Immobilization of a thermostable, fungal recombinant chitinase on biocompatible chitosan beads and the properties of the immobilized enzyme. (26th July 2015)

• Record Type: Journal Article
• Authors: Prasad, Muthu; Palanivelu, Peramachi
• Is Part Of: Biotechnology and applied biochemistry. Volume 62:Number 4(2015)
• Page Start: 523
• Page End: 529
• Publication Date: 2015-07-26
• Subjects: Biotechnology -- Periodicals; Biochemical engineering -- Periodicals; Biochemistry -- Periodicals; Biochemistry -- Periodicals; Genetic Techniques -- Periodicals; Microbiological Techniques -- Periodicals; 660.6
• DOI: 10.1002/bab.1283
• Languages: English
• ISSNs: 0885-4513

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>A recombinant, thermostable fungal chitinase from the thermophilic fungus, <italic>Thermomyces lanuginosus</italic>, was immobilized on glutaraldehyde cross‐linked chitosan beads, and the properties of the immobilized chitinase were studied. The enzyme was found to be almost completely immobilized in 6 H under shaking condition at 30 °C. The immobilized enzyme exhibited much wider pH optimum and was more stable at alkaline pH values as compared with the soluble enzyme. Both the forms of the enzyme were optimally active at 60 °C and stable at 50 °C for 3 H, and after 3 H, the activity of the soluble enzyme declined sharply, whereas the immobilized chitinase was stable up to 6 H without any significant loss in the activity. <italic>K</italic>_M and <italic>V</italic>_max values of the immobilized enzyme were 1.18 mM and 445.7 μmol/Min/mg of protein, respectively. The immobilized enzyme was stable at least for 1 month at 4 °C without any significant loss in the activity.</p> </abstract>