Biocatalyst membrane preparation

Entrapment of the biocatalyst within the matrix during membrane preparation... 

Other claimed matter DBT for enrichment, biocatalyst preparation contacting process Enzymes contacting process Pure compounds as feedstock Membrane fragments and extracts Cell-free extract (envelope and its fragments + associated enzyme) reversible emulsion microemulsion reverse micelles Cell-free enzyme preparation microemulsified process RR and derivatives and other biocatalyst concepts + any known microorganism active for C—S bond cleavage... 

Another favorable aspect of stirred batch reactors is the fact that they are compatible with most forms of a biocatalyst. The biocatalyst may be soluble, immobilized, or a whole-cell preparation in the latter case a bioconversion might be performed in the same vessel used to culture the organism. Recovery of the biocatalyst is sometimes possible, typically when the enzyme is immobilized or confined within a semi-permeable membrane. The latter configuration is often referred to as a membrane reactor. An example is the hollow fiber reactor where enzymes or whole cells are partitioned within permeable fibers that allow the passage of substrates and products but retain the catalyst. A hollow-fiber reactor can be operated in conjunction with the stirred tank and operated in batch or... 

Membrane reactors using biological catalysts can be used in enantioselective processes. Methodologies for the preparation of emulsions (sub-micron) of oil in water have been developed and such emulsions have been used for kinetic resolutions in heterogeneous reactions catalyzed by enantioselective enzyme (Figure 43.4). A catalytic reactor containing membrane immobilized lipase has been realized. In this reactor, the substrate has been fed as emulsion [18]. The distribution of the water organic interface at the level of the immobUized enzyme has remarkably improved the property of transport, kinetic, and selectivity of the immobilized biocatalyst. 

The term encapsulation has been used to distinguish entrapment preparations in which the biocatalyst environment is comparable to that of the bulk phase and where there is no covalent attachment of the protein to the containment medium (Fig. 6-1 D)[21J. Enzymes or whole cells may be encapsulated within the interior of a microscopic semi-permeable membranes (microencapsulation) or within the interior of macroscopic hollow-fiber membranes. Liposome encapsulation, a common microscopic encapsulation technique, involves the containment of an enzyme within the interior of a spherical surfactant bilayer, usually based on a phospholipid such as lecithin. The dimensions and shape of the liposome are variable and may consist of multiple amphiphile layers. Processes in which microscopic compart-mentalization (cf. living cells) such as multienzyme systems, charge transfer systems, or processes that require a gradient in concentration have employed liposome encapsulation. This method of immobilization is also commonly used for the delivery of therapeutic proteins. 

Lipases used in laundry detergents and in other bulk applications do not require enzyme immobilization however, an increasing number of applications in synthesis and biotransformation demand an immobilized biocatalyst for efficient use. It has been claimed that the success of a lipase catalyzed biotransformation for the production of certain pharmaceuticals depends on immobilization. For example, in the industrial preparation of the chiral intermediate used in the synthesis of Diltiazem, the lipase from Serratia marcescens was supported in a spongy matrix, which was used in a two-phase membrane bioreactor (Cowan 1996). 

The properties of supported enzyme preparations are governed by the properties of both the enzyme and the carrier material. The interaction between the two provides an immobilized enzyme with specific chemical, biochemical, mechanical and kinetic properties. The support (carrier) can be a synthetic organic polymer, a biopolymer or an inorganic solid. Enzyme-immobilized polymer membranes are prepared by methods similar to those for the immobilized enzyme, which are summarized in Fig. 22.7 (a) molecular recognition and physical adsorption of biocatalyst on a support membrane, (b) cross-linking between enzymes on (a), (c) covalent binding between the biocatalyst and the membrane, (d) ion complex formation between the biocatalyst and the membrane, (e) entrapment of the biocatalyst in a polymer gel membrane, (f) entrapment and adsorption of biocatalyst in the membrane, (g) entrapment and covalent binding between the biocatalyst and the membrane, (h) entrapment and ion complex formation between the biocatalyst and the membrane, (i) entrapment of the biocatalyst in a pore of an UF membrane, (j) entrapment of the biocatalyst in a hollow-fiber membrane, (k) entrapment of biocatalyst in microcapsule, and (1) entrapment of the biocatalyst in a liposome. 

In Part I a selection of the types of membrane reactor is presented, together with chapters on the integration of membrane reactors with current industrial processes. To summarize, in Chapter 1 (Calabro) membrane bioreactors are described from an engineering point of view, together with a straightforward description and simulation, with a simple mathematical approach, of the most important configurations and processes in which they are involved. Basic principles of bioconversion, bioreactors and biocatalysis with immobilized biocatalysts are also presented. For all the cited systems the most significant parameters are defined in order to estimate their performances. The best approaches for the preparation of... 

Many enzyme immobilization techniques developed in connection with the preparation of heterogeneous biocatalysts have been applied for the construction of enzyme electrodes as well as for other types of biosensors. The immobilization of enzymes or other biocomponents on different membranes is most frequently realized by crosslinking agents, first of all by glutaraldehyde, and with the addition of bovine serum albumin [169] or other proteins, with l,8-diamino-4-aminomethyloc-tane, [170], etc. 

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