Enzyme immobilization onto renewable polymeric matrixes: Past, present, and future trends

Abstract

In this review, we present an overview of the different renewable polymers that are currently being used as matrixes for enzyme immobilization and their properties and of new developments in biocatalysts preparation and applications. Polymers obtained from renewable resources have attracted much attention in recent years because they are environmentally friendly and available in large quantities from natural sources. Different methods for the immobilization of enzymes with these matrixes are reviewed, in particular: (1) binding to a prefabricated biopolymer, (2) entrapment, and (3) crosslinking of enzyme molecules. Emphasis is given to relatively recent developments, such as the use of novel supports, novel entrapment methods and protocols of polymer derivatization, and the crosslinking of enzymes.

Polymer supports for the removal and degradation of hazardous organic pollutants: an overview

“…This type of immobilization is mainly carried out with biopolymers – such as chitosan, cellulose, alginate/agarose, carrageenan, collagen and sugar agar – probably because of the ability of these compounds to generate gels and different geometric configurations, the ease of implementation of the method, and the biodegradability of the resulting material . Among the advantages of entrapment are its low cost of implementation, the decrease in the leaching of enzymes because the networks only allow the passage of substrates and products, and the structure of the enzyme remaining unmodified so that the catalytic activity is maintained . In addition, since there is no direct interaction of the enzyme with the environment, the inhibition problems due to bubbles, organic solvents or denaturing agents in the medium are also reduced .…”

“…For that reason, when performing enzymatic immobilization, the selection of the method of immobilization is probably the most significant aspect since it will determine both the catalytic properties (activity, selectivity, stability) and the non‐catalytic properties (physical and chemical characteristics) in the system of immobilized enzymes . It is important to note that, in all cases, the selection of a suitable support and the immobilization protocols must be carefully established since the structural changes produced in the enzymes after immobilization can cause total or partial loss of activity in the immobilized enzyme . In this context, several factors must be considered in the selection of the method of immobilization such as the intended final use, the enzyme used and the characteristics desired in the immobilized enzyme system (reusability, cost of the immobilization procedure, stability, operational stability and ease of synthesis) …”

“…The use of biopolymers for immobilization has multiple benefits since they are eco‐friendlier, less toxic and better preserve the activity of the immobilized enzyme. Some of the most used biopolymers include chitosan, collagen, starch, cellulose, pectin and carrageenan . Additionally, the use of some biopolymers is economically profitable because they are sometimes byproducts of some process and, like synthetic polymers, can be modified to have different physical properties.…”

Moving towards a Competitive Fully Enzymatic Biodiesel Process

“…In general, immobilization allows reuse of the biocatalyst, makes the product recovery easier, and frequently enhances enzyme resistance against inactivation by different denaturants, providing more stable and efficient catalysts [41,42]. Nevertheless, many immobilization procedures use sophisticated protocols for lipase entrapment on expensive supports [43], not always suitable for a real scaling-up, and causing an increase in the costs of industrial processes [44,45].…”

Estabilização De Lecitase Ultra Por Imobilização Em Suporte Macroporoso

“…Diante da grande disponibilidade de suportes para imobilização enzimática, os macroporosos se destacam por permitir a imobilização de uma grande quantidade de enzimas, mantendo-as completamente dispersas e impossibilitadas de interagir com qualquer interface externa, estabilizando, assim, a proteína imobilizada e prevenindo a agregação, autólise ou até mesmo proteólise por proteases do extrato (que podem também estar dispersas e imobilizadas) (BEZERRA et al, 2015).…”