Immobilization of catalase on chitosan and amino acid- modified chitosan beads

Figures & data

Figure 1. Schematic illustration for preparation of amino acid-modified chitosan beads and immobilization of enzymes (Yi et al. 2009).

Figure 2. Scanning electron micrographs of the surfaces of (A) chitosan bead, (B) lysine-modified chitosan bead, (C) alanine-modified chitosan bead, (D) catalase-immobilized chitosan bead, (E) catalase-immobilized Lys–CB, (F) catalase-immobilized Ala–CB.

Figure 3. FTIR spectra (A) and TGA curves (B) of chitosan and modified chitosan beads.

Table I. Kinetic parameters of free and immobilized catalases.

	Free catalase	Catalase immobilized on chitosan	Catalase immobilized on alanine-chitosan	Catalase immobilized on lysine-chitosan
Km (mM)	14.28	33.76	25.67	27.0
Vmax (μmol H2O2/min)	3076.92	141.92	201.39	197.50

Figure 4. pH (A) and temperature (B) stability of free and immobilized catalase at various pH and temperature after 60 min (

: free enzyme,

: chitosan,

: chitosan–alanine,

: chitosan–lysine).

Figure 5. Reusability of immobilized catalase on modified chitosan beads (

: lysine-modified chitosan beads,

: alanine-modified chitosan beads).

Yi S, Noh J, Lee Y. 2009. Amino acid modified chitosan beads: improved polymer supports for immobilization of lipase from Candida rugosa. J Mol Catal B Enzym. 57:123–129.

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