enzyme loading and flow can be engineered within the materials to enable biocatalysis at maximal productivity. SLS can be used to process nearly any kind of material from metals, ceramics, plastics, and combinations thereof, for tailor-made composite materials. It is critical, however, that the material is available in fine powder form and that the powder particles are operative to fuse when exposing them to heat (Kruth et al., Assembly Automation 23(4):357-371(2003), incorporated by reference herein in its entirety). When the material lacks those features, or is prone to phase transitions at the temperature range or conditions of the sintering process, the addition of a sacrificial binder can make this process still feasible for that material. Commonly, polymers are used as sacrificial binders in order to expand the range of materials suitable for this technology. After sintering, the sacrificial binder can be either removed by thermal decomposition or kept as part of the composition. This concept applies to magnetite that loses its permanent magnetic properties above 585° C. This is significantly lower than its melting temperature (1538° C.). Another advantage of using a polymeric matrix to incorporate magnetite particles is that the former can act as a protective barrier to prevent oxidation and corrosion as well as aiding to disperse the magnetite particles. Also, magnetite can mechanically reinforce the polymer. (Shishkovsky et al., Microelectronic Engineering 146:85-91 (2015), incorporated by reference herein in its entirety). Laser sintering of plastic parts is one of two additive manufacturing processes used for Rapid Manufacturing (Wegner, Physics Procedia 83:1003-1012 (2016), incorporated by reference herein in its entirety). There are several polymer properties that determine its capability to be sintered and produce good quality 3D objects. These include structural properties such crystalline structure (i.e. thermal properties such as Tm, Tg, and Tc), mechanical properties (Young's modulus and elongation at break, etc.), density, particle size, and shape. In SLS, the temperature-processing window is determined from the difference between the melting and crystallization temperatures of the polymer. For instance, nylon 12 (PA 12) has one of the highest operational windows and is thus a widely used SLS material. In theory, the higher this value is, the easier the material can be sintered. In practice, however there are many more parameters that can still make this process difficult for any specific polymer (Shishkovsky et al., Microelectronic Engineering 146:85-91 (2015), incorporated by reference herein in its entirety). In order to prevent curling of the sintered part, a low polymer crystallization rate is desired together with a melt index that provides a suitable rheology and surface tension. Additionally, the bulk density, particle shape, and size distribution of the powder are key factors (Wegner, Physics Procedia 83:1003-1012 (2016), incorporated by reference herein in its entirety). It has been determined that the optimal particle size range is about 40 to about 90 microns. Smaller particles prevent flowability and their rapid vaporization is detrimental to the optical sensors of the sintering device. This can fog the device and lead to inaccurately sintered parts (Goodridge et al. Materials Science 57:229-267 (2012), incorporated by reference herein in its entirety). The powders should have good flowing properties and preferably an approximately round particle shape. This allows good powder spreading during the process. High heat conductivity of the material is desired at the CO2 laser beam wavelength (10.6 microns). This is not the case for most polymers. The last two requirements can be met by the incorporation of additives such as high-energy absorption materials, e.g. carbon black, to improve heat absorption, and fume silica nanoparticles (talc) to aid the particle flowability with irregularly-shaped particles. Additive manufacturing (AM), also referred to as 3D printing, involves manufacturing a part by depositing material layer-by-layer. This differs from conventional processes such as subtractive processes (i.e., milling or drilling), formative processes (i.e., casting or forging), and joining processes (i.e., welding or fastening). Quick production time, low prototyping costs, and design flexibility make 3D printing a valuable tool for both prototyping and industrial manufacturing. The three most common types of 3D printers are fused filament fabrication, stereolithography, and selective laser sintering. Fused filament fabrication (FFF) melts a thermoplastic continuous filament and builds the object layer by layer until the print is complete. Although alternative materials exist, the two most popular filament materials are polylactic acid (PLA) and acrylonitrile butadiene styrene (ABS). FFF printers and materials are among the cheapest on the market but currently have a lower print resolution and build quality. Stereolithography (SLA) uses a laser to polymerize photosensitive resins. Uncured liquid resin is placed in a vat where a laser is used to cure resin into solid plastic and build the object layer by layer. SLA printers have a much higher resolution than FFF printers due to the fine spot size of the laser and thus can print intricate features and complex shapes. The resins, however, are more expensive than filaments and completed prints currently require post processing with solvents to optimize the surface finish and material characteristics. Selective laser sintering (SLS) is a powder-based layer-additive manufacturing process generally meant for rapid prototyping and rapid tooling. Laser beams either in continuous or pulse mode are used as a heat source for scanning and joining powders in predetermined sizes and shapes of layers. The geometry of the scanned layers corresponds to the various cross sections of the computer-aided design (CAD) models or stereolithography (STL) files of the object. After the first layer is scanned, a second layer of loose powder is deposited over it, and the process is repeated from bottom to top until the artifact (3D object) is complete.” (Kumar, JOM, 55(10), 43-47 (2003), incorporated by reference herein in its entirety). SLS provides advantages for printing objects with magnetic properties that can be used for immobilizing BNCs. This is because the printing process creates porosity and a high surface area. The surrounding, unsintered powder acts as a natural support that eliminates the need for dedicated support structures. The lack of support structures allows for complex geometries that would otherwise be impossible to manufacture using alternative 3D printing methods. In addition, the nature of sintering itself creates macro and microporous volumes. During the printing process, the laser flashes thermoplastic crystalline thermoplastic powders (e.g. Polypropylene, polystyrene) between their glass transition temperature and melting temperature to generate stiff parts. By avoiding amorphous behavior with a quick laser scan speed (>100 mm/s), powders are sintered in place to form small bonds amongst themselves. The low-density powders trap air in their structures resulting in remarkable porosity and surface area in three dimensions. These pores increase the surface area for enzyme immobilization. In recent years, industrial use of enzymes has garnered significant attention due to the wide range of potential manufacturing applications. Using enzymes in industrial processes offers several advantages over conventional chemical methods. This includes high catalytic activity, the ability to perform complex reactions, and promoting greener chemistry by reducing by-products and the need for toxic chemicals (Singh et al., Microbial enzymes: industrial progress in 21st century. 3 Biotech. 6(2):174 (2016), incorporated by reference herein in its entirety). One of the biggest hindrances to widespread biocatalysis use in industrial production is low enzyme stability. This is further hampered by relatively harsh process conditions that can destabilize enzymes and decrease their lifespan (Mohamad et al., Biotechnology, Biotechnological Equipment 29(2):205-220 (2015), incorporated by reference herein in its entirety). Furthermore, the free enzymes used in these processes are generally lost from the system as waste products and therefore become a high operating cost. The primary solution to these issues is immobilization of enzymes onto scaffolding to enhance their operational stability and catalytic activity. Enzyme immobilization also provides a method for enzyme recovery, making biocatalytic processes more economically feasible. Currently, biocatalytic processes for industrial production are generally carried out in batch reactors due to their simplicity and ease of operation. Despite the benefits of using batch reactors, continuous flow systems enable higher productivity and better process control (Wiles C et al., Green Chem. (14):38-54 (2012)). The rapid development of flow chemistry in biocatalytic processes has primarily been driven by a growing interest in process intensification and green chemistry. Continuous flow systems facilitate process intensification by decreasing residence times (often from hours to minutes), reducing the size of equipment required, and enabling production volume enhancement (Tamborini et al., Cell. 36(1):73-78 (2018)). From a green chemistry standpoint, these systems offer significant improvements in safety, waste generation, and energy efficiency due to heat management and mixing control (Newman and Jensen, Green Chem. (15):1456-1472 (2013)). The foregoing are incorporated by reference in their entirety A solution to combining biocatalysis and continuous flow systems is the use of functionalized flow cells. Biocatalytic flow cells are scaffolds containing immobilized enzymes for use in reactors such as continuous stirred tank reactors (CSTRs) and packed bed reactors (PBRs). Both types of reactors are known in the art but are primarily chosen based on the type of immobilization used. With a total market value of $5.8B in 2010, immobilized enzymes are used in a diverse range of large-scale processes including high fructose corn syrup production (107 tons/year), transesterification of food oils (105 tons/year), biodiesel synthesis (104 tons/year), and chiral resolution of alcohols and amines (103 tons/year) (DiCosimo et al., Chem. Soc. Rev. (42):6437-6474 (2013), incorporated by reference herein in its entirety). These systems allow for improved downstream process management for enzymatic systems compared to batch reactors in terms of in-line control, enzyme reuse, and production scalability. For the foregoing reasons, the inventions described herein provide biocatalytic systems for small-to-large scale manufacturing using BNCs in scaffolds that are shaped by 3D printing. In some embodiments, the biocatalytic systems are continuous flow. The novel scaffolds disclosed herein may comprise cross-linked water-insoluble polymers and an approximately uniform distribution of embedded magnetic microparticles (MMP). The cross-linked polymer comprises polyvinyl alcohol (PVA) and optionally additional polymeric materials. The scaffolds may take any shape by using 3D printing. By combining natural or engineered enzymes with cofactors and cofactor recycling systems, the scaffold technology disclosed herein allows one to quickly translate innovation in biocatalysis to innovation in production. The magnetic powders are suitable for use in sequential batch reactions. For flow chemistry applications, these powders can be 3D printed as structures in a functional object or as flow cells or plate reactors. High surface areas allow one to maximize the enzyme loadings and flow can be engineered within the materials to enable biocatalysis at maximal productivity. With the ability to immobilize any enzymes for any processes, the materials functionalized with enzymes, or enzyme systems, have applications for the production of pharmaceutical actives, agricultural actives, flavors and fragrances, fine and commodity chemicals, and food ingredients. Self-assembled mesoporous nanoclusters comprising entrapped enzymes are highly active and robust. The technology is a powerful blend of biochemistry, nanotechnology, and bioengineering at three integrated levels of organization: Level 1 is the self-assembly of enzymes with magnetic nanoparticles (MNP) for the synthesis of magnetic mesoporous nanoclusters. This level uses a mechanism of molecular self-entrapment to immobilize and stabilize enzymes. Level 2 is the stabilization of the MNPs into other matrices. Level 3 is product conditioning and packaging for Level 1+2 delivery. The assembly of magnetic nanoparticles adsorbed to enzyme is herein also referred to as a “bionanocatalyst” (BNC). MNPs allow for a broader range of operating conditions such as temperature, ionic strength and pH. The size and magnetization of the MNPs affect the formation and structure of the NPs, all of which have a significant impact on the activity of the entrapped enzymes. By virtue of their surprising resilience under various reaction conditions, MNPs can be used as improved enzymatic or catalytic agents where other such agents are currently used. Furthermore, they can be used in other applications where enzymes have not yet been considered or found applicable. The BNC contains mesopores that are interstitial spaces between the magnetic nanoparticles. The enzymes are preferably embedded or immobilized within at least a portion of mesopores of the BNC. As used herein, the term “magnetic” encompasses all types of useful magnetic characteristics, including permanent magnetic, superparamagnetic, paramagnetic, ferromagnetic, and ferrimagnetic behaviors. The magnetic nanoparticle or BNC has a size in the nanoscale, i.e., generally no more than 500 nm. As used herein, the term “size” can refer to a diameter of the magnetic nanoparticle when the magnetic nanoparticle is approximately or substantially spherical. In a case where the magnetic nanoparticle is not approximately or substantially spherical (e.g., substantially ovoid or irregular), the term “size” can refer to either the longest the dimension or an average of the three dimensions of the magnetic nanoparticle. The term “size” may also refer to an average of sizes over a population of magnetic nanoparticles (i.e., “average size”). In different embodiments, the magnetic nanoparticle has a size of precisely, about, up to, or less than, for example, 500 nm, 400 nm, 300 nm, 200 nm, 100 nm, 50 nm, 40 nm, 30 nm, 25 nm, 20 nm, 15 nm, 10 nm, 5 nm, 4 nm, 3 nm, 2 nm, or 1 nm, or a size within a range bounded by any two of the foregoing exemplary sizes. In the BNC, the individual magnetic nanoparticles can be considered to be primary nanoparticles (i.e., primary crystallites) having any of the sizes provided above. The aggregates of nanoparticles in a BNC are larger in size than the nanoparticles and generally have a size (i.e., secondary size) of at least about 5 nm. In different embodiments, the aggregates have a size of precisely, about, at least, above, up to, or less than, for example, 5 nm, 8 nm, 10 nm, 12 nm, 15 nm, 20 nm, 25 nm, 30 nm, 35 nm, 40 nm, 45 nm, 50 nm, 60 nm, 70 nm, 80 nm, 90 nm, 100 nm, 150 nm, 200 nm, 300 nm, 400 nm, 500 nm, 600 nm, 700 nm, or 800 nm, or a size within a range bounded by any two of the foregoing exemplary sizes. Typically, the primary and/or aggregated magnetic nanoparticles or BNCs thereof have a distribution of sizes, i.e., they are generally dispersed in size, either narrowly or broadly dispersed. In different embodiments, any range of primary or aggregate sizes can constitute a major or minor proportion of the total range of primary or aggregate sizes. For example, in some embodiments, a particular range of primary particle sizes (for example, at least about 1, 2, 3, 5, or 10 nm and up to about 15, 20, 25, 30, 35, 40, 45, or 50 nm) or a particular range of aggregate particle sizes (for example, at least about 5, 10, 15, or 20 nm and up to about 50, 100, 150, 200, 250, or 300 nm) constitutes at least or above about 50%, 60%, 70%, 80%, 90%, 95%, 98%, 99%, or 100% of the total range of primary particle sizes. In other embodiments, a particular range of primary particle sizes (for example, less than about 1, 2, 3, 5, or 10 nm, or above about 15, 20, 25, 30, 35, 40, 45, or 50 nm) or a particular range of aggregate particle sizes (for example, less than about 20, 10, or 5 nm, or above about 25, 50, 100, 150, 200, 250, or 300 nm) constitutes no more than or less than about 50%, 40%, 30%, 20%, 10%, 5%, 2%, 1%, 0.5%, or 0.1% of the total range of primary particle sizes. The aggregates of magnetic nanoparticles (i.e., “aggregates”) or BNCs thereof can have any degree of porosity, including a substantial lack of porosity depending upon the quantity of individual primary crystallites they are made of. In particular embodiments, the aggregates are mesoporous by containing interstitial mesopores (i.e., mesopores located between primary magnetic nanoparticles, formed by packing arrangements). The mesopores are generally at least 2 nm and up to 50 nm in size. In different embodiments, the mesopores can have a pore size of precisely or about, for example, 2, 3, 4, 5, 10, 12, 15, 20, 25, 30, 35, 40, 45, or 50 nm, or a pore size within a range bounded by any two of the foregoing exemplary pore sizes. Similar to the case of particle sizes, the mesopores typically have a distribution of sizes, i.e., they are generally dispersed in size, either narrowly or broadly dispersed. In different embodiments, any range of mesopore sizes can constitute a major or minor proportion of the total range of mesopore sizes or of the total pore volume. For example, in some embodiments, a particular range of mesopore sizes (for example, at least about 2, 3, or 5, and up to 8, 10, 15, 20, 25, or 30 nm) constitutes at least or above about 50%, 60%, 70%, 80%, 90%, 95%, 98%, 99%, or 100% of the total range of mesopore sizes or of the total pore volume. In other embodiments, a particular range of mesopore sizes (for example, less than about 2, 3, 4, or 5 nm, or above about 10, 15, 20, 25, 30, 35, 40, 45, or 50 nm) constitutes no more than or less than about 50%, 40%, 30%, 20%, 10%, 5%, 2%, 1%, 0.5%, or 0.1% of the total range of mesopore sizes or of the total pore volume. The magnetic nanoparticles can have any of the compositions known in the art. In some embodiments, the magnetic nanoparticles are or include a zerovalent metallic portion that is magnetic. Some examples of such zerovalent metals include cobalt, nickel, and iron, and their mixtures and alloys. In other embodiments, the magnetic nanoparticles are or include an oxide of a magnetic metal, such as an oxide of cobalt, nickel, or iron, or a mixture thereof. In some embodiments, the magnetic nanoparticles possess distinct core and surface portions. For example, the magnetic nanoparticles may have a core portion composed of elemental iron, cobalt, or nickel and a surface portion composed of a passivating layer, such as a metal oxide or a noble metal coating, such as a layer of gold, platinum, palladium, or silver. In other embodiments, metal oxide magnetic nanoparticles or aggregates thereof are coated with a layer of a noble metal coating. The noble metal coating may, for example, reduce the number of charges on the magnetic nanoparticle surface, which may beneficially increase dispersibility in solution and better control the size of the BNCs. The noble metal coating protects the magnetic nanoparticles against oxidation, solubilization by leaching or by chelation when chelating organic acids, such as citrate, malonate, or tartrate are used in the biochemical reactions or processes. The passivating layer can have any suitable thickness, and particularly, at least, up to, or less than, about for example, 0.1 nm, 0.2 nm, 0.3 nm, 0.4 nm, 0.5 nm, 0.6 nm, 0.7 nm, 0.8 nm, 0.9 nm, 1 nm, 2 nm, 3 nm, 4 nm, 5 nm, 6 nm, 7 nm, 8 nm, 9 nm, or 10 nm, or a thickness in a range bounded by any two of these values. Magnetic materials useful for the invention are well-known in the art. Non-limiting examples comprise ferromagnetic and ferromagnetic materials including ores such as iron ore (magnetite or lodestone), cobalt, and nickel. In other embodiments, rare earth magnets are used. Non-limiting examples include neodymium, gadolinium, sysprosium, samarium-cobalt, neodymium-iron-boron, and the like. In yet further embodiments, the magnets comprise composite materials. Non-limiting examples include ceramic, ferrite, and alnico magnets. In preferred embodiments, the magnetic nanoparticles have an iron oxide composition. The iron oxide composition can be any of the magnetic or superparamagnetic iron oxide compositions known in the art, e.g., magnetite (Fe3O4), hematite (α-Fe2O3), maghemite (γ-Fe2O3), or a spinel ferrite according to the formula AB2O4, wherein A is a divalent metal (e.g., Xn2+, Ni2+, Mn2+, Co2+, Ba2+, Sr2+, or combination thereof) and B is a trivalent metal (e.g., Fe3+, Cr3+, or combination thereof). The individual magnetic nanoparticles or aggregates thereof or BNCs thereof possess any suitable degree of magnetism. For example, the magnetic nanoparticles, BNCs, or BNC scaffold assemblies can possess a saturated magnetization (Ms) of at least or up to about 5, 10, 15, 20, 25, 30, 40, 45, 50, 60, 70, 80, 90, or 100 emu/g. The magnetic nanoparticles, BNCs, or BNC-scaffold assemblies preferably possess a permanent magnetization (Mr) of no more than (i.e., up to) or less than 5 emu/g, and more preferably, up to or less than 4 emu/g, 3 emu/g, 2 emu/g, 1 emu/g, 0.5 emu/g, or 0.1 emu/g. The surface magnetic field of the magnetic nanoparticles, BNCs, or BNC-scaffold assemblies can be about or at least, for example, about 0.5, 1, 5, 10, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 Gauss (G), or a magnetic field within a range bounded by any two of the foregoing values. If microparticles are included, the microparticles may also possess any of the above magnetic strengths. The magnetic nanoparticles or aggregates thereof can be made to adsorb a suitable amount of enzyme, up to or below a saturation level, depending on the application, to produce the resulting BNC. In different embodiments, the magnetic nanoparticles or aggregates thereof may adsorb about, at least, up to, or less than, for example, 1, 5, 10, 15, 20, 25, or 30 pmol/m2 of enzyme. Alternatively, the magnetic nanoparticles or aggregates thereof may adsorb an amount of enzyme that is about, at least, up to, or less than, for example, about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 100% of a saturation level. The magnetic nanoparticles or aggregates thereof or BNCs thereof possess any suitable pore volume. For example, the magnetic nanoparticles or aggregates thereof can possess a pore volume of about, at least, up to, or less than, for example, about 0.01, 0.05, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, or 1 cm3/g, or a pore volume within a range bounded by any two of the foregoing values. The magnetic nanoparticles or aggregates thereof or BNCs thereof possess any suitable specific surface area. For example, the magnetic nanoparticles or aggregates thereof can have a specific surface area of about, at least, up to, or less than, for example, about 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, or 200 m2/g. MNPs, their structures, organizations, suitable enzymes, and uses are described in WO2012122437 and WO2014055853, incorporated by reference herein in their entirety. Some embodiments of the invention comprise hydrolases. Hydrolases catalyze the hydrolysis of many types of chemical bonds by using water as a substrate. The substrates typically have hydrogen and hydroxyl groups at the site of the broken bonds. Hydrolases are classified as EC 3 in the EC number classification of enzymes. Hydrolases can be further classified into several subclasses, based upon the bonds they act upon. Exemplary hydrolases and the bonds they hydrolyze include EC 3.1: ester bonds (esterases: nucleases, phosphodiesterases, lipase, phosphatase), EC 3.2: sugars (DNA glycosylases, glycoside hydrolase), EC 3.3: ether bonds, EC 3.4: peptide bonds (Proteases/peptidases), EC 3.5: carbon-nitrogen bonds, other than peptide bonds, EC 3.6 acid anhydrides (acid anhydride hydrolases, including helicases and GTPase), EC 3.7 carbon-carbon bonds, EC 3.8 halide bonds, EC 3.9: phosphorus-nitrogen bonds, EC 3.10: sulphur-nitrogen bonds, EC 3.11: carbon-phosphorus bonds, EC 3.12: sulfur-sulfur bonds, and EC 3.13: carbon-sulfur bonds. In some preferred embodiments, the hydrolase is a glycoside hydrolase. These enzymes have a variety of uses including degradation of plant materials (e.g. cellulases for degrading cellulose to glucose that are used for ethanol production), food manufacturing (e.g. sugar inversion, maltodextrin production), and paper production (removing hemicelluloses from paper pulp). In some preferred embodiments, the hydrolase is lipolase 100L (EC +1-315-571-0466). It is used to synthesize pregabalin (marketed as by Pfizer as Lyrica®), an anticonvulsant drug used for neuropathic pain, anxiety disorders, and epilepsy. These conditions affect about 1% of the world's population. Lipolase 100L was found to reduce the required starting material by 39% and cut the waste per unit by 80%. In some preferred embodiments, the hydrolase is a gamma-lactamase (e.g. EC +1-315-571-0466). It is used to make Vince lactam, an intermediate for abacavir production (an antiretroviral drug for treating HIV/AIDS). It was found that changing from a stoichiometric process to a catalytic flow process reduced the number of unit operations from 17 to 12 and reduced the waste by 35%. Additionally, the use of the toxic substance cyanogen chloride is minimized. In some preferred embodiments, the hydrolase is a Lactase (e.g. EC +1-315-571-0466). These enzymes break apart lactose in milk into simple sugars to produce lactose-free milk. This important product serves approximately 15% of the world population that is lactose intolerant. In some preferred embodiments, the hydrolase is a penicillin amidase (e.g. EC +1-315-571-0466). These enzymes split penicillin into a carboxylate and 6-aminopenicillanate (6-APA). 6-APA is the core structure in natural and synthetic penicillin derivatives. These enzymes are used to produce semisynthetic penicillins tailored to fight specific infections. In some preferred embodiments, the hydrolase is a nitralase (e.g. EC +1-315-571-0466). These enzymes split nitriles into carboxyl groups. A nitralase is used to manufacture atorvastatin (marketed by Pfizer as Lipitor®). It catalyzes the reaction of meso-3-hydroxyglutaronitrile to ethyl (R)-4-cyano-3-hydroxybutyrate, the latter of which form the core of atorvastatin. Hydrolases are discussed in the following references, incorporated herein by reference in their entirety: Anastas, P. T. Handbook of Green Chemistry. Wiley-VCH-Verlag, 2009; Dunn, Peter J., Andrew Wells, and Michael T. Williams, eds. Green chemistry in the pharmaceutical industry. John Wiley & Sons, 2010.; Martinez et al., Curr. Topics Med. Chem. 13(12):1470-90 (2010); Wells et al., Organic Process Res. Dev. 16(12):1986-1993 (2012). In some embodiments, the invention provides hydrogen peroxide producing (HPP) enzymes. In certain embodiments, the HPP enzymes are oxidases that may be of the EX 1.1.3 subgenus. In particular embodiments, the oxidase may be EC +1-315-571-0466 (malate oxidase), EC +1-315-571-0466 (glucose oxidase), EC +1-315-571-0466 (hexose oxidase), EC +1-315-571-0466 (cholesterol oxidase), EC +1-315-571-0466 (aryl-alcohol oxidase), EC +1-315-571-0466 (L-gulonolactone oxidase), EC +1-315-571-0466 (galactose oxidase), EC +1-315-571-0466 (pyranose oxidase), EC +1-315-571-0466 (L-sorbose oxidase), EC +1-315-571-0466 (pyridoxine 4-oxidase), EC +1-315-571-0466 (alcohol oxidase), EC +1-315-571-0466 (catechol oxidase), EC +1-315-571-0466 (2-hydroxy acid oxidase), EC +1-315-571-0466 (ecdysone oxidase), EC +1-315-571-0466 (choline oxidase), EC +1-315-571-0466 (secondary-alcohol oxidase), EC +1-315-571-0466 (4-hydroxymandelate oxidase), EC +1-315-571-0466 (long-chain alcohol oxidase), EC +1-315-571-0466 (glycerol-3-phosphate oxidase), EC +1-315-571-0466, EC +1-315-571-0466 (thiamine oxidase), EC +1-315-571-0466 (L-galactonolactone oxidase), EC +1-315-571-0466, EC +1-315-571-0466, EC +1-315-571-0466 (hydroxyphytanate oxidase), EC +1-315-571-0466 (nucleoside oxidase), EC +1-315-571-0466 (Nacylhexosamine oxidase), EC +1-315-571-0466 (polyvinyl alcohol oxidase), EC +1-315-571-0466, EC +1-315-571-0466, EC +1-315-571-0466, EC +1-315-571-0466, EC +1-315-571-0466, EC +1-315-571-0466, EC +1-315-571-0466 D-arabinono-1,4-lactone oxidase), EC +1-315-571-0466 (vanillyl alcohol oxidase), EC +1-315-571-0466 (nucleoside oxidase, H2O2 forming), EC +1-315-571-0466 (D-mannitol oxidase), or EC +1-315-571-0466 (xylitol oxidase). Some embodiments of the invention may comprise hydroxylases. Hydroxylation is a chemical process that introduces a hydroxyl group (—OH) into an organic compound. Hydroxylation is the first step in the oxidative degradation of organic compounds in air. Hydroxylation plays a role in detoxification by converting lipophilic compounds into hydrophilic products that are more readily excreted. Some drugs (e.g. steroids) are activated or deactivated by hydroxylation. Hydroxylases are well-known in the art. Exemplary hydroxylases include proline hydroxylases, lysine hydroxylases, and tyrosine hydroxylases. Some embodiments of the invention comprise Nitrilases (NIT). They are hydrolyzing enzymes (EC +1-315-571-0466) that catalyze the hydrolysis of nitriles into chiral carboxylic acids with high enantiopurity and ammonia. NIT activity may be measured by monitoring the conversion of mandelonitirile into a (R)-mandelic acid. This results in a pH drop that may be monitored spectrophotometrically. Nitrilases are used to produce nicotinic acid, also known as vitamin B3 or niacin, from 3-cyanopyridine. Nicotinic acid is a nutritional supplement in foods and a pharmaceutical intermediate. Exemplary industrial uses are discussed in Gong et al., Microbial Cell Factories, 11(1), 142 (2012), incorporated herein by reference herein in its entirety. Some embodiments of the invention comprise hydratases. They are enzymes that catalyze the addition or removal of the elements of water. Hydratases, also known as hydrolases or hydrases, may catalyze the hydration or dehydration of C—O linkages. Some embodiments of the invention comprise oxidoreductases. These enzymes catalyze the transfer of electrons from one molecule to another. This involves the transfer of H and O atoms or electrons from one substance to another. They typically utilize NADP or NAD+ as cofactors. In some preferred embodiments of the invention, Oxidoreductases are used for the decomposition of pollutants such as polychlorinated biphenyls and phenolic compounds, the degradation of coal, and the enhancement of the fermentation of wood hydrolysates. The invention further includes their use in biosensors and disease diagnosis. In some preferred embodiments, the oxidoreductase is a dehydrogenase (DHO). This group of oxidoreductases oxidizes a substrate by a reduction reaction that transfers one or more hydrides (H—) to an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Exemplary dehydrogenases include aldehyde dehydrogenase, acetaldehyde dehydrogenase, alcohol dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase, pyruvate dehydrogenase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, sorbitol dehydrogenase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, and malate dehydrogenase. In some preferred embodiments, the oxidoreductase is a ketoreductase (EC +1-315-571-0466), an oxidoreductase used to make atorvastatin (marketed by Pfizer as Lipitor®). This biocatalytic process is commercially important because it substantially reduces starting materials, limits the use of organic solvents, and increases the biodegradability of the waste streams. In some preferred embodiments, the oxidoreductase is a glucose dehydrogenase (e.g. EC +1-315-571-0466). They are used by pharmaceutical companies to recycle cofactors used in drug production. They catalyze the transformation of glucose into gluconate. NADP+ is reduced to NADPH. This is used in Avastan production. Cytochrome P450 (referred to as P450 or CYP) are of the E.C. 1.14 class of enzymes. (Br. J. Pharmacol. 158(Suppl 1): S215-S217 (2009), incorporated by reference herein in its entirety). They constitute a family of monooxygenases involved in the biotransformation of drugs, xenobiotics, alkanes, terpenes, and aromatic compounds. They also participate in the metabolism of chemical carcinogens and the biosynthesis of physiologically relevant compounds such as steroids, fatty acids, eicosanoids, fat-soluble vitamins, and bile acids. Furthermore, they are also involved in the degradation of xenobiotics in the environment such pesticides and other industrial organic contaminants. They function by incorporating one hydroxyl group into substrates found in many metabolic pathways. In this reaction, dioxygen is reduced to one hydroxyl group and one H2O molecule by the concomitant oxidation of a cofactor such as NAD(P)H. In some preferred embodiments, the oxidoreductase is P450 (EC +1-315-571-0466). It is used in the pharmaceutical industry for difficult oxidations. P450 reduces the cost, inconsistency, and inefficiency associated with natural cofactors (e.g., NADPH/NADP+). There are several advantages of using drug metabolites as active ingredients because they can show superior properties compared to the original drugs. This includes improved pharmacodynamics, improved pharmacokinetics, lower probability of drug-drug interactions, less variable pharmacokinetics and/or pharmacodynamics, improved overall safety profile
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