Principles, techniques, and applications of biocatalyst immobilization for industrial application

Abstract

Immobilization is one of the most effective and powerful tools used in industry, which has been studied and improved since the last century. Various immobilization techniques and support materials have been used on both laboratory and industrial scale. Each immobilization technique is applicable for a specific production mostly depending on the cost and sensibility of process. Compared to free biocatalyst systems, immobilization techniques often offer better stability, increased activity and selectivity, higher resistance, improved separation and purification, reuse of enzymes, and consequently more efficient process. Recently, many reviews have been published about immobilization systems; however, most of them have focused on a specific application or not emphasized in details. This review focuses on most commonly used techniques in industry with many recent applications including using bioreactor systems for industrial production. It is also aimed to emphasize the advantages and disadvantages of the immobilization techniques and how these systems improve process productivity compared to non-immobilized systems.

Nano-Immobilized Biocatalysts for Biodiesel Production from Renewable and Sustainable Resources

“…It is based on a physical binding mechanism, such as a dipole-dipole, hydrophobic, or van der Waals interaction or hydrogen bonding [18,22]. Physical binding was performed in relatively ambient conditions and showed a high enzyme loading [16,22].…”

“…It is based on a physical binding mechanism, such as a dipole-dipole, hydrophobic, or van der Waals interaction or hydrogen bonding [18,22]. Physical binding was performed in relatively ambient conditions and showed a high enzyme loading [16,22]. Adsorption immobilization does not provide a high stability and might cause a loss of enzyme molecules during operation and washing because of weak binding between the enzyme and the supports [23].…”

“…The strong binding of enzyme to the support matrix via the covalent bond prevents enzyme leaching from the surface and improves the thermal stability in some cases [18,22]. This technique, however, often provokes the deactivation of enzyme because of the conformational restriction of the enzyme by covalent binding [22,26]. Hong et al [26] immobilized α-chymotrypsin on an amine-functionalized superparamagnetic nanogel by covalent binding and compared the stability of the immobilized enzyme and free enzyme.…”

“…The SENs of HPR showed similar Michaelis-Menten parameters (K m and K cat ), but the thermal stability of the SENs was enhanced up to 65 • C. Moreover, the enzyme activity was maintained in the presence of polar organic solvents, such as methanol, tetrahydrofuram, and dioxane. The enzyme immobilization techniques are summarized in Figure 1 [18,22]. (from Pseudomonas cepacia) and nanostructured magnetite (Fe3O4) containing hydrophobic sol-gel material.…”

A Microfluidic Toolbox for the Development of In-Situ Product Removal Strategies in Biocatalysis

“…The listed unit operations give a good indication of different microfluidic separation modules that are required in a microfluidic toolbox to quickly assess and test various ISPR options. In terms of separating and recycling of the biocatalyst, if required, size differences are often exploited, i.e., filtration or membrane-based separation [32,33]. There are of course also more complex examples where a combination of several differences in physicochemical properties is exploited to separate compounds from complex reaction mixtures [34].…”