Although many methods for enzyme immobilization have been described in patents and publications, relatively few processes employing immobilized enzymes have been successfully commercialized. The cost of most industrial enzymes is often only a minor component in overall process economics, and in these instances, the additional costs associated with enzyme immobilization are often not justified. More commonly the benefit realized from enzyme immobilization relates to the process advantages that an immobilized catalyst offers, for example, enabling continuous production, improved stability and the absence of the biocatalyst in the product stream. The development and attributes of several established and emerging industrial applications for immobilized enzymes, including high-fructose corn syrup production, pectin hydrolysis, debittering of fruit juices, interesterification of food fats and oils, biodiesel production, and carbon dioxide capture are reviewed herein, highlighting factors that define the advantages of enzyme immobilization.

Industrial use of immobilized enzymes

Polymeric materials, natural and unnatural, are indispensable to the modern society. They are widely used from everyday life usages as commodity materials to industry and technology usages in the fields such as electronics, machinery, communications, transportations, pharmacy, and medicine as highly advanced materials. Today, it is hard to think of the present society without polymeric materials. Developments of various polymeric materials have been owed to epoch-making innovative works as exemplified typically by the discovery of Ziegler-Natta catalyst,1-3 the concept of living polymerization,4 the discovery of conducting polymers,5 and the discovery of metathesis catalyst.6,7 These observations demonstrate that new polymeric materials are often brought about by new production methods including polymerization catalysts. Historically, polymerization catalysts utilized classical catalysts of acids (Brønsted acids, Lewis acids, and various cations), bases (Lewis bases and various anions), and radical generating compounds since the 1920s, the early stage of polymer chemistry. In the following * To whom correspondence should be addressed. Fax/Tel: (+81)-75-7247688. E-mail: kobayash@kit.ac.jp. † Kyoto Institute of Technology and Emeritus Professor of Kyoto University. ‡ Kyoto University. Chem. Rev. 2009, 109, 5288–5353 5288

Enzymatic polymer synthesis: an opportunity for green polymer chemistry.

The present article comprehensively reviews the macromolecular synthesis using enzymes as catalysts. Among the six main classes of enzymes, the three classes, oxidoreductases, transferases, and hydrolases, have been employed as catalysts for the in vitro macromolecular synthesis and modification reactions. Appropriate design of reaction including monomer and enzyme catalyst produces macromolecules with precisely controlled structure, similarly as in vivo enzymatic reactions. The reaction controls the product structure with respect to substrate selectivity, chemo-selectivity, regio-selectivity, stereoselectivity, and choro-selectivity. Oxidoreductases catalyze various oxidation polymerizations of aromatic compounds as well as vinyl polymerizations. Transferases are effective catalysts for producing polysaccharide having a variety of structure and polyesters. Hydrolases catalyzing the bond-cleaving of macromolecules in vivo, catalyze the reverse reaction for bond forming in vitro to give various polysacchar...

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

Synthesis of biodegradable polymers from renewable resources

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions.

https://homepages.rpi.edu/~grossr/_doc/Biomacromolecules_2008_9_463.pdf

Elizabeth M. Miller

Papers

Candida antarctica lipase B chemically immobilized on epoxy-activated micro- and nanobeads: catalysts for polyester synthesis.