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

α-l-Rhamnosidase: A review

Production, purification, and characterization of the debittering enzyme naringinase.

Naringinase, an enzyme complex, is commercially attractive due to its potential usefulness in pharmaceutical and food industries. It is of particular interest in the biotransformation of steroids, antibiotics, and mainly of glycosides hydrolysis. Moreover, it can be used in citrus juices debittering and wine industries. Naringinase expresses activity on α-L-rhamnosidase and β-D-glucosidase. Many natural glycosides, including naringin, rutin, quercitrin, hesperidin, diosgene, and ter-phenyl glycosides, containing terminal α-rhamnose and β-glucose can act as substrates of naringinase. The sources, production, activity, biochemical properties, and substrate specificity of naringinase are reviewed, along with a description of the enzymatic deglycosylation systems and applications, concluding with the identification of areas which need further extensive studies.

Naringinases: occurrence, characteristics, and applications.

Optimization of process parameters for the production of naringinase by Aspergillus niger MTCC 1344

Immobilized naringinase can be converted to a preparation showing only rhamnosidase activity by treatment with 0.1M glycine-NaOH buffer, pH 12. A simple method is described to obtain pure prunin in high yield from naringin with the help of this immobilizate.

M. RoitNer

Papers

Preparation of prunin with the help of immobilized naringinase pretreated with alkaline buffer