Cross-linked enzyme aggregates application

Immobilized enzymes, particularly LAC, have been employed in the degradation of triclosan. The immobilization of LAC from Coriolopsis polyzona through the formation of cross-linked enzyme aggregates (CLEAs) and their subsequent use in an FBR for the removal of endocrine disrupting compounds [42] produced the complete removal of triclosan, nonylphenol, and bisphenol A (5 mg L-1 each) at a HRT of 150 min. The application of CLEAs in a perfusion basket reactor [43]... 

Litthauer D, Ginster A, Skein EVE (2002) Pseudomonas luteola hpase a new member of the 320-residue Pseudomonas lipase family. Enzyme Microb Technol 30 209-215 Lopez-Serrano P, Cao L, van Rantwijk F et al. (2002) Cross-linked enzyme aggregates with enhanced activity application to lipases. Biotechnol Lett 24 1379-1383 Lorenz P, Liebeton K, Niehaus (2002) Screening for novel enzymes for biocatalytic processes accessing the metagenome as a resource of novel functional sequence space. Curr Opin Biotechnol 13 572-577... 

Cross-linked enzyme aggregates (CLEAs) rely on chemical cross-linking to form a self-assembled enzyme matrix that can be fabricated into, or onto, an electrode material. CLEAs find application in EECs, particularly anodic catalysts [65]. GOx, for example, can be cross-linked in the presence of ammonium sulfate onto the surface of various nanomaterials. The aggregation of the enzyme results in a substantial increase in volumetric protein loading and enhanced stability (>200 days). The use of GOx as CLEA was used as the anode of a biological fiiel cell and demonstrated reproducible power density and stability up to 50 "C. 

Rev. 42 (2013) 6213-6222. (d) L. Cao, F.v. Rantwijk, R.A. Sheldon, Cross-linked enzyme aggregates a simple and effective method for the immobilization of penicillin acylase, Org. Lett. 2 (2000) 1361-1364. (e) T. Matsuda, K. Nakayama, T. Abe, M. Mukouyama, Stabilization of pyruvate decarboxylase under pressurized carbon dioxide and water biphasic system, Biocatal. Bio-trans. 28 (2010) 167-171. (f)T. Matsuda, R. Marukado, M. Mukouyama, . Harada, K. Nakamura, Asymmetric reduction of ketones by Geotrichum candidum immobilization and application to reactions using supercritical carbon dioxide. Tetrahedron Asymm. 19 (2008) 2272-2275. 

Entrapment of enzymes and cells has played an important role in developing bioprocesses. Applications of entrapment technology to biosensors and bioanalysis have mainly been focused on udlizadon of cells and, to a smaller extent, on enzymes (24). Combining covalent coupling and entrapment cross-links enzymes and inert protein to form a protein membrane that covers the sensitive part of the electrode dp in bioanalytical applications (25). Entrapping enzyme aggregates is another variadon of this methodology (26). 

Enzymatic modification of proteins applicable to foods is reviewed by Whitaker ( ). Described briefly are present uses of proteolytic enzymes for modifying proteins through partial hydrolysis. Major emphasis is placed on those enzymes which bring about aggregation of proteins, cross-link formation, and side chain modification through post-translational changes in the polypeptide chain. 

Many applications rely on enzymes being retained by membranes, aggregated by cross-linking, or immobilized by encapsulation. These techniques are often simple and inexpensive, but typically also generate a poorly defined immobilized enzyme. The immobilization can involve isolated enzymes or whole cell preparations. Sweetzyme IT, an immobilized glucose isomerase produced by Novozymes is an example of the latter, in which the cells are cross-linked by glutaraldehyde (GA) and extruded to produce dry, solid particles [32]. 

---