Cellulase immobilized on copolymers based on N-vinylformamide: Influence of immobilization on the catalytic activity of the enzyme
Katarzyna SOKOŁOWSKA – Faculty of Chemistry, Jagiellonian University, Kraków, Poland; Anna KONIECZNA–MOLENDA – Institute of Chemistry and Physics, University of Agriculture, Kraków, Poland; Ewa WITEK* – Faculty of Chemistry, Jagiellonian University, Kraków, Poland

Please cite as: CHEMIK 2015, 69, 8, 447–454

Cellulolytic enzymes play an important role in many advanced
technologies, in various industries. They are used, among others, in
the textile industry, food, pharmaceutical, and pulp and paper [1].
Perceiving the great potential of cellulosic biomass as a renewable
energy source, which allows to reduce carbon dioxide emissions, and
thus prevent global warming, has contributed to a broad examination of
the enzymatic hydrolysis of cellulose [2 – 9]. The hydrolysis of cellulose
to reducing sugars requires complex enzymatic system, consisting
of the endoglucanase (EC 3.2.1.4), cellobiohydrolase (EC 3.2.1.91)
and β-glucosidase (EC 3.2.1.21). During the process, endoglucanase
and cellobiohydrolase first degrade crystalline cellulose to soluble
cellodextrins and amorphous cellulose, which are hydrolyzed to the
reducing sugars by β-glucosidase [10]. Unfortunately, the unstable nature
of most enzymes, the high cost of isolation and difficulty in recovery
of cellulases leads to their limited use in the energy industry [11]. One
of the effective solutions can be cellulolytic enzyme immobilization,
which allows to increase their stability and reusability, and above all,
reduce the cost of their practical application [12]. Because of the great
advantages, for many years, the possibility of wider use of immobilized
cellulase in technological and biotechnological processes are sought
[13, 14]. At present, immobilization of enzymes can also increase their
selectivity, specificity and resistance to inhibitors and other chemical
and physical factors [15 – 17].

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